organism: Tetrahymena pyriformis

substrate_name: ATP

sequence_source: UniProtKB U3T2Y2 direct accession lookup on 2026-06-28

proof_lines: pH 8.0, 25°C, recombinant His6-tagged isozyme AK2

substrate: ATP


enzyme_display_name: arginine kinase

source_db: oed

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

enzyme: arginine kinase

source: oed


organism: Toxocara canis

substrate_name: L-Arg

source_db: brenda

protein_accession_database: UniProt

sequence_source: UniProtKB A7YVI5 direct accession lookup on 2026-06-28

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

proof_lines: in 100 mM Tris-HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate, 5 mM NADH, at 25°C

substrate: L-Arg

source: brenda


organism: Tribolium castaneum

substrate_name: L-Arginine

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: L-Arginine


substrate_name: Nomega-phospho-L-arginine

substrate: Nomega-phospho-L-arginine


organism: Trypanosoma brucei brucei

kcat_display: Not reported

sequence_source: UniProtKB Q38EV2 direct accession lookup on 2026-06-28

assay_conditions_summary: pH 7.5; 301.15 K; cofactor ATP

proof_lines:
pH 7.5, 28°C, recombinant isozyme AK1
pH 7.5, 37°C, recombinant isozyme AK1


organism: Trypanosoma cruzi

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

sequence_source: UniProtKB O96507 direct accession lookup on 2026-06-28

assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 7.3
pH 7.3, 30°C
Raw SKiD Env: Temp=30°C, pH=7.3

source_databases_merged: brenda skid


organism: Abyssogena kaikoi

sequence_source: UniProtKB REST direct accession lookup Q4AEC4; primary=Q4AEC4; retrieved 2026-06-28

assay_conditions_summary: cofactor ATP


organism: Anthopleura japonica

km_display: Not reported

sequence_source: UniProtKB REST direct accession lookup O15992; primary=O15992; retrieved 2026-06-28

proof_lines: recombinant wild-type enzyme with MBP tag. The intact 2D/wild-type enzyme has a higher catalytic constant than the isolated domains


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Ascaris suum

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28 and applied mutation signature A105S to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28 and applied mutation signature A105S/S106G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28

proof_lines: mutant enzyme A105S, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


proof_lines: mutant enzyme A105S/S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


proof_lines: recombinant wild type enzyme, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup D5FLG2; primary=D5FLG2; retrieved 2026-06-28 and applied mutation signature S106G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S106G, in 4.76 mM Tris-HCl (pH 8.0), at 25°C


organism: Caenorhabditis elegans

sequence_source: UniProtKB REST direct accession lookup Q10454; primary=Q10454; retrieved 2026-06-28


sequence_source: UniProtKB REST direct accession lookup O45011; primary=O45011; retrieved 2026-06-28


sequence_source: UniProtKB REST direct accession lookup O45518; primary=O45518; retrieved 2026-06-28


sequence_source: UniProtKB REST direct accession lookup Q27535; primary=Q27535; retrieved 2026-06-28


enzyme_display_name: Arginine kinase

organism: Limulus polyphemus

substrate_name: L-Arginine phosphate

verification_status: verified

smiles: NC(=NCCCC(N)C(=O)O)NP(=O)(O)O

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

column_label: Table 3, construct row 'Wild type'; column 'kcat (s-1) (% wild type)' = 180; column 'KM (phospho-arginine), mM' = 0.17; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 180 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 180.0 s^(-1). Km: printed Table 3 cell 0.17 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.17 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 1058.8235294117646 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 180.0 / 0.17 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'Wild type': kcat = 180 s-1; KM (phospho-arginine) = 0.17 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'Wild type'

table_label: Table 3: Kinetic analysis of site directed mutants of Limulus arginine kinase in the specificity loops (Protein Science 2004, 13:575-585)

enzyme: Arginine kinase

substrate: L-Arginine phosphate

status: verified


substrate_name: ADP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature L61P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor ADP

column_label: Table 3, construct row 'L61P'; column 'kcat (s-1) (% wild type)' = 78; column 'KM (ADP), mM' = 0.018; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 78 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 78.0 s^(-1). Km: printed Table 3 cell 0.018 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.018 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 4333.333333333334 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 78.0 / 0.018 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'L61P': kcat = 78 s-1; KM (ADP) = 0.018 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'L61P'

substrate: ADP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature K16G to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'K16G'; column 'kcat (s-1) (% wild type)' = 2.00; column 'KM (ADP), mM' = 0.084; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.00 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 2.0 s^(-1). Km: printed Table 3 cell 0.084 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.084 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 23.809523809523807 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.0 / 0.084 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'K16G': kcat = 2.00 s-1; KM (ADP) = 0.084 mM; Table 3 prints no kcat/Km cell for this row.

row_label: Table 3, construct row 'K16G'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51541 and applied mutation signature R312G/E314V/H315D/E317A/E319V to reconstruct the assayed variant sequence.

column_label: Table 3, construct row 'R312G/E314V/H315D/E317A/E319V'; column 'kcat (s-1) (% wild type)' = 116; column 'KM (ADP), mM' = 0.08; Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 116 s-1; already in s^-1, no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 116.0 s^(-1). Km: printed Table 3 cell 0.08 mM; already in mM, no unit conversion applies (this paper prints no micromolar kinetic cell); the paper value is 0.08 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 1450.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 116.0 / 0.08 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, construct row 'R312G/E314V/H315D/E317A/E319V': kcat = 116 s-1; KM (ADP) = 0.08 mM; Table 3 prints no kcat/Km cell for this row.


organism: Locusta migratoria manilensis

substrate_name: L-arginine

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

substrate: L-arginine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: mutant enzyme L113G, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L113K, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L113D, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L113I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L113I, in 100 mM Tris, pH 8.0, at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T273A to reconstruct the assayed variant sequence.


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


organism: Lucilia cuprina

proof_lines: recombinant enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C

proof_lines: native enzyme, in 50 mM Tris–HCl pH 7.5, at 22°C


enzyme_display_name: Arginine kinase Met e 2

organism: Metapenaeus ensis

substrate_name: ATP; L-Arginine

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

enzyme: Arginine kinase Met e 2

substrate: ATP; L-Arginine


organism: Nautilus pompilius


organism: Neocaridina denticulata

proof_lines:
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 20°C, recombinant enzyme
pH 8.0, 15°C, recombinant enzyme


assay_conditions_summary: pH 8; 290.65 K; cofactor ATP

proof_lines:
pH 8.0, 17.5°C, recombinant enzyme
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 30°C, recombinant enzyme


organism: Octopus vulgaris


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


organism: Polybetes pythagoricus

proof_lines:
pH 8.6, 30°C
Raw SKiD Env: Temp=30°C, pH=8.6


verification_status: unverified

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

status: unverified


organism: Sabellastarte spectabilis


organism: Sepioteuthis lessoniana


organism: Teladorsagia circumcincta

proof_lines: pH 7.5, 30°C, recombinant His-tagged enzyme


organism: Tetrahymena pyriformis

proof_lines: pH 8.0, 25°C, recombinant His6-tagged isozyme AK1


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


enzyme_display_name: thioredoxin-disulfide reductase (NADPH)

organism: Bos taurus

substrate_name: thioredoxin

source_db: uniprot

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

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1200 sec(-1) with thioredoxin as substrate.

enzyme: thioredoxin-disulfide reductase (NADPH)

substrate: thioredoxin

source: uniprot


organism: Drosophila melanogaster

substrate_name: NADPH (at pH 7.4)

proof_lines: Measurements were conducted with isoform A unless noted otherwise.

substrate: NADPH (at pH 7.4)


organism: Homo sapiens

proof_lines: kcat is 100 min(-1) with H2O2 as substrate.


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: TRX1 (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: kcat is 1725 min(-1) with TRX1 as substrate (at pH 7.4) (PubMed:23845423). kcat is 51.7 sec(-1) with TRX1 as substrate (at 25 degrees Celsius and at pH 7.4) (PubMed:23845423). kcat is 275.2 min(-1) with NADPH and DTNB as substrates (at pH 7

substrate: TRX1 (at pH 7.4)


organism: Rattus norvegicus

proof_lines: kcat is 2500 min(-1) with thioredoxin as substrate.


enzyme_display_name: deoxycytidine kinase

organism: Gallus gallus

substrate_name: deoxyguanosine

proof_lines: kcat is 0.67 sec(-1) with deoxyguanosine as substrate. kcat is 0.52 sec(-1) with deoxycytidine as substrate. kcat is 2.56 sec(-1) with deoxyadenosine as substrate. kcat is 0.53 sec(-1) with deoxyuridine as substrate. kcat is 0.26 sec(-1) wi

enzyme: deoxycytidine kinase

substrate: deoxyguanosine


substrate_name: deoxycytidine

proof_lines: kcat is 0.05 sec(-1) with deoxycytodine as substrate. kcat is 4.07 sec(-1) with deoxyadenosine as substrate. kcat is 1.23 sec(-1) with deoxyguanosine as substrate. kcat is 1.05 sec(-1) with deoxyuridine as substrate. kcat is 1.08 sec(-1) wi

substrate: deoxycytidine


organism: Xenopus laevis

proof_lines: kcat is 1.26 sec(-1) with deoxyguanosine as substrate. kcat is 4.87 sec(-1) with deoxyadenosine as substrate. kcat is 0.42 sec(-1) with deoxycytidine as substrate. kcat is 0.36 sec(-1) with deoxyuridine as substrate. kcat is 0.14 sec(-1) wi


proof_lines: kcat is 0.09 sec(-1) with deoxycytodine as substrate. kcat is 3.40 sec(-1) with deoxyguanosine as substrate. kcat is 2.73 sec(-1) with deoxyadenosine as substrate. kcat is 0.29 sec(-1) with deoxythymidine as substrate. kcat is 1.27 sec(-1)


enzyme_display_name: peptide deformylase

organism: Arabidopsis thaliana

substrate_name: N-Formyl-Met-Ala-Ser

sequence_source: UniProtKB reviewed accession Q9FV53; direct REST lookup 2026-06-28

enzyme: peptide deformylase

substrate: N-Formyl-Met-Ala-Ser


sequence_source: UniProtKB reviewed accession Q9FUZ2; direct REST lookup 2026-06-28


substrate_name: H2O; Formyl-L-methionyl peptide

proof_lines: at 37°C, pH not specified in the publication

substrate: H2O; Formyl-L-methionyl peptide


substrate_name: N-Formyl-Met-Ser-Asn-Glu

substrate: N-Formyl-Met-Ser-Asn-Glu


substrate_name: N-Formyl-Nle-Ala-Ser

substrate: N-Formyl-Nle-Ala-Ser


substrate_name: N-Formyl-Nva-Ala-Ser

smiles: CCCC(N=CO)C(O)=NC(C)C(O)=NC(CO)C(=O)O

substrate: N-Formyl-Nva-Ala-Ser


substrate_name: N-Formyl-Met-Leu-Phe

substrate: N-Formyl-Met-Leu-Phe


substrate_name: N-Formyl-Met-Leu-Glu

substrate: N-Formyl-Met-Leu-Glu


substrate_name: Formyl-L-methionyl peptide

smiles: CSCCC(NC=O)C(=O)O

substrate: Formyl-L-methionyl peptide


substrate_name: N-Formyl-Phe-Ala-Ser

substrate: N-Formyl-Phe-Ala-Ser


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


smiles: CCCCC(N=CO)C(O)=NC


sequence_source: UniProtKB:Q9FV53 canonical sequence retrieved by direct accession lookup on 2026-06-28


substrate_name: Formyl-L-methionyl peptide; H2O

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

substrate: Formyl-L-methionyl peptide; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9FV53 canonical sequence retrieved by direct accession lookup on 2026-06-28 and applied mutation signature L91E to reconstruct the assayed variant sequence.


substrate_name: H2O; N-Formyl-Met-Leu-p-nitroanilide

sequence_source: UniProtKB:Q9FUZ2 canonical sequence retrieved by direct accession lookup on 2026-06-28

substrate: H2O; N-Formyl-Met-Leu-p-nitroanilide


organism: Escherichia coli

sequence_source: UniProtKB:P0A6K3 canonical sequence retrieved by direct accession lookup on 2026-06-28


substrate_name: formyl-Met-Ala-Ser

substrate: formyl-Met-Ala-Ser


substrate_name: N-Formyl-Met-Leu

substrate: N-Formyl-Met-Leu


substrate_name: N-Formyl-L-methionine

substrate: N-Formyl-L-methionine


substrate_name: H2O; N-Formyl-L-methionine

assay_conditions_summary: pH 4.5; 310.15 K; buffer 50 mM potassium phosphate

proof_lines: pH 4.5, 37°C, recombinant enzyme with bound Ni2+

proof_lines: pH 4.5, 37°C, recombinant enzyme with bound Zn2+

proof_lines: in 50 mM potassium phosphate buffer, pH 7.0, temperature not specified in the publication

substrate: H2O; N-Formyl-L-methionine


organism: Helicobacter pylori

sequence_source: UniProtKB:Q672W7 canonical sequence retrieved by direct accession lookup on 2026-06-28


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 canonical sequence retrieved by direct accession lookup on 2026-06-28 and applied mutation signature E91M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9HBH1 canonical sequence retrieved by direct accession lookup on 2026-06-28

proof_lines: pH and temperature not specified in the publication


substrate_name: N-formyl-Met-Leu-rho-nitroanilide

substrate: N-formyl-Met-Leu-rho-nitroanilide


sequence_source: UniProtKB:Q9HBH1 direct accession check

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature E91A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature S47A/E91L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9HBH1 canonical context only; row-specific variant unresolved


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature E91L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9HBH1 direct accession check and applied mutation signature S47A to reconstruct the assayed variant sequence.


organism: Leptospira interrogans

substrate_name: N-formyl-Met-Ala-Ser

sequence_source: UniProtKB:Q93LE9 direct accession check

substrate: N-formyl-Met-Ala-Ser


organism: Mycobacterium tuberculosis

substrate_name: N-formyl-Met-Ala

sequence_source: UniProtKB:P9WIJ3 direct accession check

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WIJ3 direct accession check and applied mutation signature M145C to reconstruct the assayed variant sequence.

smiles: CSCCC(N=CO)C(O)=NC(C)C(=O)O

substrate: N-formyl-Met-Ala


proof_lines: pH 7.0, 30°C, recombinant enzyme mutant M145C


proof_lines: pH 7.0, 30°C, recombinant wild-type enzyme


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_source: UniProtKB:Q8ZLM7 direct accession check


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8ZLM7 direct accession check and applied mutation signature C130M/V63C to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, recombinant enzyme mutant C130M/V63C


organism: Solanum lycopersicum

sequence_source: UniProtKB:Q9FUZ0 direct accession check


substrate_name: 5,5'-dithiobis(2-nitrobenzoic acid)

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

substrate: 5,5'-dithiobis(2-nitrobenzoic acid)


substrate_name: Lipoamide

assay_conditions_summary: pH 8; 310.15 K; cofactor NADPH

proof_lines: isoform TrxR1, in 50 mM Tris-HCl, 1 mM EDTA, pH 8.0, at 37°C

proof_lines: TrxR-16, TrxR lacking the last 16 C-terminal amino acids

substrate: Lipoamide


organism: Hordeum vulgare

substrate_name: Hordeum vulgare thioredoxin disulfide h2

proof_lines:
pH 5.7, HvNTR2
pH 7.4, HvNTR1
pH 5.7, HvNTR1


organism: Medicago truncatula


organism: Meleagris gallopavo

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 323.15 K; cofactor NADPH

substrate: NADPH


organism: Methanosarcina acetivorans

proof_lines: cosubstrate: 5,5-dithiobis(2-nitrobenzoic acid), pH and temperature not specified in the publication

proof_lines: Methanosarcina acetivorans thioredoxin 7, cosubstrate: NADPH, pH and temperature not specified in the publication


organism: Mus musculus

substrate_name: thioredoxin

proof_lines: Escherichia coli thioredoxin as substrate

substrate: thioredoxin


mutation_type: truncation

assay_conditions_summary: pH 7

proof_lines: truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0


proof_lines: wild type enzyme, in 50 mM potassium phosphate at pH 7.0


organism: Plasmodium berghei

substrate_name: dithionitrobenzene

substrate: dithionitrobenzene


organism: Plasmodium falciparum

substrate_name: methylseleninate

substrate: methylseleninate


substrate_name: DTNB

substrate: DTNB


substrate_name: H2O; Formyl-L-methionyl peptide

sequence_source: UniProtKB reviewed accession Q9FUZ0 FASTA

substrate: H2O; Formyl-L-methionyl peptide


substrate_name: Formyl-L-methionyl peptide; H2O

sequence_source: UniProtKB reviewed accession Q9FV54 FASTA

substrate: Formyl-L-methionyl peptide; H2O


organism: Staphylococcus epidermidis

substrate_name: N-formyl-L-Met-L-Ala-L-Ser

sequence_source: UniProtKB reviewed accession Q5HQ78 FASTA

proof_lines: Co2+-substituted PDF-1, in 50 mM HEPES, pH 7.5, at 37°C

substrate: N-formyl-L-Met-L-Ala-L-Ser


organism: Streptococcus agalactiae

substrate_name: Unknown

ki_unit: mM

sequence_source: UniProtKB reviewed accession Q8E378 FASTA

substrate: Unknown


organism: Vibrio phage VP16T

substrate_name: formyl-Met-Ala-Ser

substrate: formyl-Met-Ala-Ser


proof_lines: pH 7.5, 37°C, recombinant enzyme with bound Zn2+, Zn-Vp16 PDF1B

proof_lines: pH 7.5, 37°C, recombinant enzyme with bound Ni2+, Ni-Vp16 PDF1B


organism: Drosophila melanogaster


organism: Entamoeba histolytica

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

proof_lines: with NADH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C

proof_lines: with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 2 mM EDTA at 30°C


organism: Escherichia coli

substrate_name: glutaredoxin 4

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: pH 7.5, temperature not specified in the publication

substrate: glutaredoxin 4


substrate_name: thioredoxin-R

assay_conditions_summary: pH 8

proof_lines: chimeric enzyme mutant, partly from Salmonella typhimurium AhpF protein

proof_lines: substrate mutant, thioredoxin-CAC, pH 8.0

substrate: thioredoxin-R


proof_lines: substrate wild-type, thioredoxin P34S, pH 8.0


organism: Haemonchus contortus

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH


organism: Homo sapiens


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: wild type enzyme, 10 mM potassium phosphate buffer (pH 7.0) containing 10 mM EDTA, at 25°C


enzyme_display_name: pyruvate kinase

organism: Bos taurus

substrate_name: Phosphoenolpyruvate; ADP

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

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Ricinus communis

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ADP

proof_lines: 2 isozymes with different kinetic mechanisms


organism: Spinacia oleracea

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


organism: Unknown

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: N-formylmethionyl-Leu-p-nitroanilide

substrate: N-formylmethionyl-Leu-p-nitroanilide


enzyme_display_name: beta-lactamase

substrate_name: H2O; Cephalothin

enzyme: beta-lactamase

substrate: H2O; Cephalothin


organism: Apostichopus japonicus

substrate_name: L-Arg

substrate: L-Arg


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C


assay_conditions_summary: 298.15 K; cofactor ATP


proof_lines: mutant enzyme D57A, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme Q53E, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme Q53A, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme Q53A/D57A, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme D57E, in 100 mM Tris, pH 8.0, at 30°C


organism: Cissites cephalotes

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Corbicula japonica

proof_lines:
25°C, D197G mutant of domain 2
37°C, D197G mutant enzyme of domain 2


proof_lines:
25°C, H60R mutant of domain 2
37°C, H60R mutant of domain 2


organism: Triticum aestivum

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6.2; 303.15 K; cofactor ADP


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: Toxoplasma gondii

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


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP


organism: Abyssogena kaikoi

proof_lines: isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 10°C

proof_lines: two-domain enzyme, in 100 mM Tris-HCl (pH 8.0), at 25°C

proof_lines: isolated domain 2, in 100 mM Tris-HCl (pH 8.0), at 25°C


organism: Anthopleura japonica

proof_lines: mutant two-domain-enzyme D1-Lys6-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C


proof_lines: mutant two-domain-enzyme D1(Y68G)-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C

proof_lines: mutant two-domain-enzyme D1-D2(Y68G), in 100 mM Tris/HCl, pH 8.0 at 25°C


proof_lines: wild type one-domain-enzyme D1, in 100 mM Tris/HCl, pH 8.0 at 25°C

proof_lines: wild type one-domain-enzyme D2, in 100 mM Tris/HCl, pH 8.0 at 25°C

proof_lines: wild type two-domain-enzyme D1-D2, in 100 mM Tris/HCl, pH 8.0 at 25°C


mutation_type: delins


substrate_name: L-arginine

assay_conditions_summary: pH 8.1; cofactor ATP

substrate: L-arginine


organism: Anopheles gambiae

substrate_name: 5,5'-dithiobis(2-nitrobenzoic acid)

proof_lines: thioredoxin-2 from Drosophila melanogaster, pH 7.4

proof_lines: thioredoxin-1 from Anopheles gambiae, pH 7.4

substrate: 5,5'-dithiobis(2-nitrobenzoic acid)


organism: Arabidopsis thaliana

substrate_name: thioredoxin

substrate: thioredoxin


proof_lines:
thioredoxin from E. coli
human thioredoxin
E. coli thioredoxin


organism: Caenorhabditis elegans

assay_conditions_summary: pH 7

proof_lines: thioredoxin from Escherichia coli, wild type enzyme

proof_lines: wild type enzyme, in 50 mM potassium phosphate at pH 7.0


proof_lines: thioredoxin from Escherichia coli, mutant TR-GCCS

proof_lines: thioredoxin from Escherichia coli, mutant TR-SCCS


proof_lines: truncated thioredoxin reductase missing its final eight amino acids, in 50 mM potassium phosphate at pH 7.0


organism: Cereibacter sphaeroides

substrate_name: reductase

substrate: reductase


organism: Corynebacterium nephridii

substrate_name: thioredoxin C-2

substrate: thioredoxin C-2


organism: Drosophila melanogaster

substrate_name: methylseleninate

proof_lines:
recombinant protein
pH 7, 25°C
mitochondrial TrxR1 isoform

substrate: methylseleninate


mutation_signature: truncated thioredoxin reductase missing its final eight amino acids


organism: Plasmodium falciparum

substrate_name: DTNB

substrate: DTNB


organism: Rattus norvegicus

proof_lines: SeC498C mutant enzyme, human thioredoxin


proof_lines: wild-type enzyme, Km-value can be reduced by addition of selenocysteine


proof_lines: substrate: thioredoxin from calf and rat


substrate_name: thioredoxin 3

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

substrate: thioredoxin 3


substrate_name: thioredoxin 2

proof_lines: mutant enzyme K137A, pH and temperature not specified in the publication

substrate: thioredoxin 2


organism: Schistosoma mansoni

assay_conditions_summary: pH 7; 298.15 K; buffer conditions

proof_lines: truncated recombinant enzyme (lacking the last two amino acids Sec597-Gly598), in 100 mM potassium phosphate pH 7.0, at 25°C


proof_lines: full length enzyme, in 100 mM potassium phosphate pH 7.0, at 25°C

proof_lines: full length enzyme, in 50 mM potassium phosphate pH 7.0, at 25°C


organism: Solanum lycopersicum

substrate_name: Insulin; Reduced thioredoxin

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: with NADPH as cosubstrate, in 50 mM potassium phosphate, pH 7.0, 1 mM EDTA, temperature not specified in the publication

substrate: Insulin; Reduced thioredoxin


organism: Spinacia oleracea


organism: Limulus polyphemus

substrate_name: ADP

sequence_source: NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context.

assay_conditions_summary: cofactor ADP

substrate: ADP


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E225D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E225Q/E314Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E314S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E225Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E314Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature E314D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI Protein/Swiss-Prot P51541.1 linked from PMID 12732621; PDB chains 1P50_A/1P52_A also link to the same paper context. and applied mutation signature R312G/E314V/H315D/E317A/E319V to reconstruct the assayed variant sequence.


organism: Locusta migratoria

substrate_name: Unknown

substrate: Unknown


organism: Locusta migratoria manilensis

substrate_name: ATP

assay_conditions_summary: pH 8.6; 303.15 K; cofactor ATP

substrate: ATP


proof_lines: pH 8.6, 30°C, recombinant arginine kinase


organism: Corbicula japonica

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

proof_lines:
25°C, domain 2
25°C, two-domain enzyme
37°C, domain 2


proof_lines:
25°C, H60G mutant of domain 2
37°C, H60G mutant of domain 2


organism: Crassostrea sp.

assay_conditions_summary: pH 7.9; 298.15 K; cofactor ATP


organism: Desulfotalea psychrophila

assay_conditions_summary: pH 8; 298.15 K; cofactor ADP


enzyme_display_name: peroxidase

organism: Aggregatibacter actinomycetemcomitans

sequence_source: UniProtKB exact accession A2A1C5

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

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: peroxidase


organism: Amphitrite ornata

sequence_source: UniProtKB exact accession Q9NAV8

proof_lines: 2,4,6-trichlorophenol, pH 7.0, temperature not specified in the publication

proof_lines: cosubstrate 2,2-azinobis(3-ethylbenzthiazoline-6-sulfonic acid), pH 7.0, temperature not specified in the publication


organism: Amycolatopsis sp.

sequence_source: UniProtKB exact accession K7N5M8

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


organism: Armoracia rusticana

substrate_name: H2O2; 2,4-Dichlorophenol

substrate: H2O2; 2,4-Dichlorophenol


smiles: OO


substrate_name: N-Acetyl-L-tryptophanamide

substrate: N-Acetyl-L-tryptophanamide


substrate_name: 2-Chloro-4-methoxyphenol; H2O2

substrate: 2-Chloro-4-methoxyphenol; H2O2


substrate_name: L-Dopa; H2O2

substrate: L-Dopa; H2O2


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


sequence_source: UniProtKB exact accession K7ZW57


sequence_source: UniProtKB exact accession K7ZWW6


sequence_source: UniProtKB exact accession K7ZW28


substrate_name: guaiacol

assay_conditions_summary: pH 5

proof_lines: mutant F143A, pH 5, temperature not specified in the publication

substrate: guaiacol


proof_lines: mutant F130A, pH 5, temperature not specified in the publication


proof_lines: mutant F130A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication


proof_lines: mutant F68A/F142A/ F143A/F179A, pH 5, temperature not specified in the publication


proof_lines: mutant F179A, pH 5, temperature not specified in the publication


proof_lines: mutant F68A, pH 5, temperature not specified in the publication


proof_lines: mutant F142A, pH 5, temperature not specified in the publication


proof_lines: wild-type isoform C, pH 5, temperature not specified in the publication


substrate_name: H2O2 / 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)

sequence_source: UniProtKB exact accession P00433


sequence_variant_note: Resolved canonical sequence from UniProtKB exact accession P00433 with reconstructed mature-chain substitutions and applied mutation signature N13D/N57S/N255D/N268D with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

substrate: H2O2 / 2,2'-azinobis(3-ethylbenzthiazoline-6-sulfonic acid)


substrate_name: 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid); H2O2 / 2,2'-Azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) / H2O2 / H2O / Oxidized 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulfonic acid) / Guaiacol; H2O2 / Guaiacol / Oxidized donor / 4-Cresol; H2O2 / 4-Cresol / 4-Methylcatechol


substrate_name: Guaiacol

substrate: Guaiacol


organism: Chromolaena odorata

substrate_name: pyrogallol

proof_lines: 30°C, pH 5.5, cosubstrate: pyrogallol, isoenzyme E5

proof_lines: 30°C, pH 5.5, cosubstrate: o-phenylenediamine, isoenzyme E5

substrate: pyrogallol


organism: Fagopyrum esculentum

substrate_name: ascorbic acid

proof_lines:
isoenzyme POX II
isoenzyme POX I

substrate: ascorbic acid


organism: Ficus carica

proof_lines: pH 5.5, temperature not specified in the publication, isoenzyme FP3

proof_lines: pH 5.5, temperature not specified in the publication, isoenzyme FP2

proof_lines: pH 5.5, temperature not specified in the publication, isoenzyme FP1


organism: Nicotiana tabacum

proof_lines:
isozyme Af
isozyme Cn


organism: Arabidopsis thaliana

substrate_name: phosphoenolpyruvate (for the phosphatase activity)


organism: Auricularia auricula-judae

substrate_name: 2,2'-azino-bis(3-ethylbenzthiazoline-6-sulphonic acid) (ABTS) (Dye-decolorizing peroxidase AauDyP1, at pH 4.5)


organism: Bubalus bubalis

substrate_name: 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (at pH 6.0 and 60 degrees Celsius)

assay_conditions_summary: pH 6


organism: Exidia glandulosa


organism: Mycena epipterygia


organism: Mycetinis scorodonius


organism: Sus scrofa

substrate_name: cloride

substrate: cloride


organism: Taiwanofungus camphoratus

substrate_name: veratryl alcohol

substrate: veratryl alcohol


proof_lines: cosubstrate 2,4,6-tribromophenol, pH 7.0, temperature not specified in the publication


organism: Anabaena sp.

substrate_name: Reactive Blue 5

substrate: Reactive Blue 5


substrate_name: 4-Methoxyphenol; H2O2

assay_conditions_summary: pH 7; 298.15 K; buffer potassium phosphate

proof_lines: in the presence of 25% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C

proof_lines: in the presence of 20% (v/v) 1-butyl-3-methylimidazolium tetrafluoroborate, in potassium phosphate buffer (20 mM, pH 7.0) at 25°C

substrate: 4-Methoxyphenol; H2O2


organism: Armoracia sp.


organism: Artocarpus heterophyllus

proof_lines: pH 6.0, temperature not specified in the publication, cosubstrate: gallic acid

proof_lines: pH 6.0, temperature not specified in the publication, cosubstrate: o-phenylenediamine


organism: Beta vulgaris

assay_conditions_summary: pH 5.5; 298.15 K; buffer 0.2 M sodium phosphate

proof_lines: at 25°C in 0.2 M sodium phosphate buffer (pH 6.0)


organism: Bjerkandera adusta

substrate_name: Pentachlorophenol

assay_conditions_summary: pH 4

proof_lines: pH 4, oxidative dehalogenation of pentachlorophenol

proof_lines: pH 4, oxidative dehalogenation of 3,5-dibromo-4-hydroxybenzonitrile

substrate: Pentachlorophenol


organism: Boucerosia umbellata


organism: Brassica napus

proof_lines: 25°C, pH 6.0, partially deglycosylated enzyme


organism: Brassica oleracea

substrate_name: H2O2; Guaiacol

proof_lines: membrane-bound isoform, pH not specified in the publication, temperature not specified in the publication

proof_lines: soluble isoform, pH not specified in the publication, temperature not specified in the publication

substrate: H2O2; Guaiacol


organism: Euphorbia characias

sequence_source: UniProtKB:Q6PQF2 canonical sequence fetched by exact accession lookup


organism: Homo sapiens

substrate_name: 3,3',5,5'-Tetramethylbenzidine; H2O2

sequence_source: UniProtKB:Q92626 canonical sequence fetched by exact accession lookup

substrate: 3,3',5,5'-Tetramethylbenzidine; H2O2


organism: Lepidium draba

sequence_source: UniProtKB:A0A076L8M7 canonical sequence fetched by exact accession lookup

proof_lines:
pH 6.5, 30°C, 300 mM glycine
pH 6.5, 30°C
pH 6.5, 30°C, 600 mM sorbitol


organism: Neisseria gonorrhoeae


organism: Pleurotus eryngii

sequence_source: UniProtKB:O94753 canonical sequence fetched by exact accession lookup

proof_lines:
24°C, pH 3, wild-type enzyme
24°C, pH 3.5, wild-type enzyme
24°C, pH 5, wild-type enzyme


substrate_name: Reactive Black 5

sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature P76H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
24°C, pH 3.5, mutant enzyme P76H
24°C, pH 3, mutant enzyme P76H
24°C, pH 5, mutant enzyme P76H

substrate: Reactive Black 5


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature W164S/P76H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature W164S with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature W164H with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94753 canonical sequence with row-specific mature-chain mutation reconstruction and applied mutation signature H232F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

proof_lines:
24°C, pH 3, mutant enzyme H232F
24°C, pH 3.5, mutant enzyme H232F
24°C, pH 5, mutant enzyme H232F


organism: Trachycarpus fortunei

sequence_source: UniProtKB:A0A0A0Y4H8 canonical sequence fetched by exact accession lookup

proof_lines:
pH 3.0, 23°C
Raw SKiD Env: Temp=23°C, pH=3


organism: Brassica oleracea var. capitata f. rubra

substrate_name: guaiacol


organism: Brassica rapa

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

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.01 M phosphate

proof_lines: native enzyme, in 0.01 M phosphate buffer at pH 7.5 and 25°C

proof_lines: pyromellitic dianhydride-modified enzyme, in 0.01 M phosphate buffer at pH 7.5 and 25°C


organism: Calotropis procera

substrate_name: o-Dianisidine

proof_lines: pH 6.0, temperature not specified in the publication

substrate: o-Dianisidine


organism: Camellia sinensis


organism: Capsicum annuum

assay_conditions_summary: pH 5; 298.15 K; buffer pH 5

proof_lines: in 50 mM sodium citrate buffer (pH 5.0), at 25°C


organism: Citrus jambhiri

assay_conditions_summary: pH 5.5; buffer 50 mM sodium acetate

proof_lines: in 50 mM sodium acetate buffer, at pH 5.5


organism: Commiphora gileadensis

proof_lines: pH 7.0, temperature not specified in the publication, immobilized enzyme (entrapped onto a carboxymethyl cellulose/Fe3O4 magnetic hybrid material)

proof_lines: pH 7.0, temperature not specified in the publication, soluble enzyme


organism: Coprinopsis cinerea

substrate_name: 2,2'-Dihydroxyazobenzene; H2O2

substrate: 2,2'-Dihydroxyazobenzene; H2O2


organism: Cucumis melo

substrate_name: 3,4-dihydroxyphenylacetic acid

proof_lines: for Cucumis melo L. cantalupensis cv. Charentais

proof_lines: for Cucumis melo L. inodorus cv. Amarillo

substrate: 3,4-dihydroxyphenylacetic acid


organism: Cucumis melo var. cantalupo


organism: Cucumis melo var. inodorus


organism: Cynara cardunculus

substrate_name: ferulic acid

proof_lines: covalently bound POD from artichoke leaves, apparent Km value

proof_lines: covalently bound POD from artichoke heads, apparent Km value

proof_lines: soluble POD from artichoke leaves, apparent Km value

substrate: ferulic acid


organism: Amycolatopsis sp. (strain ATCC 39116 / 75iv2)

substrate_name: ABTS

proof_lines: kcat is 87 sec(-1) for peroxidase activity with ABTS as substrate. kcat is 34 sec(-1) for peroxidase activity with Reactive Blue 5 as substrate. kcat is 0.38 sec(-1) for peroxidase activity with Reactive Black 5 as substrate. kcat is 68 sec

substrate: ABTS


organism: Zea mays

substrate_name: Unknown

substrate: Unknown


organism: Zinnia elegans

substrate_name: p-coumaryl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme)

proof_lines: The full glycosylation reduces the affinity of the enzyme for both p-coumaryl and coniferyl, but not sinapyl, alcohol.


substrate: p-coumaryl alcohol (in the presence of 10.2 uM H2O2, for a partially glycosylated enzyme)


organism: Armoracia rusticana


substrate_name: Guaiacol

substrate: Guaiacol


organism: Bacillus altitudinis

substrate_name: Sinapoylcholine

substrate: Sinapoylcholine


substrate_name: sinapate

substrate: sinapate


substrate_name: H2O2; Sinapate

substrate: H2O2; Sinapate


organism: Bos taurus

substrate_name: N-Acetyl-L-tryptophanamide

substrate: N-Acetyl-L-tryptophanamide


organism: Cucumis sativus

substrate_name: H2O2; 4-Methoxy-alpha-naphthol

substrate: H2O2; 4-Methoxy-alpha-naphthol


organism: Euphorbia characias


organism: Cytisus multiflorus


organism: Elais guineensis

substrate: guaiacol


organism: Elizabethkingia meningoseptica


organism: Escherichia coli

substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Fragaria vesca

assay_conditions_summary: pH 7; 298.15 K; buffer 0.01 M citrate phosphate

proof_lines: in 0.01 M citrate phosphate buffer (pH 7.0), at 25°C


organism: Fragaria x ananassa


organism: Glycine max


organism: Homo sapiens

substrate_name: Br-

substrate: Br-


organism: Ipomoea carnea

assay_conditions_summary: pH 8

proof_lines:
at pH 8.0
at pH 7.0
at pH 5.5


organism: Lepidium sativum

proof_lines: pH 6.0-7.5, 30°C, cationic peroxidase GCP1


organism: Lupinus albus

substrate_name: H2O2; Guaiacol

substrate: H2O2; Guaiacol


organism: Momordica charantia

substrate: o-Dianisidine


organism: Locusta migratoria manilensis

substrate_name: L-Arg

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: native wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C

proof_lines: recombinant wild type enzyme, in 100 mM Tris, pH 8.0, at 30°C

substrate: L-Arg


proof_lines: mutant enzyme I121K, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme I121L, in 100 mM Tris, pH 8.0, at 30°C


proof_lines: mutant enzyme I121D, in 100 mM Tris, pH 8.0, at 30°C


organism: Manduca sexta

substrate_name: L-(+)-(S)-canavanine

assay_conditions_summary: 310.15 K; cofactor ADP

substrate: L-(+)-(S)-canavanine


organism: Molpadia arenicola

assay_conditions_summary: cofactor ATP


organism: Musca domestica


organism: Myzostoma cirriferum

substrate_name: ATP

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


organism: Paracentrotus lividus

substrate_name: ADP

assay_conditions_summary: pH 6.7; 298.15 K; cofactor ADP

substrate: ADP


organism: Paramecium tetraurelia

substrate_name: L-arginine

proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, wild-type enzyme

proof_lines: 25°C, pH not specified in the publication, arginine kinase AK4, wild-type enzyme

proof_lines: 25°C, pH and temperature not specified in the publication, wild-type enzyme

substrate: L-arginine


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme Q80A

proof_lines: 25°C, pH and temperature not specified in the publication, mutant enzyme Q80A


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme V81A

proof_lines: 25°C, pH and temperature not specified in the publication, mutant enzyme V81A


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme Q80S


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme G298R


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme D77A


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme D78A


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK3, mutant enzyme S79A

proof_lines: 25°C, pH and temperature not specified in the publication, mutant enzyme S79A


proof_lines: 25°C, pH not specified in the publication, arginine kinase AK4, mutant enzyme R298G


organism: Penaeus chinensis

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM Tris-HCl

proof_lines: at 25°C in 50 mM Tris-HCl buffer (pH 7.0)

substrate: Unknown


organism: Periplaneta americana

proof_lines:
ADP in form of MgADP-
ATP in form of MgATP2-
with L-arginine as substrate


organism: Sabella pavonina

substrate_name: D-Arg

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP

proof_lines:
pH 8.5, 25°C
ATP in form of MgATP2-

substrate: D-Arg


organism: Sabellastarte spectabilis

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: the reaction mixture contains 100 mM Tris/HCl (pH 8), 750 mM KCl, 250 mM Mg-acetate, 25 mM phosphoenolpyruvate made up in 100 mM imidazole/HCl (pH 7), 5 mM NADH made up in Tris/HCl (pH 8), pyruvate kinase/lactate dehydrogenase mixture made


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: isoform AK2 mutant G54S, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant G54S, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant G54S, in 100 mM Tris/HCl (pH 8.0), at 25°C


proof_lines: isoform AK2 mutant Y89Q, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant Y89Q, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant Y89Q, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C


organism: Mycobacterium avium

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 7.0


organism: Neurospora crassa


organism: Oryza sativa

assay_conditions_summary: pH 6


organism: Ovis aries

substrate_name: SCN-

substrate: SCN-


organism: Pelargonium graveolens


organism: Persea americana

substrate_name: pyrogallol

substrate: pyrogallol


organism: Plasmodium falciparum

substrate_name: guaiacol


organism: Pleurotus ostreatus

substrate_name: sinapinic acid

substrate: sinapinic acid


organism: Prunus persica

assay_conditions_summary: pH 5; 298.15 K; buffer 50 mM sodium acetate

proof_lines: in the presence of chlorogenic acid, in 50 mM sodium acetate buffer (pH 5.0), at 25°C

proof_lines: in the presence of 4-methoxy-alpha-naphthol, in 50 mM sodium acetate buffer (pH 5.0), at 25°C


organism: Pyrococcus furiosus

substrate_name: rubredoxin

substrate: rubredoxin


organism: Raphanus sativus


organism: Raphanus sativus var. niger

proof_lines:
isoform PRB-B, pH 7, pH 7, 23°C
isoform PRB-A, pH 7, pH 7, 23°C


proof_lines: wild type enzyme isoform AK2, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: wild type isoform AK2, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: wild type enzyme isoform AK2, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C


assay_conditions_summary: pH 8; 298.15 K; buffer context; cofactor ATP

proof_lines: isoform AK2 mutant L64V, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant L64V, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant L64V, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C


proof_lines: isoform AK2 mutant L64I, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant L64I, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant L64I, in 100 mM Tris/HCl (pH 8.0), at 25°C


organism: Sulfurovum lithotrophicum

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

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


organism: Torpedo californica

substrate_name: ADP; L-Arginine phosphate

assay_conditions_summary: cofactor ADP

substrate: ADP; L-Arginine phosphate


organism: Tribolium castaneum


organism: Trypanosoma brucei

assay_conditions_summary: pH 8.6; 303.15 K; cofactor ATP

proof_lines: pH 8.6, 30°C, ATP as a variable substrate while L-arginine is fixed at 2 mM

proof_lines: pH 8.6, 30°C, L-arginine as a variable when ATP is fixed at 0.5 mM


organism: Trypanosoma cruzi

substrate_name: Unknown


organism: Arabidopsis thaliana

substrate_name: N-formyl-Met-Leu-Glu

proof_lines:
enzyme form PDF1A
enzyme form Ni-PDF1B
enzyme form PDF1B

substrate: N-formyl-Met-Leu-Glu


organism: Sclerocarya birrea


organism: Solanum betaceum


organism: Solanum melongena


organism: Sorghum bicolor

proof_lines:
presence of Ca2+, pH 5.5, 25°C
pH 5.5, 25°C


organism: Streptomyces lividans


organism: Triticum aestivum

proof_lines: 30°C, pH 5.0, reaction with o-phenylenediamine


organism: Vigna radiata

proof_lines: pH 5.5, temperature not specified in the publication


organism: Locusta migratoria manilensis


proof_lines: mutant enzyme I121G, in 100 mM Tris, pH 8.0, at 30°C


organism: Bacillus subtilis

substrate_name: N-formyl-Met-Ala-Ser

proof_lines:
enzyme YkrB
enzyme Def
cobalt-substituted enzyme

substrate: N-formyl-Met-Ala-Ser


organism: Borreliella burgdorferi


organism: Chlamydia trachomatis


proof_lines: mutant enzyme F134C/R137S, at pH 7.2 and 37°C


organism: Escherichia coli


substrate_name: N-formyl-phenylglycinol

proof_lines:
pH 7.2, 37°C
nickel-containing enzyme
pH 7.5, 37°C

substrate: N-formyl-phenylglycinol


substrate_name: N-formylmethionylleucyl-p-nitroanilide

proof_lines: recombinant mutant E133D Co2+-bound enzyme

substrate: N-formylmethionylleucyl-p-nitroanilide


substrate_name: N-formyl-L-Met-L-Val

mutation_signature: truncated zinc deformylase truncated zinc deformylase

substrate: N-formyl-L-Met-L-Val


mutation_signature: truncated cobalt deformylase truncated cobalt deformylase


mutation_signature: truncated Zn-PDF truncated Zn-PDF


mutation_signature: truncated Co-PDF truncated Co-PDF


organism: Haemophilus influenzae

substrate_name: formyl-Met-Ala-Ser

substrate: formyl-Met-Ala-Ser


organism: Homo sapiens

substrate_name: formyl-L-Met-Leu-p-nitroanilide

substrate: formyl-L-Met-Leu-p-nitroanilide


organism: Legionella pneumophila

proof_lines:
Ni2+ PdB
Zn2+ PdfC
Zn2+ PdfB


organism: Mycobacterium tuberculosis

substrate_name: N-formyl-L-Met-L-Ala

proof_lines: 19.7 nM calculated value for the Mycobacterium tuberculosis enzyme

substrate: N-formyl-L-Met-L-Ala


substrate_name: formyl-Met-Ala

substrate: formyl-Met-Ala


assay_conditions_summary: pH 7.4; buffer 20 mM phosphate

proof_lines: wild type enzyme, in 20 mM phosphate buffer, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme G49C, in 20 mM phosphate buffer, pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme G151A, in 20 mM phosphate buffer, pH 7.4, temperature not specified in the publication


assay_conditions_summary: pH 7.4; buffer phosphate

proof_lines: mutant enzyme G151D, in 20 mM phosphate buffer, pH 7.4, temperature not specified in the publication


organism: Solanum lycopersicum


organism: Staphylococcus aureus

proof_lines: pH 7.0, temperature not specified in the publication


organism: Streptococcus pneumoniae


organism: Trypanosoma cruzi

mutation_type: deletion

assay_conditions_summary: pH 7.5; 310.15 K; buffer KH2PO4

proof_lines: truncated PDF-1DeltaN37, in 50 mM KH2PO4, pH 7.5, at 37°C


organism: Aeromonas sobria

substrate_name: H2O; Imipenem

substrate: H2O; Imipenem


organism: Enterobacter cloacae

substrate_name: H2O; Nitrocefin

proof_lines: pH and temperature not specified in the publication

substrate: H2O; Nitrocefin


organism: Klebsiella pneumoniae

substrate_name: H2O; Benzylpenicillin

assay_conditions_summary: pH 6.8; 313.15 K; buffer 50 mM HEPES

substrate: H2O; Benzylpenicillin


proof_lines:
at 30°C
in 100 mM MES (pH 6.4)


organism: Stenotrophomonas maltophilia

substrate_name: Cefdinir; H2O

proof_lines:
30°C, pH 8.0
30°C, pH 8.0, uncompetitive
30°C, pH 8.0, competitive

substrate: Cefdinir; H2O


enzyme_display_name: methionine adenosyltransferase

organism: Methanocaldococcus jannaschii

substrate_name: L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y120W to reconstruct the assayed variant sequence.

assay_conditions_summary: 328.15 K; cofactor ATP

enzyme: methionine adenosyltransferase

substrate: L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y72W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q58605 reviewed canonical sequence, checked 2026-06-29


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y323W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y85W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y226W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y344W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y170W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y371W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y49W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y273W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y233W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 reviewed canonical sequence plus row-specific mutation reconstruction, checked 2026-06-29 and applied mutation signature W387F/Y267W to reconstruct the assayed variant sequence.


substrate_name: ATP

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

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP

substrate: ATP


organism: Mus musculus

sequence_source: UniProtKB:Q3THS6 reviewed canonical sequence, checked 2026-06-29

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

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


substrate_name: Phosphoenolpyruvate; ADP

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

sequence_source: UniProtKB reviewed accession P14618 (KPYM_HUMAN), direct REST lookup 2026-06-29

assay_conditions_summary: pH 8; 305.15 K; cofactor ATP

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

proof_lines: Zn2+ bound to the ADP-binding site of the free enzyme, pH 7.4, 37°C

source_databases_merged: sabio_rk brenda skid

substrate: Phosphoenolpyruvate; ADP


substrate_name: phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P14618 (KPYM_HUMAN), direct REST lookup 2026-06-29 plus residue-level G415R reconstruction from selected paper mention and applied mutation signature G415R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ADP

substrate: phosphoenolpyruvate


sequence_source: UniProtKB reviewed accession P30613 (KPYR_HUMAN), direct REST lookup 2026-06-29


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB reviewed accession P00549 (KPYK1_YEAST), direct REST lookup 2026-06-29

assay_conditions_summary: cofactor ATP


sequence_source: UniProtKB reviewed accession P52489 (KPYK2_YEAST), direct REST lookup 2026-06-29


assay_conditions_summary: pH 4.5; cofactor ATP


organism: Bacillus subtilis

substrate_name: ATP; H2O; L-Methionine

substrate: ATP; H2O; L-Methionine


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: in 100 mM Tris-Cl pH 8.0, 20 mM MgCl2, at 37°C


organism: Catharanthus roseus


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 9; 295.15 K; cofactor ATP

proof_lines:
22°C, pH 9.0
at pH 8.5 and 35°C


organism: Escherichia coli

substrate_name: L-Methionine; ATP; H2O

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

substrate: L-Methionine; ATP; H2O


substrate_name: tripolyphosphate

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

assay_conditions_summary: pH 8; cofactor ATP

proof_lines:
G6 mutant, tripolyphosphatase activity
G5 mutant, tripolyphosphatase activity
G8 mutant, tripolyphosphatase activity

substrate: tripolyphosphate


substrate_name: L-Methionine

substrate: L-Methionine


assay_conditions_summary: pH 8; 295.15 K; cofactor ATP


assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q3THS6 canonical sequence retrieved via UniProt REST 2026-06-29 and applied mutation signature S114A/I117A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S114A/I117A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q3THS6 canonical sequence retrieved via UniProt REST 2026-06-29 and applied mutation signature I117A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I117A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q3THS6 canonical sequence retrieved via UniProt REST 2026-06-29 and applied mutation signature Q113N/I117A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q113N/I117A, pH and temperature not specified in the publication


organism: Mycolicibacterium smegmatis

substrate_name: L-methionine; ATP

sequence_source: UniProtKB:Q7WYN1 canonical sequence retrieved via UniProt REST 2026-06-29

assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP

substrate: L-methionine; ATP


organism: Plasmodium falciparum

substrate_name: ATP; L-methionine

sequence_source: UniProtKB:Q7K6A4 canonical sequence retrieved via UniProt REST 2026-06-29; source row says mutant enzyme but does not name the mutation

assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP

substrate: ATP; L-methionine


sequence_source: UniProtKB:Q7K6A4 canonical sequence retrieved via UniProt REST 2026-06-29


organism: Pyrococcus furiosus

source_db: brenda;skid

sequence_source: UniProtKB:Q8TZW1 canonical sequence retrieved via UniProt REST 2026-06-29

assay_conditions_summary: pH 8; 353.15 K; cofactor ATP

proof_lines:
pH 8.0, 80°C
Raw SKiD Env: Temp=80°C, pH=8

source: brenda;skid


organism: Rattus norvegicus

substrate_name: ATP; methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13444 canonical sequence retrieved via UniProt REST 2026-06-29 and applied mutation signature C61S to reconstruct the assayed variant sequence.

proof_lines:
mutant C61S, presence of dithiothreitol
mutant C61S, presence of glutathione

substrate: ATP; methionine


sequence_source: UniProtKB:P13444 canonical sequence retrieved via UniProt REST 2026-06-29

proof_lines:
wild-type, presence of glutathione
wild-type, presence of dithiothreitol


substrate_name: methionine; ATP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P13444 canonical sequence retrieved via UniProt REST 2026-06-29 and applied mutation signature C35S to reconstruct the assayed variant sequence.

proof_lines:
mutant C35S, presence of glutathione
mutant C35S, presence of dithiothreitol

substrate: methionine; ATP


substrate_name: L-Methionine; ATP; H2O; L-Methionine; ATP; H2O; Diphosphate; S-Adenosyl-L-methionine; Phosphate


sequence_source: UniProtKB:P18298 canonical sequence retrieved via UniProt REST 2026-06-29

substrate: L-Methionine; ATP; H2O; L-Methionine; ATP; H2O; Diphosphate; S-Adenosyl-L-methionine; Phosphate


sequence_source: UniProtKB reviewed accession P0A817 direct check on 2026-06-29

proof_lines:
pH 8.0
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=37°C, pH=8


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P0A817 direct sequence check on 2026-06-29 and applied mutation signature I303V/I65V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P0A817 direct sequence check on 2026-06-29 and applied mutation signature I303V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P0A817 direct sequence check on 2026-06-29 and applied mutation signature I303V/I65V/L186V/N104K to reconstruct the assayed variant sequence.

proof_lines: pH 8, 37°C, mutant enzyme I303V/I65V/L186V/N104K


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P0A817 direct sequence check on 2026-06-29 and applied mutation signature I303V/I65V/L186V to reconstruct the assayed variant sequence.

proof_lines: pH 8, 37°C, mutant enzyme I303V/I65V/L186V


proof_lines: pH 8, 37°C, mutant enzyme I303V/I65V/L186 V/N104K


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


organism: Homo sapiens

proof_lines: one kinetic form of alpha-two subunit in the presence of beta subunit


substrate_name: S-(-)-methioninol

verification_status: corrected

sequence_source: UniProtKB reviewed accession P31153 direct check on 2026-06-29

column_label: Table 1 (Kinetic Parameters of Wild-Type hMAT2A and Mutants), hMAT2A variant row wild-type, substrate row L-metol; column kcat min^-1 = 11 ± 1.6; column Km uM = 2400 ± 1000; column kcat/Km min^-1 uM^-1 = 4.8 x 10^-3; column kcat/Km relative = 2.6 x 10^-2.

raw_value_unit_evidence: Table 1, hMAT2A variant row wild-type, substrate row L-metol: kcat = 11 ± 1.6 min^-1; Km = 2400 ± 1000 uM; printed kcat/Km = 4.8 x 10^-3 min^-1 uM^-1.

row_label: Table 1, hMAT2A variant row wild-type, substrate L-metol

table_label: Table 1: Kinetic Parameters of Wild-Type hMAT2A and Mutants (ACS Chem. Biol. 2020, 15(3), 695-705)

substrate: S-(-)-methioninol

status: corrected


column_label: Table 1 (Kinetic Parameters of Wild-Type hMAT2A and Mutants), hMAT2A variant row wild-type, substrate row L-Met; column kcat min^-1 = 26 ± 1.0; column Km uM = 140 ± 50; column kcat/Km min^-1 uM^-1 = 1.9 x 10^-1; column kcat/Km relative = 1.0; column selectivity index = 40.

raw_value_unit_evidence: Table 1, hMAT2A variant row wild-type, substrate row L-Met: kcat = 26 ± 1.0 min^-1; Km = 140 ± 50 uM; printed kcat/Km = 1.9 x 10^-1 min^-1 uM^-1.

row_label: Table 1, hMAT2A variant row wild-type, substrate L-Met


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P31153 direct sequence check on 2026-06-29 and applied mutation signature K289L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31153 and applied mutation signature K289L to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters of Wild-Type hMAT2A and Mutants), hMAT2A variant row K289L, substrate row L-Met; column kcat min^-1 = 0.8 ± 0.1; column Km uM = 780 ± 170; column kcat/Km min^-1 uM^-1 = 1.1 x 10^-3; column kcat/Km relative = 1.0; column selectivity index = -4.

raw_value_unit_evidence: Table 1, hMAT2A variant row K289L, substrate row L-Met: kcat = 0.8 ± 0.1 min^-1; Km = 780 ± 170 uM; printed kcat/Km = 1.1 x 10^-3 min^-1 uM^-1.

row_label: Table 1, hMAT2A variant row K289L, substrate L-Met


column_label: Table 1 (Kinetic Parameters of Wild-Type hMAT2A and Mutants), hMAT2A variant row K289L, substrate row L-metol; column kcat min^-1 = 4.1 ± 0.1; column Km uM = 1000 ± 130; column kcat/Km min^-1 uM^-1 = 4.1 x 10^-3; column kcat/Km relative = 3.8.

raw_value_unit_evidence: Table 1, hMAT2A variant row K289L, substrate row L-metol: kcat = 4.1 ± 0.1 min^-1; Km = 1000 ± 130 uM; printed kcat/Km = 4.1 x 10^-3 min^-1 uM^-1.

row_label: Table 1, hMAT2A variant row K289L, substrate L-metol


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed accession P31153 direct sequence check on 2026-06-29 and applied mutation signature Q113D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P13444 direct accession lookup on 2026-06-29


organism: Saccharolobus solfataricus

sequence_source: UniProtKB:Q980S9 direct accession lookup on 2026-06-29


substrate_name: L-ethionine

substrate: L-ethionine


proof_lines:
pH 8.0, 37°C
pH 8.0, 65°C
pH 8.0, 65°C, cosubstrate: L-methionine


sequence_source: UniProtKB:P19358 direct accession lookup on 2026-06-29

assay_conditions_summary: pH 8; 308.15 K; cofactor ATP


organism: Streptomyces avermitilis

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


organism: Thermococcus kodakarensis

sequence_source: UniProtKB:Q5JF22 direct accession lookup on 2026-06-29

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


organism: Thermus thermophilus

sequence_source: UniProtKB:Q72I53 direct accession lookup on 2026-06-29

assay_conditions_summary: pH 8; 343.15 K; cofactor ATP

proof_lines:
at pH 8.0 and 70°C
Raw SKiD Env: Temp=70°C, pH=8


enzyme_display_name: S-adenosylmethionine synthase isoform type-2

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P31153 and applied mutation signature Q113D to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic Parameters of Wild-Type hMAT2A and Mutants), hMAT2A variant row Q113D, substrate row L-Met; column kcat min^-1 = 1.2 ± 0.1; column Km uM = 47 ± 47; column kcat/Km min^-1 uM^-1 = 2.4 x 10^-2; column kcat/Km relative = 1.0; column selectivity index = 3.

raw_value_unit_evidence: Table 1, hMAT2A variant row Q113D, substrate row L-Met: kcat = 1.2 ± 0.1 min^-1; Km = 47 ± 47 uM; printed kcat/Km = 2.4 x 10^-2 min^-1 uM^-1.

row_label: Table 1, hMAT2A variant row Q113D, substrate L-Met


column_label: Table 1 (Kinetic Parameters of Wild-Type hMAT2A and Mutants), hMAT2A variant row Q113D, substrate row L-metol; column kcat min^-1 = 3.3 ± 0.1; column Km uM = 390 ± 70; column kcat/Km min^-1 uM^-1 = 8.6 x 10^-3; column kcat/Km relative = 3.5 x 10^-1.

raw_value_unit_evidence: Table 1, hMAT2A variant row Q113D, substrate row L-metol: kcat = 3.3 ± 0.1 min^-1; Km = 390 ± 70 uM; printed kcat/Km = 8.6 x 10^-3 min^-1 uM^-1.

row_label: Table 1, hMAT2A variant row Q113D, substrate L-metol

enzyme: S-adenosylmethionine synthase isoform type-2


sequence_source: UniProtKB:P31153 direct accession FASTA lookup on 2026-06-29

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
pH 8.0, 25°C
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----


enzyme_display_name: S-adenosylmethionine synthase

organism: Leishmania donovani

sequence_source: UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29

proof_lines:
tripolyphosphase activity
S-adenosylmethionine synthesis activity
L-methionine concentrations of 0.5-5 mM

enzyme: S-adenosylmethionine synthase


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature K256A to reconstruct the assayed variant sequence.

proof_lines: mutant K256A, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature H17A to reconstruct the assayed variant sequence.

proof_lines: mutant H17A, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature D19N to reconstruct the assayed variant sequence.

proof_lines: mutant D19N, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature D166N to reconstruct the assayed variant sequence.

proof_lines: mutant D166N, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature D282N to reconstruct the assayed variant sequence.

proof_lines: mutant D282N, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature D121N to reconstruct the assayed variant sequence.

proof_lines: mutant D121N, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature K280A to reconstruct the assayed variant sequence.

proof_lines: mutant K280A, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature D249N to reconstruct the assayed variant sequence.

proof_lines: mutant D249N, presence of 0.05 mM S-adenosyl methionine, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9U6Q8 direct accession FASTA lookup on 2026-06-29 and applied mutation signature H17N to reconstruct the assayed variant sequence.

proof_lines: mutant H17N, presence of 0.05 mM S-adenosyl methionine, pH 8.0


proof_lines: wild-type, presence of 0.05 mM S-adenosyl methionine, pH 8.0


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB:Q58605 direct accession FASTA lookup on 2026-06-29

assay_conditions_summary: pH 8; 331.15 K; cofactor ATP

proof_lines:
pH 8.0, 58°C
Raw SKiD Env: Temp=55°C, pH=-----
Raw SKiD Env: Temp=58°C, pH=8


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q58605 direct accession FASTA lookup on 2026-06-29 and applied mutation signature W387F/Y255W to reconstruct the assayed variant sequence.

assay_conditions_summary: 328.15 K; cofactor ATP


sequence_source: UniProt REST exact accession lookup P52489 on 2026-06-29

assay_conditions_summary: cofactor ADP


organism: Trichomonas vaginalis


organism: Trypanosoma brucei


organism: Ustilago maydis

sequence_source: UniProt REST exact accession lookup A0A0D1E735 on 2026-06-29


organism: Zymomonas mobilis

sequence_source: UniProt REST exact accession lookup Q5NR78 on 2026-06-29


organism: Pseudomonas aeruginosa

substrate_name: H2O; Penicillin G

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

sequence_source: UniProt REST exact accession lookup P16897 on 2026-06-29

substrate: H2O; Penicillin G


sequence_source: UniProt REST exact accession lookup Q3SAW3 on 2026-06-29

proof_lines:
30°C, pH 7.0
Raw SKiD Env: Temp=30°C, pH=7


organism: Mus musculus

substrate_name: Unknown

proof_lines:
isoenzyme II
isoenzyme I

substrate: Unknown


proof_lines:
S-adenosylmethionine synthesis
tripolyphosphatase activity
beta form from liver


proof_lines:
S-adenosylmethionine synthetase A
isoenzyme B
S-adenosylmethionine synthetase B


organism: Unknown

substrate_name: L-methionine

substrate: L-methionine


organism: Catharanthus roseus


organism: Escherichia coli (strain K12)


organism: Mammalia


organism: Saccharomyces cerevisiae


organism: Streptomyces xinghaiensis

substrate_name: ATP

assay_conditions_summary: pH 8.5; 328.15 K; buffer and pH 8; cofactor ATP

proof_lines:
pH 8.5, 55°C, Co2+ buffer
pH 8.5, 55°C, Mg2+/K+ buffer

substrate: ATP


organism: Trypanosoma brucei brucei


organism: Acacia koa

substrate_name: L-methionine (at 50 degrees Celsius)

proof_lines: kcat is 1.29 sec(-1) with L-methionine as substrate (at 50 degrees Celsius) (PubMed:38631157). kcat is 1.69 sec(-1) with L-methionine as substrate (at 35 degrees Celsius) (PubMed:38631157). Thermoalkaliphic enzyme which tolerates conditions

substrate: L-methionine (at 50 degrees Celsius)


organism: Bacteroides fragilis

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

proof_lines: pH 8.0, 37°C, mutant enzyme E42C/E55L/K290I


organism: Bos taurus

assay_conditions_summary: cofactor ATP


organism: Cryptosporidium parvum

sequence_source: UniProtKB:Q7Z0D0 direct PMID/title follow-up


organism: Escherichia coli

assay_conditions_summary: pH 8.5; 318.15 K; cofactor ATP

proof_lines: alpha subunit at high L-methionine concentrations. Also one kinetic form of alpha subunit in the presence of beta subunit


assay_conditions_summary: pH 9; 303.15 K; cofactor ATP


proof_lines:
mutant enzyme I303V, pH 9.0, 30°C
37°C, pH 8.0, mutant enzyme I303V


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
pH 8.0, 37°C, wild-type enzyme
wild-type enzyme, pH 9.0, 30°C
37°C, pH 8.0, wild-type enzyme


proof_lines: pH 8.0, 37°C, mutant enzyme E42R/E55L/K290I


proof_lines: pH 8.0, 37°C, mutant enzyme E42M/E55L/K290I


organism: Felis catus


organism: Homo sapiens


proof_lines: Q113A mutant, S-adenosylmethionine synthesis


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: uninduced E. coli NM522 strain extract alpha subunit at low L-methionine concentrations


organism: Lactiplantibacillus paraplantarum

assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP


organism: Lactiplantibacillus plantarum


organism: Lathyrus oleraceus


organism: Leishmania infantum

proof_lines: noncompetitive inhibition at 0.5-5 mM ATP concentrations


organism: Limosilactobacillus fermentum


organism: Limosilactobacillus reuteri


organism: Macaca mulatta


enzyme_display_name: carbonic anhydrase

assay_conditions_summary: pH 6.28; buffer conditions for carbonic anhydrase I mutant assays

proof_lines: pH 6.28, MES buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 8.98, TAPS buffer, carbonic anhydrase I mutant V62N,H67N,H200T

proof_lines: pH 7.23, 1-methylimidazolebuffer, carbonic anhydrase I mutant V62N,H67N,H200T

enzyme: carbonic anhydrase


organism: Methanosarcina thermophila

proof_lines: pH 7.5, 25°C, variant E84Q, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84D, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62H, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E89A, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84Y, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E84S, 50 mM MOPS buffer


proof_lines: pH 7.5, 25°C, variant E62T, 50 mM MOPS buffer


organism: Methanothermobacter thermautotrophicus

proof_lines: pH 8.5, 25°C, wild-type, imidazole buffer


enzyme_display_name: GDP-D-glucose phosphorylase

organism: Caenorhabditis elegans

substrate_name: GDP-D-glucose (at 26 degrees Celsius)

proof_lines: kcat is 265 sec(-1). The catalytic efficiency for GDP-D-glucose is 750-fold higher than for GDP-L-galactose.

enzyme: GDP-D-glucose phosphorylase

substrate: GDP-D-glucose (at 26 degrees Celsius)


substrate_name: GDP-D-glucose (at 31 degrees Celsius)

proof_lines: kcat is 26 sec(-1) at 31 degrees Celsius. The catalytic efficiency for GDP-D-glucose is 35-fold higher than for GDP-L-galactose.

substrate: GDP-D-glucose (at 31 degrees Celsius)


substrate_name: phosphate

smiles: O=P(O)(O)O

substrate: phosphate


substrate_name: GDP-alpha-D-glucose

substrate: GDP-alpha-D-glucose


enzyme_display_name: beta-glucosidase

organism: Acetivibrio thermocellus

enzyme: beta-glucosidase


organism: Agroathelia rolfsii

proof_lines:
beta-glucosidase 3
beta-glucosidase 1
beta-glucosidase 2


organism: Agrobacterium tumefaciens

proof_lines:
no change for chimeric enzymes
marked increase for chimeric enzyme


organism: Alternaria alternata

substrate_name: cellobiose

substrate: cellobiose


organism: Aspergillus fumigatus


organism: Aspergillus japonicus

proof_lines:
at pH 5.0 and 40°C
30°C, 5.0


organism: Fusarium proliferatum

substrate_name: ginsenoside Rg3

assay_conditions_summary: pH 5; 323.15 K; buffer NaAc/HAc

proof_lines: in NaAc/HAc buffer (0.2 M, pH 5.0), at 50°C

substrate: ginsenoside Rg3


organism: Saccharomyces cerevisiae

substrate_name: Phosphoenolpyruvate; ADP

sequence_source: UniProtKB reviewed accession P00549 (KPYK1_YEAST), direct UniProt REST/FASTA check

substrate: Phosphoenolpyruvate; ADP


sequence_source: UniProtKB reviewed accession P52489 (KPYK2_YEAST), direct UniProt REST/FASTA check


assay_conditions_summary: pH 4.5; cofactor ADP


organism: Amycolatopsis methanolica

sequence_source: UniProtKB REST exact accession lookup A0A076MW80; UniProtKB unreviewed (TrEMBL)


organism: Arabidopsis thaliana


organism: Bos taurus

sequence_source: UniProtKB REST exact accession lookup Q1JPG7; UniProtKB unreviewed (TrEMBL)


sequence_source: UniProtKB REST exact accession lookup B3IVN4; UniProtKB unreviewed (TrEMBL)


organism: Chlamydia trachomatis

sequence_source: UniProtKB REST exact accession lookup B0B7Q0; UniProtKB reviewed (Swiss-Prot)


organism: Corynebacterium glutamicum

sequence_source: UniProtKB REST exact accession lookup Q46078; UniProtKB reviewed (Swiss-Prot)


organism: Escherichia coli

sequence_source: UniProtKB REST exact accession lookup P0AD61; UniProtKB reviewed (Swiss-Prot)


organism: Homo sapiens

sequence_source: UniProtKB REST exact accession lookup P14618; UniProtKB reviewed (Swiss-Prot)

assay_conditions_summary: pH 8; 305.15 K; cofactor ATP

proof_lines: pH 8.0, 32°C, activation by 2 mM D-fructose-1,6-bisphosphate

proof_lines: Zn2+ bound to the ADP-binding site of the free enzyme, pH 7.4, 37°C


organism: Rattus norvegicus

sequence_source: UniProtKB REST exact accession lookup P12928; UniProtKB reviewed (Swiss-Prot)


sequence_source: UniProtKB REST exact accession lookup P11980; UniProtKB reviewed (Swiss-Prot)


organism: Ricinus communis

sequence_source: UniProtKB REST exact accession lookup Q43117; UniProtKB reviewed (Swiss-Prot)


enzyme_display_name: xylulokinase

organism: Escherichia coli (strain K12)

substrate_name: D-xylulose

proof_lines: kcat is 255 sec(-1) with D-xylulose as substrate. kcat is 235 sec(-1) with D-ribulose as substrate. kcat is 237 sec(-1) with xylitol as substrate. kcat is 105 sec(-1) with D-arabitol as substrate.

enzyme: xylulokinase

substrate: D-xylulose


organism: Klebsiella aerogenes


organism: Saccharococcus caldoxylosilyticus

proof_lines:
pH 8.0, 25°C
ATP in form of MgATP2-


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


organism: Scheffersomyces stipitis


organism: Toxoplasma gondii

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

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


substrate_name: D-xylulose (at pH 8)

assay_conditions_summary: pH 8

substrate: D-xylulose (at pH 8)


organism: Aspergillus niger


substrate_name: ATP; D-Xylulose

substrate: ATP; D-Xylulose


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_manual_mutation_reconstruction and applied mutation signature D6A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_manual_mutation_reconstruction and applied mutation signature D233A to reconstruct the assayed variant sequence.


substrate_name: D-arabitol

proof_lines:
in the presence of 5 mM ATP
in the presence of 0.167 mM ATP
in the presence of 0.28 mM xylulose

substrate: D-arabitol


organism: Halorhabdus utahensis


proof_lines: in 50 mM NH4HCO3, pH 8.0, 10% (v/v) D2O, 10 mM MgCl2 at 25°C


substrate_name: D-Xylulose

substrate: D-Xylulose


organism: Mucor circinelloides

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP


organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: (Polyphosphate)n

substrate: (Polyphosphate)n


enzyme_display_name: kojibiose phosphorylase

organism: Pyrococcus sp.

enzyme: kojibiose phosphorylase


organism: Citrus maxima

substrate_name: UDP-L-rhamnose; Prunin

sequence_source: UniProtKB REST exact accession lookup: Q8GVE3

substrate: UDP-L-rhamnose; Prunin


organism: Amycolatopsis orientalis

substrate_name: UDP-L-epi-vancosamine

sequence_source: UniProtKB REST exact accession lookup: Q9AFC7

substrate: UDP-L-epi-vancosamine


substrate_name: desvancosaminyl-vancomycin

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

substrate: desvancosaminyl-vancomycin


substrate_name: dTDP-beta-L-daunosamine

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

substrate: dTDP-beta-L-daunosamine


organism: Gardenia jasminoides

substrate_name: beta-D-glucosyl crocetin

sequence_source: UniProtKB REST exact accession lookup: F8WKW8

substrate: beta-D-glucosyl crocetin


substrate_name: bis(beta-D-glucosyl) crocetin

substrate: bis(beta-D-glucosyl) crocetin


organism: Panax ginseng

substrate_name: ginsenoside C-K

sequence_source: UniProtKB REST exact accession lookup: A0A0A6ZFR4

substrate: ginsenoside C-K


substrate_name: (20S)-ginsenoside Rh2

sequence_source: UniProtKB REST exact accession lookup: A0A0A6ZFY4

substrate: (20S)-ginsenoside Rh2


enzyme_display_name: taxadiene 5alpha-hydroxylase

organism: Taxus cuspidata

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: taxadiene 5alpha-hydroxylase


substrate_name: O2; Reduced acceptor; Taxa-4(5),11(12)-diene

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

assay_conditions_summary: cofactor NADPH


organism: Homo sapiens

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


substrate_name: Piceid

substrate: Piceid


substrate_name: H+; NADPH; Testosterone; O2

assay_conditions_summary: cofactor NADP+

substrate: H+; NADPH; Testosterone; O2


substrate_name: Resveratroloside

substrate: Resveratroloside


enzyme_display_name: ent-sandaracopimaradiene 3-hydroxylase

organism: Oryza sativa

substrate_name: ent-Cassa-12,15-diene; O2; H+; NADPH

enzyme: ent-sandaracopimaradiene 3-hydroxylase

substrate: ent-Cassa-12,15-diene; O2; H+; NADPH


enzyme_display_name: phenylacetonitrile alpha-monooxygenase

organism: Chamberlinius hualienensis

substrate_name: 3-methyl phenylacetonitrile

enzyme: phenylacetonitrile alpha-monooxygenase

substrate: 3-methyl phenylacetonitrile


substrate_name: 2-methyl phenylacetonitrile

substrate: 2-methyl phenylacetonitrile


substrate_name: phenylacetonitrile

substrate: phenylacetonitrile


enzyme_display_name: pentalenic acid synthase

organism: Streptomyces avermitilis

substrate_name: Compactin

enzyme: pentalenic acid synthase

substrate: Compactin


substrate_name: diclofenac

substrate: diclofenac


enzyme_display_name: isopenicillin-N synthase

organism: Cephalosporium acremonium

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C255S to reconstruct the assayed variant sequence.

enzyme: isopenicillin-N synthase


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C106S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C106S/C255S to reconstruct the assayed variant sequence.


enzyme_display_name: (-)-pinoresinol reductase

organism: Arabidopsis thaliana

substrate_name: (-)-pinoresinol

enzyme: (-)-pinoresinol reductase

substrate: (-)-pinoresinol


proof_lines:
at pH 7.5 and 30°C
Raw SKiD Env: Temp=30°C, pH=7.5


organism: Camellia sinensis var. sinensis


enzyme_display_name: NAD(P)H oxidase (H2O-forming)

organism: Thermococcus kodakarensis

substrate_name: NADH

assay_conditions_summary: pH 7.8; 348.15 K; cofactor NADH

enzyme: NAD(P)H oxidase (H2O-forming)

substrate: NADH


organism: Thermococcus profundus

substrate_name: NADPH

assay_conditions_summary: pH 7.2; 348.15 K; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 7.2; 348.15 K; cofactor NADH


enzyme_display_name: caffeoyl-CoA O-methyltransferase

substrate_name: eriodictyol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G46Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

enzyme: caffeoyl-CoA O-methyltransferase

substrate: eriodictyol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G46Y/W193F/R194M/I195K to reconstruct the assayed variant sequence.


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium hassiacum

sequence_variant_note: Resolved canonical sequence from UniProtKB:K5B7F3 canonical sequence with reviewed row-specific substitution H79A and applied mutation signature H79A to reconstruct the assayed variant sequence.

enzyme: MMP 1-O-methyltransferase


sequence_variant_note: Resolved canonical sequence from UniProtKB:K5B7F3 canonical sequence with reviewed row-specific substitution E78A and applied mutation signature E78A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:K5B7F3 canonical sequence with reviewed row-specific substitution E78A


enzyme_display_name: pinosylvin synthase

organism: Pinus sylvestris

substrate_name: Malonyl-CoA; Cinnamoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: pinosylvin synthase

substrate: Malonyl-CoA; Cinnamoyl-CoA


enzyme_display_name: demethoxycurcumin synthase

organism: Curcuma longa

enzyme: demethoxycurcumin synthase


enzyme_display_name: glycine C-acetyltransferase

organism: Escherichia coli

substrate_name: Glycine; Acetyl-CoA

enzyme: glycine C-acetyltransferase

substrate: Glycine; Acetyl-CoA


organism: Thermus thermophilus


enzyme_display_name: trehalose 6-phosphate phosphorylase

organism: Badhamia polycephala

substrate_name: alpha,alpha-trehalose 6-phosphate

enzyme: trehalose 6-phosphate phosphorylase

substrate: alpha,alpha-trehalose 6-phosphate


organism: Lactococcus lactis

substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


organism: Lactococcus lactis subsp. lactis

substrate_name: Phosphate; Trehalose 6-phosphate

substrate: Phosphate; Trehalose 6-phosphate


substrate_name: Phosphate; Kojibiose

substrate: Phosphate; Kojibiose


enzyme_display_name: gallate dioxygenase

organism: Sphingobium sp. SYK-6

substrate_name: gallate

proof_lines: at pH 7.5, temperature not specified in the publication

enzyme: gallate dioxygenase

substrate: gallate


enzyme_display_name: Gallate dioxygenase

organism: Sphingomonas paucimobilis

sequence_source: UniProtKB:Q5NTE5 direct exact accession lookup

assay_conditions_summary: pH 8.5; 303.15 K; buffer 50 mM GTA

proof_lines: in 50 mM GTA buffer (pH 8.5) consisting of 50 mM 3,3-dimethylglutarate, 50 mM Tris, and 50 mM 2-amino-2-methyl-1,3-propanediol, at 30°C

enzyme: Gallate dioxygenase


organism: Synechocystis sp.

substrate_name: O2; all-trans-8'-apo-beta-Carotenal

sequence_source: UniProtKB:P74334 direct exact accession lookup

substrate: O2; all-trans-8'-apo-beta-Carotenal


organism: Streptomyces coeruleorubidus

sequence_source: UniProtKB:A0A3B6UEU3 direct exact accession lookup

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: Methylxanthine N1-demethylase NdmA

organism: Pseudomonas putida

substrate_name: theophylline

sequence_source: UniProtKB:H9N289 direct exact accession lookup

column_label: Table 2. Kinetic parameters of NdmA and NdmB. Enzyme block 'NdmA-His6'; substrate row 'Theophylline'; product column '3-Methylxanthine'; column 'Km (uM)' = 9.1; column 'kcat (min^-1)' = 83; column 'kcat/Km (min^-1 uM^-1)' = 9.1.

raw_value_unit_evidence: Table 2, enzyme block 'NdmA-His6', substrate row 'Theophylline': Km = 9.1 uM; kcat = 83 min^-1; printed kcat/Km = 9.1 min^-1 uM^-1.

enzyme: Methylxanthine N1-demethylase NdmA

substrate: theophylline


substrate_name: Caffeine

column_label: Table 2. Kinetic parameters of NdmA and NdmB. Enzyme block 'NdmA-His6'; substrate row 'Caffeine'; product column 'Theobromine'; column 'Km (uM)' = 37; column 'kcat (min^-1)' = 190; column 'kcat/Km (min^-1 uM^-1)' = 5.1.

raw_value_unit_evidence: Table 2, enzyme block 'NdmA-His6', substrate row 'Caffeine': Km = 37 uM; kcat = 190 min^-1; printed kcat/Km = 5.1 min^-1 uM^-1.

substrate: Caffeine


substrate_name: paraxanthine

column_label: Table 2. Kinetic parameters of NdmA and NdmB. Enzyme block 'NdmA-His6'; substrate row 'Paraxanthine'; product column '7-Methylxanthine'; column 'Km (uM)' = 53; column 'kcat (min^-1)' = 130; column 'kcat/Km (min^-1 uM^-1)' = 2.5.

raw_value_unit_evidence: Table 2, enzyme block 'NdmA-His6', substrate row 'Paraxanthine': Km = 53 uM; kcat = 130 min^-1; printed kcat/Km = 2.5 min^-1 uM^-1.

substrate: paraxanthine


enzyme_display_name: Methylxanthine N3-demethylase NdmB

sequence_source: UniProtKB:H9N290 direct exact accession lookup

enzyme: Methylxanthine N3-demethylase NdmB


substrate_name: Theobromine

column_label: Table 2. Kinetic parameters of NdmA and NdmB. Enzyme block 'NdmB-His6'; substrate row 'Theobromine'; product column '7-Methylxanthine'; column 'Km (uM)' = 25; column 'kcat (min^-1)' = 46; column 'kcat/Km (min^-1 uM^-1)' = 1.8.

raw_value_unit_evidence: Table 2, enzyme block 'NdmB-His6', substrate row 'Theobromine': Km = 25 uM; kcat = 46 min^-1; printed kcat/Km = 1.8 min^-1 uM^-1.

substrate: Theobromine


column_label: Table 2. Kinetic parameters of NdmA and NdmB. Enzyme block 'NdmB-His6'; substrate row '3-Methylxanthine'; product column 'Xanthine'; column 'Km (uM)' = 22; column 'kcat (min^-1)' = 32; column 'kcat/Km (min^-1 uM^-1)' = 1.4.

raw_value_unit_evidence: Table 2, enzyme block 'NdmB-His6', substrate row '3-Methylxanthine': Km = 22 uM; kcat = 32 min^-1; printed kcat/Km = 1.4 min^-1 uM^-1.


column_label: Table 2. Kinetic parameters of NdmA and NdmB. Enzyme block 'NdmB-His6'; substrate row 'Caffeine'; product column 'Paraxanthine'; column 'Km (uM)' = 42; column 'kcat (min^-1)' = 0.23; column 'kcat/Km (min^-1 uM^-1)' = 0.006.

raw_value_unit_evidence: Table 2, enzyme block 'NdmB-His6', substrate row 'Caffeine': Km = 42 uM; kcat = 0.23 min^-1; printed kcat/Km = 0.006 min^-1 uM^-1.


enzyme_display_name: Tabersonine 16-hydroxylase 1

organism: Catharanthus roseus

substrate_name: H+; NADPH; O2; Tabersonine

sequence_source: UniProtKB:P98183 direct exact accession lookup

enzyme: Tabersonine 16-hydroxylase 1

substrate: H+; NADPH; O2; Tabersonine


substrate_name: tabersonine

sequence_source: UniProtKB:P98183 (primary accession for source C0KYN4)

proof_lines:
isoform T16H1, at pH 8.0 and 30°C
isoform T16H2, at pH 8.0 and 30°C

substrate: tabersonine


organism: Arabidopsis thaliana

sequence_source: UniProtKB direct lookup Q9C5D7

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q9C5D7 and applied mutation signature G46Y/W193F/R194M/I195K to reconstruct the assayed variant sequence.


organism: Goniophlebium amoenum

substrate_name: caffeoyl-CoA

sequence_source: UniProtKB direct lookup A0A4Y5R9F4

substrate: caffeoyl-CoA


substrate_name: quercetin

substrate: quercetin


proof_lines:
isoform CCoAOMT1, at pH 7.5 and 37°C
isoform CCoAOMT2, at pH 7.5 and 37°C


organism: Linum usitatissimum

sequence_source: UniProtKB direct lookup Q4JHB1

assay_conditions_summary: 303.15 K; cofactor CoA


organism: Mesembryanthemum crystallinum

substrate_name: eriodictyol

sequence_source: UniProtKB direct lookup Q6YI95

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q6YI95 and applied mutation signature D228A to reconstruct the assayed variant sequence.

proof_lines: mutant D228A, pH 7.5, temperature not specified in the publication

substrate: eriodictyol


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


substrate_name: quercetagetin

sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q6YI95 and applied mutation signature K157A to reconstruct the assayed variant sequence.

proof_lines: mutant K157A, pH 7.5, temperature not specified in the publication

substrate: quercetagetin


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup Q6YI95 and applied mutation signature N181A to reconstruct the assayed variant sequence.

proof_lines: mutant N181A, pH 7.5, temperature not specified in the publication


organism: Plagiochasma appendiculatum

sequence_source: UniProtKB direct lookup A0A0U2YR01


organism: Pyrus x bretschneideri

sequence_source: UniProtKB direct lookup A0A343J4W7

assay_conditions_summary: pH 4; 310.15 K; cofactor CoA


organism: Escherichia coli


substrate_name: D-mannitol[side 1]

proof_lines:
at pH 8.0 and 37°C
Km above 0.5 mM, at pH 8.0 and 37°C
at pH 5.5 and 30°C

substrate: D-mannitol[side 1]


organism: Methanocaldococcus jannaschii

substrate_name: GTP

substrate: GTP


substrate_name: Adenosyl cobinamide phosphate

substrate: Adenosyl cobinamide phosphate


enzyme_display_name: cardiolipin synthase (CMP-forming)

substrate_name: CDP-dioleoylglycerol

enzyme: cardiolipin synthase (CMP-forming)

substrate: CDP-dioleoylglycerol


organism: Saccharomyces cerevisiae


enzyme_display_name: thiosulfate--thiol sulfurtransferase

organism: Homo sapiens

substrate_name: thiosulfate

enzyme: thiosulfate--thiol sulfurtransferase

substrate: thiosulfate