sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

smiles: CCC(N)=O

column_label: Table 1. Kinetic properties of Sulfolobus solfataricus amidase. The turnover number (kcat) was obtained dividing by the molecular mass of the active monomer (55,784 Da); temperature was 70 C; in 50 mM citrate buffer at pH 5.0. Wild-type non-bold line of the substrate block 'Propionamide'; column 'Km (mM)' = 10.0; column 'kcat (sec-1)' = 82.9; column 'kcat/Km (M^-1 sec^-1) x 10^2' = 82.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 10.0 mM; already in mM, no conversion; the exported value is 10.0 mM. kcat: printed Table 1 cell 82.9 sec-1; 1 sec-1 is 1 s^(-1), so the printed cell is 82.9 s^(-1); the exported value is 82.9. kcat/Km: printed Table 1 cell 82.9 in the column headed kcat/Km (M^-1 sec^-1) x 10^2, that is 8290 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 mM^-1 s^-1, so the printed cell is 8.29 s^(-1)*mM^(-1); the exported value is 8.29.

raw_value_unit_evidence: Table 1, wild-type non-bold line of the substrate block 'Propionamide': Km = 10.0 mM; kcat = 82.9 sec-1; printed kcat/Km = 82.9 in the column unit 10^2 M^-1 sec^-1, that is 8290 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription (section 2), wild-type non-bold line of the substrate block 'Propionamide'


enzyme_display_name: amidase

organism: Saccharolobus solfataricus

substrate_name: hexanamide

source_db: oed

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y41C to reconstruct the assayed variant sequence.

smiles: CCCCCC(=N)O

mutation_type: substitution

assay_conditions_summary: pH 5; 343.15 K; buffer 50 mM citrate buffer

data_origin: experimental

enzyme: amidase

substrate: hexanamide

source: oed


substrate_name: Pentanamide

smiles: CCCCC(=N)O

substrate: Pentanamide


substrate_name: acetamide

verification_status: verified

mutation_signature: Unknown

smiles: CC(=N)O

column_label: Table 1. Kinetic properties of Sulfolobus solfataricus amidase. The turnover number (kcat) was obtained dividing by the molecular mass of the active monomer (55,784 Da); temperature was 70 C; in 50 mM citrate buffer at pH 5.0. Wild-type non-bold line of the substrate block 'Acetamide'; column 'Km (mM)' = 22.0; column 'kcat (sec-1)' = 28.9; column 'kcat/Km (M^-1 sec^-1) x 10^2' = 13.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 22.0 mM; already in mM, no conversion; the exported value is 22.0 mM. kcat: printed Table 1 cell 28.9 sec-1; 1 sec-1 is 1 s^(-1), so the printed cell is 28.9 s^(-1); the exported value is 28.9. kcat/Km: printed Table 1 cell 13.1 in the column headed kcat/Km (M^-1 sec^-1) x 10^2, that is 1310 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 mM^-1 s^-1, so the printed cell is 1.31 s^(-1)*mM^(-1); the exported value is 1.31.

raw_value_unit_evidence: Table 1, wild-type non-bold line of the substrate block 'Acetamide': Km = 22.0 mM; kcat = 28.9 sec-1; printed kcat/Km = 13.1 in the column unit 10^2 M^-1 sec^-1, that is 1310 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription (section 2), wild-type non-bold line of the substrate block 'Acetamide'

substrate: acetamide

status: verified


substrate_name: Isobutyramide

smiles: CC(C)C(=N)O

substrate: Isobutyramide


source_db: brenda

kcat_over_km_display: Not reported

proof_lines:
pH 5.0, 70°C, mutant enzyme Y41C
mutant enzyme Y41C

source: brenda


kcat_over_km_origin: calculated


substrate_name: butyramide

smiles: CCCC(=N)O

substrate: butyramide


substrate_name: metacrylamide

smiles: C=C(C)C(=N)O

assay_conditions_summary: pH 5; 343.15 K; buffer 50 mM citrate

column_label: Table 1. Kinetic properties of Sulfolobus solfataricus amidase. The turnover number (kcat) was obtained dividing by the molecular mass of the active monomer (55,784 Da); temperature was 70 C; in 50 mM citrate buffer at pH 5.0. Wild-type non-bold line of the substrate block 'Metacrylamide'; column 'Km (mM)' = 0.3; column 'kcat (sec-1)' = 4.8; column 'kcat/Km (M^-1 sec^-1) x 10^2' = 160.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.3 mM; already in mM, no conversion; the exported value is 0.3 mM. kcat: printed Table 1 cell 4.8 sec-1; 1 sec-1 is 1 s^(-1), so the printed cell is 4.8 s^(-1); the exported value is 4.8. kcat/Km: printed Table 1 cell 160.0 in the column headed kcat/Km (M^-1 sec^-1) x 10^2, that is 16000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 mM^-1 s^-1, so the printed cell is 16.0 s^(-1)*mM^(-1); the exported value is 16.0.

raw_value_unit_evidence: Table 1, wild-type non-bold line of the substrate block 'Metacrylamide': Km = 0.3 mM; kcat = 4.8 sec-1; printed kcat/Km = 160.0 in the column unit 10^2 M^-1 sec^-1, that is 16000 M^-1 s^-1.

row_label: Table 1, decoded plain-numeral transcription (section 2), wild-type non-bold line of the substrate block 'Metacrylamide'

substrate: metacrylamide


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB P95896 direct REST/FASTA lookup and applied mutation signature Y41C to reconstruct the assayed variant sequence.

status: unverified


substrate_name: nicotinamide

sequence_source: UniProtKB P95896 direct REST/FASTA lookup

substrate: nicotinamide


substrate_name: Benzamide

substrate: Benzamide


substrate_name: Propionamide

substrate: Propionamide


substrate_name: 4-nitrobenzamide; 2-toluamide; indol-3-acetamide; 3-phenylpropionamide; metacrylamide; 4-hydroxybenzamide; 4-toluamide; acetamide; Benzamide; nicotinamide; Propionamide; Isobutyramide

sequence_source: UniProtKB:P95896 direct REST check; active reviewed AMID_SACS2 amidase entry with EC 3.5.1.4

proof_lines: 85°C, pH not specified in the publication, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB:P95896 direct REST check plus direct Y41C reconstruction from canonical sequence and applied mutation signature Y41C to reconstruct the assayed variant sequence.


organism: Starkeya sp. YW6

substrate_name: 2-chloro-N-(2-methyl-6-ethylphenyl)acetamide; propanil; 2-chloro-N-(2,6-diethylphenyl)acetamide; propham; chlorpropham

sequence_source: UniProtKB:A0A142FJE8 direct REST check reported inactive/deleted; no sequence available

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


organism: Streptomyces sp.

sequence_source: UniProtKB:A0A088BHP3 direct REST check; active unreviewed A0A088BHP3_9ACTN sequence


substrate_name: Propionamide; nicotinamide; acetamide; 4-Guanidinobutyramide; Benzamide


smiles: NC(=O)CCCN=C(N)N


enzyme_display_name: ferredoxin--NADP(+) reductase

organism: Spinacia oleracea

substrate_name: reduced ferredoxin I

assay_conditions_summary: pH 7; 288.15 K; cofactor NADPH

proof_lines: pH 7.0, 15°C, wild-type leaf isozyme, diaphorase activity

enzyme: ferredoxin--NADP(+) reductase

substrate: reduced ferredoxin I


enzyme_display_name: pyruvate kinase

organism: Monoraphidium minutum

substrate_name: IDP

kcat_display: Not reported

assay_conditions_summary: cofactor ADP

proof_lines:
isozyme PKc
PKc-isozyme
isozyme PKp

enzyme: pyruvate kinase

substrate: IDP


organism: Unknown

substrate_name: reduced ferredoxin

km_display: Not reported

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

substrate: reduced ferredoxin


organism: Rhodococcus sp. N-771

sequence_source: UniProtKB:Q7DKE4 canonical sequence from direct UniProt REST lookup


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

source: skid


sequence_source: UniProtKB:P95896 canonical sequence from direct UniProt REST lookup


substrate_name: Acrylamide

smiles: C=CC(=N)O

substrate: Acrylamide


substrate_name: L-prolinamide

substrate: L-prolinamide


substrate_name: Isonicotinamide

substrate: Isonicotinamide


substrate_name: cyclohexanamide

substrate: cyclohexanamide


organism: Ricinus communis

substrate_name: ADP; Phosphoenolpyruvate

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines: 2 isozymes with different kinetic mechanisms

substrate: ADP; Phosphoenolpyruvate


organism: Pyrococcus yayanosii

substrate_name: hexanamide

sequence_source: UniProtKB:F8AEP0 direct accession check

substrate: hexanamide


substrate_name: L-glutamine

substrate: L-glutamine


organism: Rhodococcus erythropolis

substrate_name: acetamide

substrate: acetamide


sequence_source: UniProtKB:Q7DKE4 direct accession check; RCSB 3A1K/3A1I SIFTS mapping

proof_lines: pH 5.9, 55°C, recombinant wild-type enzyme


assay_conditions_summary: pH 7.1; 298.15 K; cofactor ADP

proof_lines:
isozyme PKII, pH 7.1, 25°C
isozyme PKI, pH 7.1, 25°C
pH 7.1, 25°C


enzyme_display_name: trypsin

organism: Homo sapiens

substrate_name: H2O; Glu-Gly-Arg-p-nitroanilide

assay_conditions_summary: pH 7.4; 310.15 K; buffer 10 mM phosphate

proof_lines: in 10 mM Tris, 20 mM CaCl2, pH 7.4, at 37°C

proof_lines: pH 8.0, 37°C, uncleaved enzyme, nonsulfated

proof_lines: pH 8.0, 37°C, uncleaved enzyme, sulfated

enzyme: trypsin

substrate: H2O; Glu-Gly-Arg-p-nitroanilide


organism: Oncorhynchus keta

substrate_name: benzoyl-L-arginine-p-nitroanilide

proof_lines:
isozyme ST-1, at 15°C
isozyme ST-1, at 25°C
isozyme ST-3, at 5°C

substrate: benzoyl-L-arginine-p-nitroanilide


organism: Euphausia pacifica

proof_lines:
isozyme TLE I, at 37°C, pH 8.0
isozyme TLE II, at 37°C, pH 8.0


organism: Engraulis japonicus

substrate_name: benzoyl-Arg 4-nitroanilide

proof_lines:
pH 8.0, 25°C, isoenzyme aT-I
pH 8.0, 25°C, isoenzyme aT-II

substrate: benzoyl-Arg 4-nitroanilide


organism: Sardinella aurita

proof_lines:
isozyme trypsin C, pH 9.0, 25°C
isozyme trypsin B, pH 9.0, 25°C
isozyme trypsin A, pH 9.0, 25°C


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: ADP

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ADP

proof_lines:
enzyme form I
30°C, pH 6.8
isozyme II, 30°C, pH 6.8

substrate: ADP


substrate_name: Propionamide

sequence_source: UniProtKB:A0A088BHP3 direct REST/FASTA lookup; sequenceVersion 1


organism: Rhodococcus rhodochrous strain J1

substrate_name: Benzamide

sequence_source: UniProtKB Q9ZBD4 and NCBI Protein BAA03744.1, linked from PMID 7916690

column_label: Page 1 abstract and page 2 Enzyme assay; row/segment Rhodococcus rhodochrous J1 amidase, benzamide; metric/detail benzamide Km; raw 0.15 mM; normalized 0.15 mM.

raw_value_unit_evidence: Page 1 abstract and page 2 Enzyme assay; Rhodococcus rhodochrous J1 amidase, benzamide; benzamide Km: 0.15 mM.

table_label: Page 1 abstract and page 2 Enzyme assay

substrate: Benzamide


organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ADP

proof_lines:
apparent value
pH 7.1, 37°C
R-type isozyme, pH 7.4, 37°C

substrate: Phosphoenolpyruvate; ADP


organism: Arabidopsis thaliana

substrate_name: Unknown

source_db: uniprot

substrate: Unknown

source: uniprot


organism: Oryza sativa subsp. japonica


substrate_name: Gly-para-nitroanilide

substrate: Gly-para-nitroanilide


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Sorangium cellulosum (strain So ce56)


organism: Spinacia oleracea


organism: Bacillus subtilis (strain 168)

substrate_name: NADPH (at 24 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7; cofactor NADPH


organism: Escherichia coli (strain K12)

proof_lines: kcat is 338.9 min(-1) with NADPH as the donor. kcat is 33 min(-1) with NADP as the donor (PubMed:11085917). kcat is 0.15 sec(-1) with ferredoxin as substrate. kcat is 0.0042 sec(-1) with flavodoxin 1 as substrate. kcat is 0.0039 sec(-1) wit


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ferricyanide (in the presence of NADPH)

proof_lines: kcat is 63.0 sec(-1) with ferricyanide and NADPH as substrates. kcat is 25.6 sec(-1) with 2,6-dichlorophenol-indophenol and NADPH as substrates. kcat is 42 sec(-1) with ferricyanide and NADH as substrates. kcat is 21 sec(-1) with 2,6-dichlo

substrate: ferricyanide (in the presence of NADPH)


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: NADPH (with benzyl viologen as cosubstrate at pH 9.5)


substrate: NADPH (with benzyl viologen as cosubstrate at pH 9.5)


organism: Rhodobacter capsulatus

substrate_name: NADPH (in the presence of K(3)Fe(CN)(6))

proof_lines: kcat is 222 sec(-1) with K(3)Fe(CN)(6) as substrate. kcat is 20 sec(-1) with 2,6-dichlorophenolindophenol as substrate.


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

substrate_name: NADPH (at 25 degrees Celsius)

assay_conditions_summary: cofactor NADP+

substrate: NADPH (at 25 degrees Celsius)


organism: Agarophyton chilense

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: enzyme in PBS, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication

proof_lines: enzyme in soluble extract, with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0, temperature not specified in the publication


organism: Anabaena cylindrica

proof_lines: NADPH-2,6-dichlorophenol indophenol diaphorase activity

proof_lines: ferredoxin-dependent cytochrome c reductase activity


organism: Anabaena sp.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: recombinant mutant E139D, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM

proof_lines: recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 28 mM

proof_lines: recombinant mutant E139D, pH 8.0, 25°C, ionic strength of 100 mM


proof_lines: recombinant wild-type enzyme, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM

proof_lines: recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 200 mM

proof_lines: recombinant wild-type enzyme, pH 8.0, 25°C, ionic strength of 100 mM


substrate_name: reduced flavodoxin

proof_lines: recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 200 mM

proof_lines: recombinant mutant E139K, pH 8.0, 25°C, ionic strength of 28 mM

proof_lines: recombinant mutant E139K, diaphorase activity with 2,6-dichlorophenolindophenol, pH 8.0, 25°C, ionic strength of 28 mM

substrate: reduced flavodoxin


substrate_name: reduced ferredoxin

proof_lines: recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 28 mM

proof_lines: recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 200 mM

proof_lines: recombinant mutant E139Q, pH 8.0, 25°C, ionic strength of 100 mM

substrate: reduced ferredoxin


organism: Bos taurus

substrate_name: ADP; Phosphoenolpyruvate

ki_unit: mM

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

proof_lines:
M-type isozyme, 25°C, pH 7.0
L-type isozyme, 25°C, pH 7.0

substrate: ADP; Phosphoenolpyruvate


substrate_name: reduced flavodoxin mutant I59A

proof_lines: using cytochrome c as electron acceptor, for mutant I59A

substrate: reduced flavodoxin mutant I59A


substrate_name: reduced flavodoxin mutant W57K

proof_lines: using cytochrome c as electron acceptor, for mutant W57K

substrate: reduced flavodoxin mutant W57K


substrate_name: reduced flavodoxin mutant I59E

proof_lines: using cytochrome c as electron acceptor, for mutant I59E

substrate: reduced flavodoxin mutant I59E


substrate_name: reduced flavodoxin mutant I92A

proof_lines: using cytochrome c as electron acceptor, for mutant I92A

substrate: reduced flavodoxin mutant I92A


organism: Azotobacter vinelandii


organism: Bacillus subtilis

substrate_name: NADH

assay_conditions_summary: pH 7; 297.15 K; cofactor NADPH

proof_lines: 2,6-dichlorophenolindophenol reduction, pH 7.0, 24°C

proof_lines: with ferricyanide as cosubstrate, at pH 7.0 and 25°C

substrate: NADH


organism: Equisetum arvense

substrate_name: reduced ferredoxin II

substrate: reduced ferredoxin II


proof_lines: ferredoxin mutant Q39R/S28E, pH 7.5, 25°C


organism: Escherichia coli

proof_lines: electron transfer via the enzyme to Fe(CN)63-


organism: Euglena gracilis

substrate_name: iodonitrotetrazolium violet

proof_lines: 4 different fractions after ferredoxin-Sepharose chromatography

substrate: iodonitrotetrazolium violet


organism: Lathyrus oleraceus


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, presence of Zn2+, 30°C, pH 8.0

proof_lines: mutant bearing an artificial metal binding site of nine amino acids at the C-terminus, absence of Zn2+, 30°C, pH 8.0


proof_lines:
wild-type, 30°C, pH 8.0
pH 8.0, 13°C, wild-type enzyme


organism: Leptospira interrogans

assay_conditions_summary: pH 8

proof_lines: pH 8.0, 25°, recombinant mutant LepFNR-Loop, Cytochrome c reductase activity with 2[4Fe-4S] ferredoxin

proof_lines: above, pH 8.0, 25°, recombinant mutant LepFNR-K, cytochrome c reductase activity with 2[4Fe-4S] ferredoxin

proof_lines: pH 8.0, 25°, recombinant mutant LepFNR-Loop-K, cytochrome c reductase activity with 2[4Fe-4S] ferredoxin


organism: Mucor rouxii

substrate_name: Phosphoenolpyruvate; ADP

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

substrate: Phosphoenolpyruvate; ADP


organism: Mus musculus


organism: Musa cavendishii

substrate_name: phosphoenolpyruvate

assay_conditions_summary: pH 6.9; 298.15 K; cofactor ADP

proof_lines: hyperbolic saturation kinetics, pH 6.9, 25°C

proof_lines: cosubstrate phosphoenolpyruvate, pH 7.5, 25°C

substrate: phosphoenolpyruvate


organism: Mustela vison


organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ADP

proof_lines:
native enzyme, at pH 7.4 and 37°C
recombinant enzyme, at pH 7.4 and 37°C


organism: Pelophylax ridibundus

substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


organism: Pigeon


organism: Plasmodium falciparum


organism: Rhodotorula toruloides


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6.2; 303.15 K; cofactor ATP


proof_lines: mutant enzyme T298A, activated be Tl+ and Mn2+


proof_lines: mutant enzyme T298S, activated be Tl+ and Mn2+


organism: Sus scrofa

substrate_name: NADPH

substrate: NADPH


organism: Synechocystis sp.

substrate_name: reduced ferricyanide

proof_lines:
at pH 8.7 and 22°C
at pH 7.5 and 22°C

substrate: reduced ferricyanide


organism: Toxoplasma gondii


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADPH

proof_lines: mutant lacking amino acids 81 to 118, pH 9.0, 25°C


assay_conditions_summary: pH 9; 298.15 K; cofactor NADPH

proof_lines:
wild-type, pH 9.0, 25°C
wild-type, pH 8.2, 25°C
wild-type


organism: Trichormus variabilis

proof_lines: NADPH cytochrome c reductase activity, flavodoxin

proof_lines: diaphorase activity, FNR-flavodoxin complex

proof_lines: NADPH-dichlorophenol indophenol diaphorase activity


organism: Triticum aestivum

substrate_name: Unknown

proof_lines: pH 8.7, temperature not specified in the publication

substrate: Unknown


proof_lines: wild-type, pH 7.5, temperature not specified in the publication


proof_lines: mutant bearing a lysine to glutamine mutation in the first lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication

proof_lines: mutant bearing lysine to glutamine mutations in the second and third lysine residues of the KISKK domain, pH 7.5, temperature not specified in the publication

proof_lines: mutant bearing a lysine to glutamine mutation in the second lysine residue of the KISKK domain, pH 7.5, temperature not specified in the publication


mutation_type: truncation

proof_lines: mutant bearing a truncated N-terminal domain beginning after the KISKK domain, pH 7.5, temperature not specified in the publication


organism: Xanthomonas citri pv. citri

proof_lines: with oxidized 2,6-dichlorophenolindophenol as cosubstrate, at pH 8.0 and 25°C


organism: Zea mays

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines:
K3Fe(CN)6 as electron acceptor
at pH 7.5 and 30°C
at pH 7.5 and 20°C


organism: Cynodon dactylon


organism: Entamoeba histolytica


organism: Entodinium sp.


organism: Geobacillus stearothermophilus

assay_conditions_summary: pH 7.2; 303.15 K; buffer 50 mM imidazole-HCl; cofactor NADH

proof_lines: wild type enzyme, in the presence of 0.1 mM ribose 5-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30°C


proof_lines: mutant enzyme C9S/C268S, in the presence of 0.1 mM ribose 5-phosphate, in 50 mM imidazole-HCl buffer, pH 7.2, 50 mM KCl, 7 mM MgCl2, 0.12 mM NADH, 0.02 mg/ml lactate dehydrogenase, 2 mM PEP, and 4 mM ADP, at 30°C


organism: Homo sapiens

assay_conditions_summary: pH 6; 298.15 K; cofactor ADP

proof_lines: wild type enzyme, in the presence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C

proof_lines: wild type enzyme, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°Cin 50 mM Mes-Tris, pH 6.0, at 25°C


proof_lines: mutant enzyme E117K, in the absence of K+, in 50 mM Mes-Tris, pH 6.0, at 25°C


proof_lines: in the presence of D-fructose 1,6-bisphosphate


organism: Lactococcus lactis

substrate_name: GDP

substrate: GDP


organism: Lactococcus lactis subsp. lactis

substrate_name: Pyruvate; ATP

assay_conditions_summary: cofactor ATP

substrate: Pyruvate; ATP


organism: Lethenteron camtschaticum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ADP


organism: Meganyctiphanes norvegica

assay_conditions_summary: pH 7

proof_lines:
15°, pH 7.0, isoform PK I, in winter
15°, pH 7.0, isoform PK II, in winter
15°, pH 7.0, isoform PK II, in summer


enzyme_display_name: acetolactate synthase

organism: Alopecurus aequalis

substrate_name: pyruvate

sequence_source: UniProtKB:A0A1Q2U746 direct REST lookup 2026-06-15

enzyme: acetolactate synthase

substrate: pyruvate


organism: Amaranthus palmeri

sequence_source: UniProtKB:A0A221C9A2 direct REST lookup 2026-06-15

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A221C9A2 direct REST lookup 2026-06-15 and applied mutation signature A282D to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from UniProtKB:P17597 direct REST lookup 2026-06-15 and applied mutation signature P197L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P17597 direct REST lookup 2026-06-15


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17597 direct REST lookup 2026-06-15 and applied mutation signature P197T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17597 direct REST lookup 2026-06-15 and applied mutation signature W574L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17597 direct REST lookup 2026-06-15 and applied mutation signature S653T to reconstruct the assayed variant sequence.


substrate_name: Pyruvate

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant GH50(csr1-1)

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant GH90(csr1-2)

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant Tzp5(csr1-3)

substrate: Pyruvate


proof_lines: IC50 above 1.0 mM, pH and temperature not specified in the publication


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q04789 direct REST lookup 2026-06-15 and applied mutation signature Q487S to reconstruct the assayed variant sequence.

smiles: CC(=O)C(=O)O


organism: Anabaena sp.

assay_conditions_summary: cofactor NADPH

proof_lines: electron transfer via the enzyme to oxidized ferredoxin and further to cytochrome c

proof_lines: electron transfer via the enzyme to K3Fe(CN)6


substrate_name: reduced flavodoxin mutant W57R

proof_lines: using cytochrome c as electron acceptor, for mutant W57R

substrate: reduced flavodoxin mutant W57R


substrate_name: reduced flavodoxin mutant W57E

proof_lines: using cytochrome c as electron acceptor, for mutant W57E

substrate: reduced flavodoxin mutant W57E


substrate_name: reduced flavodoxin mutant I59E/I92E

proof_lines: using cytochrome c as electron acceptor, for mutant I59E/I92E

substrate: reduced flavodoxin mutant I59E/I92E


substrate_name: reduced flavodoxin mutant I92E

proof_lines: using cytochrome c as electron acceptor, for mutant I92E

substrate: reduced flavodoxin mutant I92E


substrate_name: reduced flavodoxin mutant I59A/I92A

proof_lines: using cytochrome c as electron acceptor, for mutant I59A/I92A

substrate: reduced flavodoxin mutant I59A/I92A


organism: Brucella ovis

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


organism: Chlamydomonas reinhardtii

substrate_name: reduced ferredoxin

proof_lines:
native enzyme, pH 8.0, 30°C
recombinant enzyme, pH 8.0, 30°C

substrate: reduced ferredoxin


organism: Cryptosporidium parvum

proof_lines: pH 7.4, temperature not specified in the publication, recombinant enzyme

proof_lines: pH 8.2, temperature not specified in the publication, recombinant enzyme

proof_lines: pH 6.8, temperature not specified in the publication, recombinant enzyme


organism: Equisetum arvense

substrate_name: reduced ferredoxin II

substrate: reduced ferredoxin II


substrate_name: oxidized ferredoxin II mutant D64N

substrate: oxidized ferredoxin II mutant D64N


organism: Archaeoglobus fulgidus

assay_conditions_summary: 323.15 K; cofactor ADP

proof_lines: 50°C, pH not specified in the publication


organism: Bacillus licheniformis

substrate_name: phosphoenolpyruvate

assay_conditions_summary: pH 7.1; 303.15 K; cofactor ADP

proof_lines: pH 7.1, 30°C, in the presence of Mg2+, 7fold lower in the presence of Mn2+

substrate: phosphoenolpyruvate


organism: Brassica juncea

substrate_name: ADP

assay_conditions_summary: pH 7; 298.15 K; cofactor ADP

substrate: ADP


organism: Brassica napus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 6.8; 297.15 K; cofactor ADP

substrate: Phosphoenolpyruvate; ADP


organism: Brassica rapa subsp. oleifera

assay_conditions_summary: pH 6.8; 303.15 K; cofactor ADP


organism: Busycotypus canaliculatum

assay_conditions_summary: pH 7; 293.15 K; cofactor ADP

proof_lines: in the absence of fructose 1,6-diphosphate


organism: Canis familiaris

substrate_name: ADP; Phosphoenolpyruvate

assay_conditions_summary: cofactor ADP

substrate: ADP; Phosphoenolpyruvate


organism: Cicer arietinum


organism: Columba livia


organism: Coprinopsis lagopus


organism: Cupriavidus necator


organism: Enterococcus faecalis

sequence_source: UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record.

assay_conditions_summary: pH 6.8; 310.15 K; cofactor FAD

proof_lines:
at pH 6.8 and 37°C
pH 6.8, 37°C, recombinant enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature H111R to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant H111R
mutant enzyme H111R, at pH 6.8 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature Q112N to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant Q112N
mutant enzyme Q112N, at pH 6.8 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature Q112E to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant Q112E
mutant enzyme Q112E, at pH 6.8 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature Q411N to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant Q411N
mutant enzyme Q411N, at pH 6.8 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature Q411E to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant Q411E
mutant enzyme Q411E, at pH 6.8 and 37°C


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature Q112V to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant Q112V
mutant enzyme Q112V, at pH 6.8 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q836A5 direct REST check; source accession from BRENDA selected record. and applied mutation signature H111F to reconstruct the assayed variant sequence.

proof_lines:
pH 7.5, 37°C, recombinant mutant H111F
mutant enzyme H111F, at pH 6.8 and 37°C


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature R276F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII R276F


sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature R276M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII R276M


sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature M250A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII M250A

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant His-Met250Ala


sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature R276Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII R276Q


substrate_name: Benzaldehyde; Pyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature W464Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII W464Q

substrate: Benzaldehyde; Pyruvate


sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature W464L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII W464L

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant His-Trp464Leu


sequence_variant_note: Resolved canonical sequence from UniProtKB P0DP90 direct REST check; source SABIO-RK accession bundle also lists P0ADG1 small subunit. and applied mutation signature W464A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII W464A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature F109L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII F109L


substrate_name: Pyruvate; Benzaldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature R276M to reconstruct the assayed variant sequence.

substrate: Pyruvate; Benzaldehyde


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature W464Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature W464L to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature F109W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII F109W


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature R276K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII R276K

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant His-Arg276Lys


sequence_source: UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature F109M to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII F109M


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature M250A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature R276F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature W464A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature R276Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for P0DP90 on 2026-06-15; single substitution reconstructed from selected SABIO-RK mutation signature. and applied mutation signature W464Y to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant AHASII W464Y


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0DP90 direct accession lookup with row-specific W464Y reconstruction and applied mutation signature W464Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0DP90 direct accession lookup with row-specific F109W reconstruction and applied mutation signature F109W to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant His-WT


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant I393A


proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant I393V


proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant L478A


proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant V51D/I393A


proof_lines: SABIO-RK modifier species: acetolactate synthase(Enzyme) mutant I479V


organism: Bacillus subtilis

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature Q487A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature Q487G to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature Q487S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q04789 FASTA direct accession lookup.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature I398V/A402Y/T480S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature T480S with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


proof_lines:
wild-type, pH 6,0, 30°C
wild-type, pH 7.0, 37°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature A402Y/T480S with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature A402Y with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q04789 canonical sequence by applying the selected row mutation signature. and applied mutation signature I398V with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q836A5 FASTA direct accession lookup.


organism: Oryza sativa Japonica Group

sequence_variant_note: Resolved canonical sequence from UniProtKB Q6K2E8 REST JSON and FASTA retrieved 2026-06-15 and applied mutation signature ΔW548 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: mutant DELTAW548, presence of chlorimuron-methyl, pH 7.5, 37°C

proof_lines: mutant DELTAW548, presence of rimsulfuron, pH 7.5, 37°C

proof_lines: mutant DELTAW548, presence of flucarbazone-sodium, pH 7.5, 37°C


sequence_source: UniProtKB Q6K2E8 REST JSON and FASTA retrieved 2026-06-15


organism: Pseudomonas sp.

sequence_source: UniProtKB G0ZSE6 REST JSON and FASTA retrieved 2026-06-15


organism: Saccharomyces cerevisiae

substrate_name: Unknown

sequence_source: UniProtKB P07342 REST JSON and FASTA retrieved 2026-06-15

substrate: Unknown


organism: Thermotoga maritima

substrate_name: pyruvate

sequence_source: UniProtKB Q9WZ19 REST JSON and FASTA retrieved 2026-06-15

substrate: pyruvate


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature Q86A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His6-tagged mutant Q86A


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature E85A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His6-tagged mutant E85A


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature H84A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His6-tagged mutant H84A


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature E85D to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His6-tagged mutant E85D


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature H84T to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His6-tagged mutant H84T


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature E85Q to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His6-tagged mutant E85Q


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature L141A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature W516R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature F147A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature F147R to reconstruct the assayed variant sequence.


organism: Nicotiana tabacum

substrate_name: ['Pyruvate', 'CO2', '2-Acetolactate']

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

substrate: ['Pyruvate', 'CO2', '2-Acetolactate']


organism: Oryza sativa Indica Group


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: mutant enzyme S627N, in the presence of imazethapyr, at pH 7.5 and 20°C

proof_lines: mutant enzyme S627N, in the presence of imazamox, at pH 7.5 and 20°C


substrate_name: Hydroxypyruvate

proof_lines: fusion protein containing an N-terminal oligohistidine sequence on the large subunit

substrate: Hydroxypyruvate


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADF8; direct REST lookup 2026-06-15 and applied mutation signature R32A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0ADF8; direct REST lookup 2026-06-15

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADF8; direct REST lookup 2026-06-15 and applied mutation signature H18A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0ADF8; direct REST lookup 2026-06-15 and applied mutation signature H18A/H24A to reconstruct the assayed variant sequence.


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB:Q8RL88; direct REST lookup 2026-06-15

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

proof_lines:
large subunit, pH 8.0, 60°C
holoenzyme, pH 8.0, 60°C
holoenzyme, pH 7.9, 55°C


organism: Haemophilus influenzae

sequence_source: UniProtKB:P45261; direct REST lookup 2026-06-15


sequence_source: UniProtKB:P9WG39; direct REST lookup 2026-06-15


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WG39; direct REST lookup 2026-06-15 and applied mutation signature P126T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WG39; direct REST lookup 2026-06-15 and applied mutation signature P126A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WG39; direct REST lookup 2026-06-15 and applied mutation signature P126V to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P9WG41; direct REST lookup 2026-06-15

proof_lines: pH 7.5, 37°C, recombinant His6-tagged wild-type enzyme


organism: Bacillus licheniformis


proof_lines:
UV method, pH 7, 37°C
HPLC method, pH 7, 37°C


organism: Brassica napus

proof_lines:
enzyme form I
enzyme form II


organism: Brassica rapa subsp. oleifera


organism: Cereibacter sphaeroides


organism: Corynebacterium glutamicum

substrate_name: 2-oxobutanoate; pyruvate

proof_lines: mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-isoleucine

proof_lines: mutant with a deleted C-terminal domain in the regulatory subunit IlvN, pH 7.3, 37°C, presence of 10 mM L-leucine

substrate: 2-oxobutanoate; pyruvate


proof_lines: wild-type, pH 7.3, 37°C, presence of 10 mM L-leucine

proof_lines: wild-type, pH 7.3, 37°C, presence of 10 mM L-isoleucine


organism: Descurainia sophia


organism: Escherichia coli (strain K12)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: pyruvate (with the catalytic subunit alone at pH 7.5 and at 37 degrees Celsius)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: pyruvate (catalytic subunit only)

substrate: pyruvate (catalytic subunit only)


organism: Enterobacter cloacae


organism: Enterococcus faecalis

proof_lines: wild type enzyme, pH and temperature not specified in the publication

proof_lines: recombinant wild-type enzyme, pH and temperature not specified in the publication


proof_lines: recombinant mutant E49D, pH and temperature not specified in the publication

proof_lines: mutant enzyme E49D, pH and temperature not specified in the publication


proof_lines: recombinant mutant E49A, pH and temperature not specified in the publication

proof_lines: mutant enzyme E49A, pH and temperature not specified in the publication


proof_lines: recombinant mutant E49Q, pH and temperature not specified in the publication

proof_lines: mutant enzyme E49Q, pH and temperature not specified in the publication


organism: Escherichia coli


organism: Leptospira interrogans

assay_conditions_summary: pH 8

proof_lines: pH 8.0, 25°, recombinant wild-type enzyme, cytochrome c reductase activity with 2[4Fe-4S] ferredoxin


organism: Limnospira platensis

substrate_name: NADPH

assay_conditions_summary: cofactor NADP+

proof_lines: in a 2,6-dichlorophenolindophenol reduction assay

substrate: NADPH


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADPH

proof_lines: recombinant enzyme, pH 8.2, 25°C, with NADH

proof_lines: recombinant enzyme, pH 8.2, 25°C, with NADPH

proof_lines: recombinant enzyme, pH 8.2, 25°C, with 2,6-dichlorophenolindophenol


organism: Pseudomonas putida

substrate_name: NADH

assay_conditions_summary: cofactor FAD

proof_lines: for FprA with FAD as cofactor, using Fe(III)-citrate as electron acceptor

proof_lines: for FprA with FAD as cofactor, using Fe(III)-EDTA as electron acceptor

proof_lines: for FprB with FAD as cofactor, using Fe(III)-EDTA as electron acceptor

substrate: NADH


organism: Raphanus sativus

substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


organism: Spinacia oleracea

substrate_name: dibromothymoquinone

assay_conditions_summary: pH 7; 288.15 K; cofactor NADPH

proof_lines: pH 7.0, 15°C, recombinant chimeric enzyme, diaphorase activity

substrate: dibromothymoquinone


organism: Arabidopsis thaliana

proof_lines:
Km-value of the second active site
Km-value of the first active site
about


proof_lines: mutant enzyme P197L, pH and temperature not specified in the publication


proof_lines: wild type enzyme, pH and temperature not specified in the publication


organism: Bacillus anthracis


organism: Bacillus licheniformis


proof_lines:
wild-type, pH 7.6, 37°C
wild-type with His-tag, pH 7.6, 37°C
wild-type, 37°C, pH 7.6


proof_lines:
mutant E47Q, pH 7.6, 37°C
mutant E47Q, 37°C, pH 7.6


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0DP90 (ILVG_ECOLI; ilvG), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature E47A to reconstruct the assayed variant sequence.

proof_lines:
mutant E47A, pH 7.6, 37°C
mutant E47A, 37°C, pH 7.6


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0DP90 (ILVG_ECOLI; ilvG), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature Q110E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature V477I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature R289Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature E60A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature V391A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature C83S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature Q480W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature L476M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature C83T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature C83A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P08142 (ILVB_ECOLI; ilvB), retrieved 2026-06-15; selected from E. coli EC 2.2.1.6 candidates by paper isozyme anchor and mutation-coordinate check. and applied mutation signature E60Q to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


organism: Neurospora crassa

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


organism: Nicotiana tabacum


organism: Listeria seeligeri


organism: Methanococcus aeolicus


organism: Methanococcus maripaludis


organism: Methanococcus voltae


proof_lines:
catalytic subunit
pH 7.0, 37°C, holoenzyme
pH 7.0, 37°C, catalytic subunit


proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme


proof_lines: mutant S539R, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S167R, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S167A, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S506A, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S539A, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S506R, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant S539F, pH not specified in the publication, temperature not specified in the publication


organism: Saccharomyces cerevisiae


organism: Escherichia coli


organism: Euglena gracilis


organism: Haloferax volcanii

proof_lines: pH 7.5, 37°C, in the presence of 3.5 M KCl


organism: Hordeum vulgare

proof_lines:
pH 7.0, 37°C, isoform ALS II
pH 7.0, 37°C, isoform ALS I


organism: Lactococcus lactis


organism: Lactococcus lactis subsp. lactis

substrate_name: Pyruvate

substrate: Pyruvate


organism: Leuconostoc lactis

proof_lines:
30°C, 60 ng protein in assay
30°C, 120 ng protein in assay


organism: Leuconostoc mesenteroides


proof_lines: catalytic subunit plus small subunit, pH 7.0, 30°C


organism: Schoenoplectiella juncoides

proof_lines: pH 7.0, 30°C, sulfonylurea-resistant biotype

proof_lines: pH 7.0, 30°C, sulfonylurea-susceptible biotype


organism: Serratia marcescens


organism: Thermotoga maritima

proof_lines: pH 7.0, 85°C, recombinant catalytic subunit


organism: Zea mays

proof_lines:
AHAS I
AHAS II


substrate_name: phosphoenolpyruvate

proof_lines: pH 6.2, wild-type enzyme, Mn2+- and fructose 1,6-bisphosphate activated

proof_lines: pH 6.2, wild-type enzyme, Mg2+-activated

proof_lines: pH 6.2, wild-type enzyme, Mg2+ and fructose 1,6-bisphosphate activated

substrate: phosphoenolpyruvate


proof_lines: pH 6.2, mutant enzyme T298C, Mn2+-activated

proof_lines: pH 6.2, mutant enzyme T298C, Mn2+- and fructose 1,6-bisphosphate activated

proof_lines: mutant enzyme T298C, activated be Tl+ and Mn2+


organism: Saccharomyces pastorianus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: cofactor ATP


organism: Schistosoma mansoni


organism: Sparus aurata

proof_lines:
25°C, sample taken in June
25°C, sample taken in January


organism: Streptococcus mutans

assay_conditions_summary: pH 7.5; cofactor ADP

proof_lines: in the presence of glucose 6-phosphate, at pH 7.5


organism: Bos taurus

substrate_name: Pefachrome

substrate: Pefachrome


substrate_name: N-alpha-benzoyl-L-Arg ethyl ester

proof_lines:
wild-type, pH 8.0, 25°C
pH 8.0, wild-type enzyme

substrate: N-alpha-benzoyl-L-Arg ethyl ester


assay_conditions_summary: pH 8; 310.15 K; buffer 67 mM sodium phosphate

proof_lines:
pH 8.0, 37°C
at 5°C
gamma-trypsin


organism: Cambarus affinis

substrate_name: tosyl-Arg methyl ester

proof_lines: enzyme immobilized on porous glass loaded with isothiocyanate

substrate: tosyl-Arg methyl ester


organism: Canis lupus familiaris

substrate_name: Nalpha-benzoyl-DL-Arg-p-nitroanilide

substrate: Nalpha-benzoyl-DL-Arg-p-nitroanilide


organism: Cirrhinus mrigala


organism: Colossoma macropomum

substrate_name: Abz-RPFK-EDDnp

substrate: Abz-RPFK-EDDnp


organism: Diatraea saccharalis

assay_conditions_summary: pH 8.5; 303.15 K; buffer 100 mM Tris-HCl

proof_lines: at 30°C in 100 mM Tris-HCl buffer pH 8.5


organism: Fusarium oxysporum

substrate_name: Unknown

substrate: Unknown


organism: Gadus morhua


organism: Gallus gallus

proof_lines:
cationic trypsin 2
anionic trypsin
cationic trypsin 1


organism: Homo sapiens

proof_lines: mutant enzyme R193G, in 50 mM Tricine, 10 mM CaCl2, pH 8.0 at 20°C

proof_lines: mutant enzyme R193G, in 20 mM Tricine,10 mM CaCl2, at pH 8.0 and 20°C


organism: Streptococcus sanguis

substrate_name: ADP; Phosphoenolpyruvate

substrate: ADP; Phosphoenolpyruvate


organism: Sus scrofa

substrate_name: ADP

assay_conditions_summary: 298.15 K; cofactor ADP

proof_lines:
at 25°C
solubilized enzyme
bound enzyme

substrate: ADP


organism: Synechococcus elongatus


organism: Synechococcus sp.

proof_lines:
allosteric enzyme, pH 7.5, 24°C
allosteric enzyme, pH 7.0, 24°C


organism: Takifugu rubripes

assay_conditions_summary: pH 7.4; cofactor ADP

proof_lines: activated by fructose D-1,6-bisphosphate


organism: Tenebrio molitor

proof_lines: in the presence of fructose 1,6-diphosphate


organism: Thermoproteus tenax

assay_conditions_summary: pH 7; 323.15 K; cofactor ADP


organism: Toxoplasma gondii

proof_lines: PykII, in 100 mM Tris-HCl,pH 8.5, at 37°C

substrate: Phosphoenolpyruvate; ADP


organism: Trachemys scripta


organism: Trypanosoma brucei


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant L76R


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R22G


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant R19Q


proof_lines: SABIO-RK modifier species: pyruvate kinase(Enzyme) mutant F463V


organism: Trypanosoma cruzi


organism: Urocitellus richardsonii

assay_conditions_summary: pH 7; 278.15 K; cofactor ADP

proof_lines: purified enzyme, pH 7.0, 25°C/room temperature


organism: Vigna radiata

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ADP


organism: Zapus hudsonius


organism: Zymomonas mobilis

assay_conditions_summary: pH 6.5; 298.15 K; cofactor ADP


organism: Albatrossia pectoralis

substrate_name: Nalpha-4-tosyl-L-arginine methyl ester

substrate: Nalpha-4-tosyl-L-arginine methyl ester


organism: Balistes capriscus


organism: Boops boops

substrate_name: N-benzoyl-DL-arginine 4-nitroanilide

substrate: N-benzoyl-DL-arginine 4-nitroanilide


organism: Bos taurus


organism: Homo sapiens

proof_lines: mutant enzyme R193Y, in 50 mM Tricine, 10 mM CaCl2, pH 8.0 at 20°C


proof_lines: mutant enzyme R193F, in 50 mM Tricine, 10 mM CaCl2, pH 8.0 at 20°C


proof_lines: mutant enzyme R193A, in 50 mM Tricine, 10 mM CaCl2, pH 8.0 at 20°C

proof_lines: mutant enzyme R193A, in 20 mM Tricine,10 mM CaCl2, at pH 8.0 and 20°C


substrate_name: Z-Gly-Pro-Arg-p-nitroanilide

proof_lines: mutant enzyme R193G/G142A, in 20 mM Tricine,10 mM CaCl2, at pH 8.0 and 20°C

substrate: Z-Gly-Pro-Arg-p-nitroanilide


proof_lines: mutant enzyme R193G/G184A, in 20 mM Tricine,10 mM CaCl2, at pH 8.0 and 20°C


proof_lines: mutant enzyme R193G/G19A, in 20 mM Tricine,10 mM CaCl2, at pH 8.0 and 20°C


proof_lines: wild type enzyme, in 20 mM Tricine,10 mM CaCl2, at pH 8.0 and 20°C

proof_lines: wild type enzyme, in 50 mM Tricine, 10 mM CaCl2, pH 8.0 at 20°C


organism: Lateolabrax japonicus

proof_lines:
pH 8.0, 37°C, trypsin A
pH 8.0, 37°C, trypsin B


organism: Lutjanus vitta

substrate_name: alpha-N-p-tosyl-L-arginine methyl ester

substrate: alpha-N-p-tosyl-L-arginine methyl ester


organism: Musca domestica

proof_lines: at 30°C in 100 mM Tris-HCl buffer pH 8.5


organism: Mustelus mustelus


organism: Oreochromis niloticus


organism: Periplaneta americana


organism: Pterygoplichthys disjunctivus


organism: Rattus norvegicus

substrate_name: Pefachrome tPA

proof_lines: variant X99rT containing the 99-loop (Glu97,Tyr99) of factor Xa

proof_lines: variant X(99/175/190)rT containing the 99-loop the 175-loop (Ser172,Ser173, Phe174, Ile175) and Ala190 of factor Xa

proof_lines: variant X99rT containing the 99-loop (Glu97, Tyr99) of factor Xa

substrate: Pefachrome tPA


proof_lines: recombinant inhibitor from Pichia pastoris, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, pH 7.5 containing 0.1% (w/v) bovine serum albumin, at 25°C


proof_lines: pH 8.0, 37°C, mutant enzyme D189S/DELTA223


proof_lines:
pH 8.0, 37°C, wild-type enzyme
wild-type enzyme, pH 9
wild-type enzyme, pH 8


substrate_name: Benzyloxycarbonyl-Lys-thiobenzyl ester

substrate: Benzyloxycarbonyl-Lys-thiobenzyl ester


organism: salmon


organism: Sardinops caeruleus


organism: Sepia officinalis


organism: Streptomyces griseus


substrate_name: N-benzoyl-L-Arg ethyl ester

substrate: N-benzoyl-L-Arg ethyl ester


organism: Streptomyces omiyaensis


organism: Sus scrofa


organism: Tenebrio molitor


organism: Thunnus albacares

substrate_name: N-alpha-p-tosyl-L-arginine methyl ester

proof_lines:
trypsin B, at pH 8.0 and 30°C
trypsin A, at pH 8.0 and 30°C

substrate: N-alpha-p-tosyl-L-arginine methyl ester


organism: Thunnus tonggol

substrate_name: Nalpha-p-tosyl-L-Arg methyl ester

substrate: Nalpha-p-tosyl-L-Arg methyl ester


organism: Aeribacillus pallidus

substrate_name: Acrylamide

proof_lines:
pH 7.2
pH 8.0, 50°C
at pH 7 and 50°C

substrate: Acrylamide


organism: Rhodococcus sp. C-1

substrate_name: propanil

substrate: propanil


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: acetamide

assay_conditions_summary: pH 7

proof_lines: acyl transfer reaction on hydroxylamine, pH = 7

substrate: acetamide


organism: Saccharolobus solfataricus

substrate_name: ketoprofen amide

substrate: ketoprofen amide


organism: Stutzerimonas stutzeri


organism: Homo sapiens

substrate_name: Anandamide; H2O

substrate: Anandamide; H2O


organism: Klebsiella pneumoniae


organism: Methylophilus methylotrophus


organism: Pseudomonas aeruginosa

substrate_name: N-methylpropionamide

assay_conditions_summary: pH 8.66; 298.15 K; buffer added, 25°C

proof_lines:
hydrolysis
transferase reaction
hydrolysis, strain AI3

substrate: N-methylpropionamide


organism: Pseudomonas chlororaphis

substrate_name: Propionamide

substrate: Propionamide


organism: Pseudomonas putida

proof_lines:
A-amidase
strain PPW3, C-amidase


organism: Pseudonocardia acaciae

substrate_name: 4-hydroxybenzoic acid 1-phenylethylidene hydrazide


organism: Pseudonocardia thermophila


organism: Rattus norvegicus

substrate_name: arachidonoyl-ethanolamine

substrate: arachidonoyl-ethanolamine


organism: Rhodococcus erythropolis

proof_lines: pH and temperature not specified in the publication


organism: Rhodococcus sp.

substrate_name: Hydroxylamine; Acetamide

substrate: Hydroxylamine; Acetamide


organism: Agrobacterium tumefaciens


organism: Blastobacter sp.

substrate_name: Benzamide

substrate: Benzamide


organism: Brevibacterium sp.


substrate_name: DL-Lactamide

proof_lines:
strain R312
strain R312, transfer reaction

substrate: DL-Lactamide


organism: Burkholderia sp.


organism: Cucurbita maxima


organism: Delftia acidovorans

proof_lines: substrate 4-nitroacetanilide, competitive inhibition, induction of activity for 2-nitrophenylacetate and methylbutyrate


organism: Escherichia coli


organism: Geobacillus subterraneus

substrate_name: nicotinamide

substrate: nicotinamide


enzyme_display_name: histamine N-methyltransferase

organism: Homo sapiens

substrate_name: histamine

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: pH 8

enzyme: histamine N-methyltransferase

substrate: histamine


organism: Mus musculus

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: histamine (at pH 7.5)

substrate: histamine (at pH 7.5)


enzyme_display_name: N-terminal amino-acid N(alpha)-acetyltransferase NatA

organism: Schizosaccharomyces pombe

substrate_name: SASEAGVRWGRPVGRRRRP

sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature H72A to reconstruct the assayed variant sequence.

substrate: SASEAGVRWGRPVGRRRRP


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature E62A to reconstruct the assayed variant sequence.

enzyme: N-terminal amino-acid N(alpha)-acetyltransferase NatA


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature K29A/Y33A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature L22A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature R113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature K29A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature H20A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature K59A/E61A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature K59A/E62A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature E24D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature P23A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature E61A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature E24Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q9UTI3 ARD1_SCHPO; RCSB 4KVM entity 2/chains E-F-G-H; PMID 23912279 and applied mutation signature Y33A to reconstruct the assayed variant sequence.


substrate_name: Histamine

sequence_source: UniProtKB:P50135 direct accession lookup (reviewed); Histamine N-methyltransferase (HMT); EC 2.1.1.8; Homo sapiens; length 292.

substrate: Histamine


enzyme_display_name: 3,5-dihydroxybiphenyl synthase

organism: Malus domestica

substrate_name: benzoyl-CoA

sequence_source: UniProtKB:K9MS05 direct accession lookup (unreviewed); BIS1 biphenyl synthase; EC 2.3.1.177; Malus domestica; length 390.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

enzyme: 3,5-dihydroxybiphenyl synthase

substrate: benzoyl-CoA


source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: UniProtKB:K9MST3 direct accession lookup (unreviewed); BIS3 biphenyl synthase; EC 2.3.1.177; Malus domestica; length 388.

proof_lines:
pH 7.0, 37°C
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: brenda skid


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


organism: Pyrus communis

sequence_source: UniProtKB:A0A1B1PJB0 direct accession lookup (unreviewed); Biphenyl synthase 2; EC 2.3.1.177; Pyrus communis; length 390.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: pH 7; 308.15 K; cofactor CoA


substrate_name: salicoyl-CoA

sequence_source: UniProtKB:A0A1B1PJB7 direct accession lookup (unreviewed); Biphenyl synthase 1; EC 2.3.1.177; Pyrus communis; length 390.

substrate: salicoyl-CoA


organism: Sorbus aucuparia

substrate_name: Malonyl-CoA; Benzoyl-CoA

sequence_source: UniProtKB:Q27Z07 direct accession lookup (reviewed); 3,5-dihydroxybiphenyl synthase / Biphenyl synthase 1; EC 2.3.1.177; Sorbus aucuparia; length 390.

substrate: Malonyl-CoA; Benzoyl-CoA


substrate_name: Benzoyl-CoA; Malonyl-CoA

assay_conditions_summary: cofactor CoA

substrate: Benzoyl-CoA; Malonyl-CoA


substrate_name: Benzoyl-CoA

verification_status: corrected

sequence_source: UniProtKB Q27Z07 direct REST accession check on 2026-06-15

assay_conditions_summary: pH 7; 308.15 K; buffer and no single assay pH numeral; cofactor CoA

column_label: Table 2: Steady-state kinetic parameters for BIS isoenzymes from S. aucuparia cell cultures with benzoyl-CoA and salicoyl-CoA as starter substrates (Plant Mol Biol 2010, 72:17-25); isoenzyme row 'BIS1'; group head 'benzoyl-CoA'; column 'kcat (min^-1)' = 0.43; column 'Km (uM)' = 0.7; column 'kcat/Km (M^-1 s^-1)' = 10,181; the same printed line also carries the salicoyl-CoA group (three cells) and the Malonyl-CoA group head with one cell, column 'Km (uM)' = 6.2.

raw_value_unit_evidence: Table 2, isoenzyme row 'BIS1', benzoyl-CoA group: kcat = 0.43 min^-1; Km = 0.7 uM; printed kcat/Km = 10,181 M^-1 s^-1.

row_label: Table 2, isoenzyme row 'BIS1', benzoyl-CoA starter-substrate block (the three columns headed kcat (min^-1), Km (uM) and kcat/Km (M^-1 s^-1) under the benzoyl-CoA group head)

substrate: Benzoyl-CoA

status: corrected


substrate_name: Peptide; Acetyl-CoA

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: SABIO-RK modifier species: N-terminal amino-acid Nalpha-acetyltransferase NatA(Enzyme) wildtype C-terminal truncated Naa10 (1-160)/N-terminal His6-tagged Naa15 (1-866)/MBP-tagged HYPK

substrate: Peptide; Acetyl-CoA


proof_lines: SABIO-RK modifier species: N-terminal amino-acid Nalpha-acetyltransferase NatA(Enzyme) wildtype C-terminal truncated Naa10 (1-160)/N-terminal His6-tagged Naa15 (1-866)


organism: Saccharolobus solfataricus

substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q980R9 direct REST accession check on 2026-06-15 plus selected source mutation R100A and applied mutation signature R100A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 338.15 K; cofactor CoA

substrate: acetyl-CoA


sequence_source: UniProtKB Q980R9 direct REST accession check on 2026-06-15


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q980R9 direct REST accession check on 2026-06-15 plus selected BRENDA mutation R100A and applied mutation signature R100A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q980R9 direct REST accession check on 2026-06-15 plus selected source mutation T105A and applied mutation signature T105A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q980R9 direct REST accession check on 2026-06-15 plus selected BRENDA mutation T105A and applied mutation signature T105A to reconstruct the assayed variant sequence.


enzyme_display_name: inositol-polyphosphate multikinase

organism: Arabidopsis thaliana

substrate_name: ATP; D-myo-Inositol 1,4,5-trisphosphate

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

source_databases_merged: sabio_rk brenda skid

enzyme: inositol-polyphosphate multikinase

substrate: ATP; D-myo-Inositol 1,4,5-trisphosphate


substrate_name: 1D-myo-inositol 1,4,5-trisphosphate

substrate: 1D-myo-inositol 1,4,5-trisphosphate


assay_conditions_summary: pH 7.8; 303.15 K; cofactor ATP


enzyme_display_name: NADH kinase

substrate_name: ATP; NADH

assay_conditions_summary: cofactor NADH

enzyme: NADH kinase

substrate: ATP; NADH


organism: Micrococcus luteus

substrate_name: Tetrapolyphosphate; NADH

substrate: Tetrapolyphosphate; NADH


organism: Saccharomyces cerevisiae

substrate_name: NADH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 8; 310.15 K; cofactor NADH


proof_lines:
recombinant enzyme, pH 7.2, 37°C
37°C, pH 7.2


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: recombinant wild-type enzyme, pH 7.5, 30°C


mutation_signature: recombinant deletion mutant enzyme

proof_lines: recombinant deletion mutant enzyme, pH 7.5, 30°C


organism: Rattus norvegicus

substrate_name: 1D-myo-inositol 4,5-bisphosphate

substrate: 1D-myo-inositol 4,5-bisphosphate


substrate_name: serotonin

substrate: serotonin


substrate_name: acetyl-CoA (at pH 8.0 and at 25 degrees Celsius)


assay_conditions_summary: cofactor ATP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: NAD

substrate: NAD


substrate_name: benzoyl-CoA

proof_lines: kcat is 0.43 min(-1) with benzoyl-CoA as substrate. kcat is 0.27 min(-1) with salicoyl-CoA as substrate.


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: Ser-N-terminal peptide

proof_lines: kcat is 33.57 min(-1) for acetyltransferase activity with acetyl-CoA (at 65 degrees Celsius with Ser-N-terminal peptide (Alba)) (PubMed:25728374). kcat is 3.3 min(-1) for acetyltransferase activity with Ser-N-terminal peptide (PubMed:239598

substrate: Ser-N-terminal peptide


assay_conditions_summary: pH 7.9; cofactor ATP

proof_lines: Measured at pH 7.9 and 25 degrees Celsius for all experiments.


assay_conditions_summary: pH 7.9; cofactor NADH


organism: Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / CCUG 213 / NBRC 12614 / NCIMB 9131 / NCTC 9757 / MK)

substrate_name: pAp

proof_lines: kcat is 22 sec(-1) for pAp. kcat is 7.1 sec(-1) for 2'-deoxy-pAp. kcat is 8.6 sec(-1) for pCp. kcat is 9.4 sec(-1) for 2'-deoxy-pCp. kcat is 12.3 sec(-1) for pGp. kcat is 4.2 sec(-1) for 2'-deoxy-pGp. kcat is 5.4 sec(-1) for pUp. kcat is 5.

substrate: pAp


organism: Escherichia coli (strain K12)

proof_lines: kcat is 9.9 sec(-1) with pAp as substrate. kcat is 5.6 sec(-1) with 2'-deoxy-pAp as substrate. kcat is 6.0 sec(-1) with pCp (2'5'/3'5' mixture) as substrate. kcat is 1.9 sec(-1) with 2'-deoxy-pCp as substrate. kcat is 5.5 sec(-1) with pGp (


sequence_variant_note: Resolved canonical sequence from direct UniProtKB REST lookup for Q06892 plus row-specific R293H reconstruction and applied mutation signature R293H to reconstruct the assayed variant sequence.


organism: Chromobacterium violaceum

substrate_name: uridine 3',5'-bisphosphate

sequence_source: direct UniProtKB REST lookup for Q7NXD4 canonical sequence

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pUp (footnote a)`: kcat (s^-1) = 5.4; Km (uM) = 8.8; kcat/Km (M^-1 s^-1) = 6.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.4 s^-1 is already the export unit, so no conversion is needed; the exported value is 5.4 s^(-1). Km: printed Table 3 cell 8.8 uM; 8.8 / 1000 = 0.0088 mM; the exported value is 0.0088 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 6.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.1 x 10^5 / 1000 = 610.0 s^(-1)*mM^(-1); the exported value is 613.6363636363636 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pUp (footnote a)`

substrate: uridine 3',5'-bisphosphate


substrate_name: guanosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pGp (footnote a)`: kcat (s^-1) = 12.3; Km (uM) = 17.3; kcat/Km (M^-1 s^-1) = 7.1 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.3 s^-1 is already the export unit, so no conversion is needed; the exported value is 12.3 s^(-1). Km: printed Table 3 cell 17.3 uM; 17.3 / 1000 = 0.0173 mM; the exported value is 0.0173 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 7.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.1 x 10^5 / 1000 = 710.0 s^(-1)*mM^(-1); the exported value is 710.9826589595376 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pGp (footnote a)`

substrate: guanosine 3',5'-bisphosphate


substrate_name: H2O; Adenosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pAp`: kcat (s^-1) = 22; Km (uM) = 15.5; kcat/Km (M^-1 s^-1) = 1.4 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22 s^-1 is already the export unit, so no conversion is needed; the exported value is 22.0 s^(-1). Km: printed Table 3 cell 15.5 uM; 15.5 / 1000 = 0.0155 mM; the exported value is 0.0015999999999999999 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 1.4 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^6 / 1000 = 1400.0 s^(-1)*mM^(-1); this catalog row exports no kcat/Km field, so the printed efficiency cell replaces nothing.

row_label: Table 3, decoded plain-numeral transcription, compound row `pAp`

substrate: H2O; Adenosine 3',5'-bisphosphate


substrate_name: 2'-Deoxycytidine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pCp`: kcat (s^-1) = 9.4; Km (uM) = 26; kcat/Km (M^-1 s^-1) = 3.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.4 s^-1 is already the export unit, so no conversion is needed; the exported value is 9.4 s^(-1). Km: printed Table 3 cell 26 uM; 26 / 1000 = 0.026 mM; the exported value is 0.026 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 3.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.6 x 10^5 / 1000 = 360.0 s^(-1)*mM^(-1); the exported value is 361.53846153846155 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pCp`

substrate: 2'-Deoxycytidine 3',5'-bisphosphate


substrate_name: Guanosine bisphosphate

column_label: Table 3 (PDF page 7 of 10, journal page 597), compound row `pGp (footnote a)`: kcat (s^-1) = 12.3; Km (uM) = 17.3; kcat/Km (M^-1 s^-1) = 7.1 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 12.3 s^-1 is already the export unit -> 12.3 s^(-1); the exported value is 12.3 s^(-1). Km: printed cell 17.3 uM -> 0.0173 mM (divide by 1000); the exported value is 0.017 mM. kcat/Km: the paper PRINTS the kcat/Km cell 7.1 x 10^5 M^-1 s^-1 for this compound line -> 710.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 723.5294117647059 s^(-1)*mM^(-1).

table_label: Table 3 (PDF page 7 of 10, journal page 597) 'Kinetic Constants for Cv1693 with Various Substrates'

substrate: Guanosine bisphosphate


substrate_name: Uridine bisphosphate

column_label: Table 3 (PDF page 7 of 10, journal page 597), compound row `pUp (footnote a)`: kcat (s^-1) = 5.4; Km (uM) = 8.8; kcat/Km (M^-1 s^-1) = 6.1 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 5.4 s^-1 is already the export unit -> 5.4 s^(-1); the exported value is 5.4 s^(-1). Km: printed cell 8.8 uM -> 0.0088 mM (divide by 1000); the exported value is 0.009 mM. kcat/Km: the paper PRINTS the kcat/Km cell 6.1 x 10^5 M^-1 s^-1 for this compound line -> 610.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 600.0000000000001 s^(-1)*mM^(-1).

substrate: Uridine bisphosphate


substrate_name: 2'-Deoxyuridine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pUp`: kcat (s^-1) = 5.2; Km (uM) = 29; kcat/Km (M^-1 s^-1) = 1.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.2 s^-1 is already the export unit, so no conversion is needed; the exported value is 5.2 s^(-1). Km: printed Table 3 cell 29 uM; 29 / 1000 = 0.029 mM; the exported value is 0.029 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 1.8 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.8 x 10^5 / 1000 = 180.0 s^(-1)*mM^(-1); the exported value is 179.3103448275862 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pUp`

substrate: 2'-Deoxyuridine 3',5'-bisphosphate


substrate_name: 2'-Deoxyinosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pIp`: kcat (s^-1) = 4.3; Km (uM) = 22; kcat/Km (M^-1 s^-1) = 1.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.3 s^-1 is already the export unit, so no conversion is needed; the exported value is 4.3 s^(-1). Km: printed Table 3 cell 22 uM; 22 / 1000 = 0.022 mM; the exported value is 0.022 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 1.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^5 / 1000 = 190.0 s^(-1)*mM^(-1); the exported value is 195.45454545454547 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pIp`

substrate: 2'-Deoxyinosine 3',5'-bisphosphate


substrate_name: N6-methyl adenosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `N6-methyl-3',5'-pAp`: kcat (s^-1) = 11.6; Km (uM) = 5.4; kcat/Km (M^-1 s^-1) = 2.1 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 11.6 s^-1 is already the export unit, so no conversion is needed; the exported value is 11.6 s^(-1). Km: printed Table 3 cell 5.4 uM; 5.4 / 1000 = 0.0054 mM; the exported value is 0.0054 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 2.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.1 x 10^6 / 1000 = 2100.0 s^(-1)*mM^(-1); the exported value is 2148.148148148148 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `N6-methyl-3',5'-pAp`

substrate: N6-methyl adenosine 3',5'-bisphosphate


substrate_name: 2'-Deoxyguanosine 3',5'-bisphosphate

column_label: Table 3 (PDF page 7 of 10, journal page 597), compound row `2'-deoxy-pGp`: kcat (s^-1) = 4.2; Km (uM) = 5.2; kcat/Km (M^-1 s^-1) = 7.9 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 4.2 s^-1 is already the export unit -> 4.2 s^(-1); the exported value is 4.2 s^(-1). Km: printed cell 5.2 uM -> 0.0052 mM (divide by 1000); the exported value is 0.005 mM. kcat/Km: the paper PRINTS the kcat/Km cell 7.9 x 10^5 M^-1 s^-1 for this compound line -> 790.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 840.0 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `2'-deoxy-pGp`

substrate: 2'-Deoxyguanosine 3',5'-bisphosphate


substrate_name: inosine 3',5'-bisphosphate

substrate: inosine 3',5'-bisphosphate


substrate_name: Cytidine bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `pCp (footnote a)`: kcat (s^-1) = 8.6; Km (uM) = 14; kcat/Km (M^-1 s^-1) = 6.2 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 8.6 s^-1 is already the export unit, so no conversion is needed; the exported value is 8.6 s^(-1). Km: printed Table 3 cell 14 uM; 14 / 1000 = 0.014 mM; the exported value is 0.014 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 6.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.2 x 10^5 / 1000 = 620.0 s^(-1)*mM^(-1); the exported value is 614.2857142857142 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pCp (footnote a)`

substrate: Cytidine bisphosphate


substrate_name: Thymidine 3',5'-bisphosphate

column_label: Table 3 (PDF page 7 of 10, journal page 597), compound row `pTp`: kcat (s^-1) = 3.3; Km (uM) = 9.3; kcat/Km (M^-1 s^-1) = 3.6 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 3.3 s^-1 is already the export unit -> 3.3 s^(-1); the exported value is 3.3 s^(-1). Km: printed cell 9.3 uM -> 0.0093 mM (divide by 1000); the exported value is 0.009 mM. kcat/Km: the paper PRINTS the kcat/Km cell 3.6 x 10^5 M^-1 s^-1 for this compound line -> 360.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 366.6666666666667 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, compound row `pTp`

substrate: Thymidine 3',5'-bisphosphate


substrate_name: 2'-deoxy-guanosine 3',5'-bisphosphate

column_label: Table 3 'Kinetic Constants for Cv1693 with Various Substrates' (Biochemistry 2014, 53(3):591), compound row `2'-deoxy-pGp`: kcat (s^-1) = 4.2; Km (uM) = 5.2; kcat/Km (M^-1 s^-1) = 7.9 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.2 s^-1 is already the export unit, so no conversion is needed; the exported value is 4.2 s^(-1). Km: printed Table 3 cell 5.2 uM; 5.2 / 1000 = 0.0052 mM; the exported value is 0.0052 mM. kcat/Km: the paper prints its own Table 3 efficiency cell 7.9 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.9 x 10^5 / 1000 = 790.0 s^(-1)*mM^(-1); the exported value is 807.6923076923077 s^(-1)*mM^(-1).

substrate: 2'-deoxy-guanosine 3',5'-bisphosphate


enzyme_display_name: carboxypeptidase A2

sequence_source: UniProtKB reviewed accession P48052 / CBPA2_HUMAN from direct EC 3.4.17.15 + organism Homo sapiens lookup

proof_lines:
pH 7.4, 25°C, recombinant enzyme
pH 7.5, 25°C

enzyme: carboxypeptidase A2


substrate_name: benzyloxycarbonyl-Gly-Gly-Leu

sequence_source: UniProtKB reviewed accession P19222 / CBPA2_RAT from direct EC 3.4.17.15 + organism Rattus norvegicus lookup

substrate: benzyloxycarbonyl-Gly-Gly-Leu


substrate_name: Carbobenzoxy-Gly-Gly-Phe

sequence_source: UniProtKB reviewed accession P48052 direct lookup on 2026-06-15

substrate: Carbobenzoxy-Gly-Gly-Phe


substrate_name: H2O; Carbobenzoxy-Gly-Gly-Phe

substrate: H2O; Carbobenzoxy-Gly-Gly-Phe


substrate_name: Carbobenzoxy-Gly-Phe

sequence_source: UniProtKB reviewed accession P19222 direct lookup on 2026-06-15

substrate: Carbobenzoxy-Gly-Phe


substrate_name: Carbobenzoxy-Gly-Gly-Leu

substrate: Carbobenzoxy-Gly-Gly-Leu


substrate_name: 3-(2-furyl)acryloyl-Phe-Phe (at 25 degrees Celsius)

proof_lines: kcat is 121 sec(-1) with 3-(2-furyl)acryloyl-Phe-Phe as substrate (at 25 degrees Celsius) (PubMed:20385563). kcat is 65.3 sec(-1) with 3-(2-furyl)acryloyl-Phe-Trp as substrate (at 25 degrees Celsius) (PubMed:20385563). kcat is 18.6 sec(-1)


enzyme_display_name: arachidonate 8-lipoxygenase

organism: Plexaura homomalla

substrate_name: arachidonate

smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O

enzyme: arachidonate 8-lipoxygenase

substrate: arachidonate


substrate_name: 2'-deoxy-uridine 3',5'-bisphosphate

substrate: 2'-deoxy-uridine 3',5'-bisphosphate


organism: Homo sapiens


enzyme_display_name: formimidoylglutamate deiminase

organism: Pseudomonas aeruginosa

substrate_name: H2O; N-Formimino-L-glutamate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HU77 canonical sequence with direct H269N reconstruction and applied mutation signature H269N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant H269N (Zn2+)

enzyme: formimidoylglutamate deiminase

substrate: H2O; N-Formimino-L-glutamate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HU77 canonical sequence with direct D320A reconstruction and applied mutation signature D320A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant D320A (Zn2+)


substrate_name: N-Formimino-L-glutamate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HU77 canonical sequence with direct E235Q reconstruction and applied mutation signature E235Q to reconstruct the assayed variant sequence.

substrate: N-Formimino-L-glutamate


sequence_source: UniProtKB Q9HU77 canonical sequence with direct E235Q reconstruction

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant E235Q (Zn2+)


enzyme_display_name: ATP adenylyltransferase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: Ap4A (at 37 degrees Celsius and pH 7.6)

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

enzyme: ATP adenylyltransferase

substrate: Ap4A (at 37 degrees Celsius and pH 7.6)


organism: Mycobacterium tuberculosis

substrate_name: P1,P4-bis(5'-adenosyl) tetraphosphate

substrate: P1,P4-bis(5'-adenosyl) tetraphosphate


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P9WMK9 and applied mutation signature S147T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P9WMK9 and applied mutation signature G146S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P9WMK9 and applied mutation signature S147A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P9WMK9 and applied mutation signature G146Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HU77 and applied mutation signature E235D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HU77 and applied mutation signature D320C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant D320C (Zn2+)


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


substrate_name: N-Formimino-L-glutamate; H2O

substrate: N-Formimino-L-glutamate; H2O


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HU77 and applied mutation signature H269A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant H269A (Zn2+)


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HU77 and applied mutation signature H269C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant H269C (Zn2+)


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:Q9HU77 and applied mutation signature E235A to reconstruct the assayed variant sequence.


substrate_name: Histamine; S-Adenosyl-L-methionine

sequence_source: UniProtKB:P50135 direct REST lookup on 2026-06-15

substrate: Histamine; S-Adenosyl-L-methionine


substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P50135 direct REST lookup plus local substitution reconstruction on 2026-06-15 and applied mutation signature L208V to reconstruct the assayed variant sequence.

substrate: S-adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P50135 direct REST lookup plus local substitution reconstruction on 2026-06-15 and applied mutation signature L208K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P50135 direct REST lookup plus local substitution reconstruction on 2026-06-15 and applied mutation signature L208F to reconstruct the assayed variant sequence.


organism: Mus musculus

substrate_name: S-Adenosyl-L-methionine; Histamine

sequence_source: UniProtKB:Q91VF2 direct REST lookup on 2026-06-15

substrate: S-Adenosyl-L-methionine; Histamine


enzyme_display_name: N-terminal methionine N(alpha)-acetyltransferase NatE

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


sequence_source: UniProtKB:P9WMK9 direct REST lookup on 2026-06-15

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines: in 50 mM HEPES-Na (pH 7.6), 1 mM MnCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WMK9 direct REST lookup plus local substitution reconstruction on 2026-06-15 and applied mutation signature G146Q to reconstruct the assayed variant sequence.


substrate_name: M-A-A-A peptide

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

proof_lines: kcat is 7.2 min(-1) with M-L-G-P-E peptide. kcat is 7.2 min(-1) with M-L-D-P-E peptide. kcat is 10.9 min(-1) with M-I-G-P-E peptide. kcat is 6.8 min(-1) with M-L-A-L-I peptide. kcat is 2.3 min(-1) with M-L-G-T-G peptide. kcat is 5.6 min(-1)

enzyme: N-terminal methionine N(alpha)-acetyltransferase NatE

substrate: M-A-A-A peptide


substrate_name: Ser-N-terminal peptide

substrate: Ser-N-terminal peptide


proof_lines: kcat is 93.8 sec(-1) with Ap4A as substrate.


proof_lines: kcat is 81.2 sec(-1) with Ap4A as substrate.


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: N-formimidoyl-L-glutamate (in the presence of Zn(2+))

proof_lines: kcat is 13.2 sec(-1) with N-formimidoyl-L-glutamate as substrate (in the presence of Zn(2+)). kcat is 21.3 sec(-1) with N-formimidoyl-L-glutamate as substrate (in the presence of Ni(2+)). kcat is 31.0 sec(-1) with N-formimidoyl-L-glutamate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HU77 plus reconstructed variant E235A and applied mutation signature E235A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant E235A (Zn2+)


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HU77 plus reconstructed variant E235D and applied mutation signature E235D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: formimidoylglutamate deiminase(Enzyme) mutant E235D (Zn2+)


organism: Acanthamoeba castellanii

substrate_name: P1,P3-bis(5'-adenosyl) triphosphate with CF2-bridge between P1 and P2

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


organism: Dolichospermum flos-aquae


organism: Euglena gracilis

substrate_name: phosphate

substrate: phosphate


organism: Saccharomyces cerevisiae

substrate_name: ADP

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
ADP/phosphate-exchange, pH 7.0, 37°C
pH 8.2, 37°C
pH 5.9, 37°C

substrate: ADP


organism: Tetradesmus obliquus

proof_lines: P1,P4-bis(5-adenosyl) tetraphosphate-phosphorolysis, pH 8.0, 25°C

proof_lines: P1,P4-bis(5-adenosyl) tetraphosphate-arsenolysis, pH 7.4, 25°C


substrate_name: N-formimino-L-methionine

proof_lines: Zn2+ has been reconstituted with Cu2+, pH 8.0, 30°C

proof_lines: Zn2+ has been reconstituted with Ni2+, pH 8.0, 30°C

substrate: N-formimino-L-methionine


substrate_name: N-formimino-L-glutamate

substrate: N-formimino-L-glutamate


substrate_name: arachidonate


proof_lines: recombinant His-tagged mutant A620H, pH 7.4, 22°C


sequence_source: UniProtKB O16025 direct REST check on 2026-06-15

proof_lines: recombinant His-tagged wild-type enzyme, pH 7.4, 22°C


sequence_variant_note: Resolved canonical sequence from UniProtKB O16025 direct REST check with R182A reconstruction on 2026-06-15 and applied mutation signature R182A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R182A, pH 7.4, 22°C


proof_lines: recombinant His-tagged mutant A589M, pH 7.4, 22°C


proof_lines:
Raw SKiD Env: Temp=22°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----


organism: Escherichia coli

substrate_name: ATP; NADH

assay_conditions_summary: cofactor NADPH

proof_lines: SABIO-RK modifier species: NADH kinase(Enzyme) mutant R175G

substrate: ATP; NADH


organism: Micrococcus luteus

substrate_name: Tetrapolyphosphate; NADH

substrate: Tetrapolyphosphate; NADH


proof_lines: SABIO-RK modifier species: NADH kinase(Enzyme) mutant G183R


substrate_name: NADH

substrate: NADH