column_label: Table 2 (Kinetics of glucose release by PyAMase for G3 to G7), substrate row 'G4'; column 'Km (mM)' = 2.1 (printed with its plus-minus term 0.4); column 'kcat (s^-1)' = 51.2 (printed with its plus-minus term 1.8); column 'kcat/Km (mM^-1 s^-1)' = 24 (printed without a plus-minus term).

normalized_value_unit_evidence: Km: printed Table 2 cell 2.1 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.1 mM; the exported value is 2.1 mM. kcat: printed Table 2 cell 51.2 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 51.2 s^(-1); the exported value is 51.2 s^(-1). kcat/Km: printed Table 2 cell 24 under the column head kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell is 24.0 s^(-1)*mM^(-1); the exported value 24.38095238095238 s^(-1)*mM^(-1) is the full-precision quotient of the two printed component cells, 51.2 / 2.1, and that quotient written to the significant figures of the printed column is 24, the printed cell.

raw_value_unit_evidence: Table 2, substrate row 'G4' (maltotetraose): Km = 2.1 mM; kcat = 51.2 s^-1; printed kcat/Km = 24 mM^-1 s^-1.


organism: Pyrobaculum aerophilum

substrate_name: Maltotriose; D-Glucose; Maltopentaose; Maltotetraose; Maltotetraose; Maltotetraose; Maltoheptaose; Maltopentaose; Maltopentaose; Malto-oligosaccharide; Maltohexaose

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

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


organism: Thermococcus litoralis

substrate_name: maltoheptaose

source_db: brenda;skid

kcat_display: Not reported

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

proof_lines:
pH 7.0, 95°C
Raw SKiD Env: Temp=95°C, pH=7

source_databases_merged: brenda skid

substrate: maltoheptaose

source: brenda;skid


organism: Thermus brockianus

substrate_name: maltotriose

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q2VJA0 and applied mutation signature W258G to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

substrate: maltotriose

status: unverified

source: oed


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


source_db: brenda

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q2VJA0 and applied mutation signature F251G to reconstruct the assayed variant sequence.

source: brenda


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q2VJA0 and applied mutation signature Q256G to reconstruct the assayed variant sequence.


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

source_db: uniprot

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.

source: uniprot


organism: Arabidopsis thaliana


organism: Homo sapiens

substrate_name: UTP

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

substrate: UTP


substrate_name: N-acetyl-D-galactosamine 1-phosphate

proof_lines: GST-fusion protein, N-acetyl-D-galactosamine 1-phosphate, pH 7.5, 37°C

proof_lines: GST-fusion protein, N-acetyl-D-glucosamine 1-phosphate, pH 7.5, 37°C

proof_lines: GST-fusion protein, N-acetylglucosamine 1-phosphate, pH 7.5, 37°C

substrate: N-acetyl-D-galactosamine 1-phosphate


organism: Corynebacterium glutamicum

substrate_name: starch

proof_lines: pH 6.0, 30°C, disproportionation activity, recombinant wild-type enzyme

proof_lines: pH 6.0, 30°C, starch transglycosylation, recombinant wild-type enzyme

substrate: starch


substrate_name: Maltotriose

verification_status: corrected

column_label: Table 2 (Kinetics of glucose release by PyAMase for G3 to G7), substrate row 'G3'; column 'Km (mM)' = 3.7 (printed with its plus-minus term 0.5); column 'kcat (s^-1)' = 115 (printed with its plus-minus term 5); column 'kcat/Km (mM^-1 s^-1)' = 31 (printed without a plus-minus term).

normalized_value_unit_evidence: kcat: printed Table 2 cell 115 under the column head kcat (s^-1); the column is already per second, so no unit conversion applies and the paper value is 115.0 s^(-1); the exported value is 115.0 s^(-1). Km: printed Table 2 cell 3.7 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 3.7 mM; the exported value is 1.5 mM, which is not the Km cell printed for this substrate row. kcat/Km: printed Table 2 cell 31 under the column head kcat/Km (mM^-1 s^-1); 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so the printed cell is 31.0 s^(-1)*mM^(-1); this export row carries no ratio field.

raw_value_unit_evidence: Table 2, substrate row 'G3' (maltotriose): Km = 3.7 mM; kcat = 115 s^-1; printed kcat/Km = 31 mM^-1 s^-1.

table_label: Table 2: Kinetics of glucose release by PyAMase for G3 to G7 (Applied and Environmental Microbiology 2005, 71(9):5098-5106)

substrate: Maltotriose

status: corrected


substrate_name: UDP-N-acetyl-alpha-D-galactosamine

substrate: UDP-N-acetyl-alpha-D-galactosamine


substrate_name: UDP-N-acetylglucosamine

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: UDP-N-acetylglucosamine

source: skid


enzyme_display_name: oryzalexin D synthase

organism: Oryza sativa subsp. japonica

substrate_name: ent-cassadiene

proof_lines: kcat is 0.011 sec(-1) with ent-sandaracopimaradien as substrate. kcat is 0.009 sec(-1) with ent-pimaradiene as substrate. kcat is 0.015 sec(-1) with ent-isokaurene as substrate. kcat is 0.006 sec(-1) with ent-cassadiene as substrate. kcat i

enzyme: oryzalexin D synthase

substrate: ent-cassadiene


organism: Oryza sativa

substrate_name: H+; NADPH; O2; ent-Sandaracopimaradiene

sequence_source: UniProtKB reviewed Q6YTF1 FASTA

substrate: H+; NADPH; O2; ent-Sandaracopimaradiene


substrate_name: ent-kaurene

sequence_source: Reviewed UniProtKB Q6YTF1 (C76M8_ORYSJ), reached through ENZYME/ExPASy EC 1.14.14.123 direct reference.

proof_lines: pH and temperature not specified in the publication

substrate: ent-kaurene


organism: Mus musculus

substrate_name: histone octamer

substrate: histone octamer


enzyme_display_name: magnesium protoporphyrin IX methyltransferase

organism: Chlorobaculum tepidum

substrate_name: magnesium protoporphyrin

proof_lines: concentrations between 0.3 and 30 microM in the presence of 50 nM enzyme

proof_lines: concentrations between 1 and 30 microM in the presence of 200 nM enzyme

substrate: magnesium protoporphyrin


organism: Hordeum vulgare

substrate_name: magnesium protoporphyrin IX

enzyme: magnesium protoporphyrin IX methyltransferase

substrate: magnesium protoporphyrin IX


organism: Synechocystis sp.

substrate_name: S-adenosyl-L-methionine

proof_lines: at 30°C in 100 mM Tris pH 7.5 and 100 mM glycerol, in the presence of 0.004 mM magnesium chelatase

proof_lines: at 30°C in 100 mM Tris pH 7.5 and 100 mM glycerol, in the absence of magnesium chelatase

substrate: S-adenosyl-L-methionine


organism: Triticum aestivum


organism: Rhodobacter capsulatus

sequence_source: UniProtKB reviewed accession P26236

proof_lines: determined using 250 microM S-adenosyl-L-methionine

proof_lines: non-competitive product inhibition, magnesium deuteroporphyrin as substrate


sequence_source: UniProtKB reviewed accession Q55467


substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


substrate_name: [histone H3]-L-lysine36

sequence_source: UniProtKB reviewed accession Q9NQV7

proof_lines: with [histone H3]-N6,N6-dimethyl-L-lysine36 as cosubstrate, at pH 8.5 and 23°C

proof_lines: with [histone H3]-N6-methyl-L-lysine36 as cosubstrate, at pH 8.5 and 23°C

substrate: [histone H3]-L-lysine36


substrate_name: recombinant nucleosome

sequence_source: UniProtKB reviewed accession Q9BYW2

proof_lines: cosubstrate chicken nucleosome, pH 9.0, 23°C

proof_lines: cosubstrate recombinant nucleosome, pH 9.0, 23°C

substrate: recombinant nucleosome


proof_lines: All kinetic experiments are done with 10 mm Tris-HCl, 0.01% Triton X-100, and 10 mm DTT and at pH 8.5.


assay_conditions_summary: cofactor CoA

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.


sequence_source: UniProtKB reviewed accession Q6YTF1 FASTA

assay_conditions_summary: cofactor NADPH


enzyme_display_name: formimidoylglutamase

organism: Bacillus subtilis (strain 168)

substrate_name: Unknown

km_display: Not reported

enzyme: formimidoylglutamase

substrate: Unknown


organism: Trypanosoma cruzi

substrate_name: N-formimidoyl-L-glutamate

sequence_variant_note: Resolved canonical sequence from UniProtKB accession Q4DSA0 FASTA; R144K reconstructed from the canonical sequence after confirming residue 144 is R and applied mutation signature R144K to reconstruct the assayed variant sequence.

substrate: N-formimidoyl-L-glutamate


enzyme_display_name: 5-deoxyribulose 1-phosphate aldolase

organism: Bacillus thuringiensis serovar kurstaki

substrate_name: 5-deoxy-D-ribulose 1-phosphate

sequence_source: UniProtKB reviewed accession P0DTQ0 FASTA

proof_lines:
at pH 8.2 and 21°C
Raw SKiD Env: Temp=21°C, pH=8.2

enzyme: 5-deoxyribulose 1-phosphate aldolase

substrate: 5-deoxy-D-ribulose 1-phosphate


organism: Sulfurisphaera tokodaii

substrate_name: alpha-D-galactosamine 1-phosphate

sequence_source: UniProtKB:Q975F9 direct accession lookup, 2026-06-27

substrate: alpha-D-galactosamine 1-phosphate


assay_conditions_summary: pH 7.5; 353.15 K; cofactor CoA


sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: deletion

proof_lines: pH 7.5, 80°C, mutant enzyme DC005 with a deletion of the C-terminal 5 residues of the ST0452 protein


proof_lines: pH 7.5, 80°C, mutant enzyme DC011 with a deletion of the C-terminal 11 residues of the ST0452 protein


substrate_name: N-Acetylglucosamine 6-sulfate; H2O

sequence_source: UniProtKB:P15586 direct accession lookup, 2026-06-27

substrate: N-Acetylglucosamine 6-sulfate; H2O


ki_unit: mM

sequence_source: UniProtKB:Q8IWU6 direct accession lookup, 2026-06-27


verification_status: verified

sequence_source: UniProtKB:Q4DSA0 direct accession lookup, 2026-06-27

column_label: Table 3 (Steady-State Kinetics at pH 9.5), enzyme row 'Wild-type TcFIGasea'; column 'kcat (s^-1)' = 200; column 'KM (mM)' = 40; column 'kcat/KM (M^-1 s^-1)' = 5200; footnote a, enzyme expressed and purified from LB media.

normalized_value_unit_evidence: kcat: printed Table 3 cell 200 s^-1; the cell is already in s^-1, so no unit conversion applies and the exported value is 200.0 s^(-1). KM: printed Table 3 cell 40 mM; the cell is already in mM, so no unit conversion applies and the exported value is 40.0 mM. kcat/KM: printed Table 3 cell 5200 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5200 / 1000 = 5.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Wild-type TcFIGasea': kcat = 200 s^-1; KM = 40 mM; printed kcat/KM = 5200 M^-1 s^-1.

row_label: Table 3, enzyme row 'Wild-type TcFIGasea' (footnote a, enzyme expressed and purified from LB media)

table_label: Table 3: Steady-State Kinetics at pH 9.5 (Biochemistry 2013, 52(51):9294-9309)

status: verified


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4DSA0 direct accession lookup, 2026-06-27 and applied mutation signature R144E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4DSA0 direct accession lookup, 2026-06-27 and applied mutation signature R144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4DSA0 and applied mutation signature R144E to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetics at pH 9.5), enzyme row 'R144E TcFIGaseb,d'; column 'kcat (s^-1)' = 0.05; column 'KM (mM)' = 9; column 'kcat/KM (M^-1 s^-1)' = 5.2; footnote b, enzyme expressed and purified from minimal media supplemented with 100 uM MnCl2 prior to induction; footnote d, apparent KM from the Hill equation.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.05 s^-1; the cell is already in s^-1, so no unit conversion applies and the exported value is 0.05 s^(-1). KM: printed Table 3 cell 9 mM; the cell is already in mM, so no unit conversion applies and the exported value is 9.0 mM. kcat/KM: printed Table 3 cell 5.2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.2 / 1000 = 0.0052 s^-1 mM^-1, and this record carries 0.0052 s^(-1)*mM^(-1) as the paper-side kcat/KM in place of the 0.005555555555555556 s^(-1)*mM^(-1) the catalog holds for this identity.

raw_value_unit_evidence: Table 3, enzyme row 'R144E TcFIGaseb,d': kcat = 0.05 s^-1; KM = 9 mM; printed kcat/KM = 5.2 M^-1 s^-1.

row_label: Table 3, enzyme row 'R144E TcFIGaseb,d' (footnote b, enzyme expressed and purified from minimal media supplemented with 100 uM MnCl2 prior to induction; footnote d, apparent KM from the Hill equation)


normalized_value_unit_evidence: kcat: printed Table 3 cell 200 s^-1; the cell is already in s^-1, so no unit conversion applies and the exported value is 200.0 s^(-1). KM: printed Table 3 cell 40 mM; the cell is already in mM, so no unit conversion applies and the exported value is 40.0 mM. kcat/KM: printed Table 3 cell 5200 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5200 / 1000 = 5.2 s^-1 mM^-1, and this record carries 5.2 s^(-1)*mM^(-1) as the paper-side kcat/KM in place of the 5.0 s^(-1)*mM^(-1) the catalog holds for this identity.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4DSA0 and applied mutation signature R144A to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetics at pH 9.5), enzyme row 'R144A TcFIGaseb'; column 'kcat (s^-1)' = 3.2; column 'KM (mM)' = 90; column 'kcat/KM (M^-1 s^-1)' = 37; footnote b, enzyme expressed and purified from minimal media supplemented with 100 uM MnCl2 prior to induction.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.2 s^-1; the cell is already in s^-1, so no unit conversion applies and the exported value is 3.2 s^(-1). KM: printed Table 3 cell 90 mM; the cell is already in mM, so no unit conversion applies and the exported value is 90.0 mM. kcat/KM: printed Table 3 cell 37 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 37 / 1000 = 0.037 s^-1 mM^-1, and this record carries 0.037 s^(-1)*mM^(-1) as the paper-side kcat/KM in place of the 0.035555555555555556 s^(-1)*mM^(-1) the catalog holds for this identity.

raw_value_unit_evidence: Table 3, enzyme row 'R144A TcFIGaseb': kcat = 3.2 s^-1; KM = 90 mM; printed kcat/KM = 37 M^-1 s^-1.

row_label: Table 3, enzyme row 'R144A TcFIGaseb' (footnote b, enzyme expressed and purified from minimal media supplemented with 100 uM MnCl2 prior to induction)


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4DSA0 direct accession lookup, 2026-06-27 and applied mutation signature N114H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q4DSA0 direct accession lookup, 2026-06-27 and applied mutation signature R144K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q4DSA0 and applied mutation signature N114H to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetics at pH 9.5), enzyme row 'N114H TcFIGasea'; column 'kcat (s^-1)' = 80; column 'KM (mM)' = 20; column 'kcat/KM (M^-1 s^-1)' = 3400; footnote a, enzyme expressed and purified from LB media.

normalized_value_unit_evidence: kcat: printed Table 3 cell 80 s^-1; the cell is already in s^-1, so no unit conversion applies and the exported value is 80.0 s^(-1). KM: printed Table 3 cell 20 mM; the cell is already in mM, so no unit conversion applies and the exported value is 20.0 mM. kcat/KM: printed Table 3 cell 3400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3400 / 1000 = 3.4 s^-1 mM^-1, and this record carries 3.4 s^(-1)*mM^(-1) as the paper-side kcat/KM in place of the 4.0 s^(-1)*mM^(-1) the catalog holds for this identity.

raw_value_unit_evidence: Table 3, enzyme row 'N114H TcFIGasea': kcat = 80 s^-1; KM = 20 mM; printed kcat/KM = 3400 M^-1 s^-1.

row_label: Table 3, enzyme row 'N114H TcFIGasea' (footnote a, enzyme expressed and purified from LB media)


enzyme_display_name: DNA primase AEP

substrate_name: ATP

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

assay_conditions_summary: cofactor ATP

enzyme: DNA primase AEP

substrate: ATP


organism: Pyrococcus abyssi

substrate_name: dNTP

proof_lines: pH 8.0, 60°C, presence of 5 mM Mn2+, 10 mM Mg2+

substrate: dNTP


organism: Saccharolobus solfataricus

substrate_name: NTP

substrate: NTP


organism: Sulfolobus islandicus


substrate_name: dATP

substrate: dATP


assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP


enzyme_display_name: deoxyribodipyrimidine photo-lyase

organism: Escherichia coli

substrate_name: cis-syn Cyclobutadipyrimidine

enzyme: deoxyribodipyrimidine photo-lyase

substrate: cis-syn Cyclobutadipyrimidine


organism: Homo sapiens

substrate_name: dTTP (in presence of 2 mM of Mn(2+))

proof_lines: kcat is 0.05 sec(-1) for dTTP (in presence of 2 mM of Mn(2+)). kcat is 0.02 sec(-1) for dTTP (in presence of 50 uM of Mn(2+)). kcat is 0.01 sec(-1) for dTTP (in presence of 2 mM of Mg(2+)).

substrate: dTTP (in presence of 2 mM of Mn(2+))


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dNTPs

proof_lines: kcat is 22 sec(-1) for polymerase activity (PubMed:27487482). kcat is 10 min(-1) for polymerase activity (PubMed:39490679). kcat is 1.69 min(-1) for polymerase activity on dA template with dTTP (PubMed:35220686, PubMed:32636411). kcat is 1.

substrate: dNTPs


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


organism: Escherichia coli O45:K1 (strain S88 / ExPEC)

proof_lines: kcat is 22 sec(-1) with 5-methylthioribulose-1-phosphate as substrate. kcat is 22 sec(-1) with 5-deoxyribulose 1-phosphate as substrate. kcat is 8.7 sec(-1) with ribulose-1-phosphate as substrate.


organism: Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIMB 8255 / S1)

proof_lines: kcat is 0.94 sec(-1) with 5-methylthioribulose-1-phosphate as substrate. kcat is 1.94 sec(-1) with 5-deoxyribulose 1-phosphate as substrate. kcat is 0.44 sec(-1) with ribulose-1-phosphate as substrate.


enzyme_display_name: abieta-7,13-dien-18-ol hydroxylase

organism: Abies grandis

substrate_name: abietadienol

enzyme: abieta-7,13-dien-18-ol hydroxylase

substrate: abietadienol


organism: Pinus taeda

substrate_name: isopimaradienol

substrate: isopimaradienol


organism: Bos taurus

substrate_name: N-acetyl-D-glucosamine 6-sulfate

substrate: N-acetyl-D-glucosamine 6-sulfate


organism: Capra hircus

substrate_name: 4-Methylumbelliferyl sulfate

substrate: 4-Methylumbelliferyl sulfate


substrate_name: glucose 6-sulfate

proof_lines:
form A and B
in urine
in leucocytes

substrate: glucose 6-sulfate


organism: Bacillus subtilis


organism: Pseudomonas putida


substrate_name: S-methyl-5-thio-D-ribulose 1-phosphate

proof_lines: at pH 7.8, temperature not specified in the publication

substrate: S-methyl-5-thio-D-ribulose 1-phosphate


organism: Rhodospirillum rubrum

substrate_name: ribulose 1-phosphate

proof_lines: Km above 7.0 mM, at pH 7.8, temperature not specified in the publication

proof_lines: kcat_Km value below 0.06 1/sec*mM, at pH 7.8, temperature not specified in the publication

substrate: ribulose 1-phosphate


substrate_name: pyrimidine dimer in DNA

proof_lines:
for dsDNA
for ssDNA

substrate: pyrimidine dimer in DNA


organism: Vibrio cholerae serotype O1

substrate_name: cyclobutadipyrimidine in DNA

substrate: cyclobutadipyrimidine in DNA


organism: Saccharolobus islandicus

sequence_source: UniProtKB:Q54324 REST/FASTA direct lookup on 2026-06-27

proof_lines: 50°C, pH 7.5, synthesis of full-length primer


enzyme_display_name: adrenodoxin-NADP(+) reductase

organism: Rattus norvegicus

substrate_name: NADPH

enzyme: adrenodoxin-NADP(+) reductase

substrate: NADPH


assay_conditions_summary: pH 7.5; 298.15 K; buffer sodium phosphate; cofactor NADPH

proof_lines: in sodium phosphate buffer, pH 7.5, temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: H+; NADPH; Oxidized adrenal ferredoxin

sequence_source: UniProtKB reviewed accession Q8W3L1 direct lookup

substrate: H+; NADPH; Oxidized adrenal ferredoxin


enzyme_display_name: hygromycin-B 7''-O-kinase

organism: Streptomyces hygroscopicus

substrate_name: hygromycin B

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: hygromycin-B 7''-O-kinase

substrate: hygromycin B


sequence_source: UniProtKB:P09979 direct lookup; context only

assay_conditions_summary: pH 7.5; 318.15 K; cofactor ATP


substrate_name: ATP

substrate: ATP


proof_lines: pH 7.5, 45°C, recombinant wild-type enzyme YG


sequence_source: UniProtKB:P09979 direct lookup plus PMID 24200799 HYG10 context; variant unresolved

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

proof_lines: pH 7.5, 45°C, recombinant mutant enzyme HYG10


enzyme_display_name: diglucosyl diacylglycerol synthase (1,6-linking)

organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: UDP-glucose

substrate: UDP-glucose


enzyme_display_name: oleuropein beta-glucosidase

organism: Olea europaea

substrate_name: oleuropein

enzyme: oleuropein beta-glucosidase

substrate: oleuropein


organism: Mycoplasma genitalium

sequence_source: UniProtKB reviewed FASTA Q9ZB73, accessed 2026-06-27

enzyme: diglucosyl diacylglycerol synthase (1,6-linking)


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Mycoplasmoides genitalium

proof_lines: acceptor 1,2-diacyl-sn-glycerol, pH 8.0, 28°C

proof_lines: donor UDP-alpha-D-galactose, pH 8.0, 28°C

proof_lines: acceptor 1,2-diacyl-3-O-(alpha-D-glucopyranosyl)-sn-glycerol, pH 8.0, 28°C


substrate_name: Oleuropein; H2O

sequence_source: UniProtKB reviewed FASTA Q8GVD0, accessed 2026-06-27

substrate: Oleuropein; H2O


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

proof_lines: enzyme immobilised onto Supermagnetic Nanoparticles, pH and temperature not specified in the publication


organism: Streptomyces sp.

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

proof_lines: mutant C181A, pH not specified in the publication, temperature not specified in the publication


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


proof_lines:
at pH 5.5 and 50°C
at pH 5.5 and 37°C


organism: Prunus dulcis

proof_lines: polysulfone capillary membrane-immobilized enzyme, at pH 6.5 and 25°C

proof_lines: enzyme immobilized on polysulfone capillary membranes, at pH 6.5 and 25°C


organism: Saccharolobus solfataricus

proof_lines:
pH 7.0, 60°C, soluble enzyme
pH 7.0, 70°C, soluble enzyme


organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

substrate_name: magnesium ion

sequence_source: source_record; UniProtKB Q8A712

assay_conditions_summary: pH 7

proof_lines: kcat is 72 min(-1) for 2-keto-3-deoxy-D-glycero-D-galacto-9-phosphonononic acid (KDN-9-P) as substrate (PubMed:18804026). kcat is 44 min(-1) for N-acetylneuraminate-9-phosphate (Neu5NAc-9-P) as substrate (PubMed:18804026). kcat is 3.8 min(-

substrate: magnesium ion


organism: Bacteroides thetaiotaomicron

substrate_name: N-acetylneuraminic acid 9-phosphate

sequence_source: UniProtKB:Q8A712 direct REST/FASTA lookup, with selected mutation applied when present

substrate: N-acetylneuraminic acid 9-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8A712 direct REST/FASTA lookup, with selected mutation applied when present and applied mutation signature E56A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8A712 direct REST/FASTA lookup, with selected mutation applied when present and applied mutation signature T34A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8A712 direct REST/FASTA lookup, with selected mutation applied when present and applied mutation signature S37A to reconstruct the assayed variant sequence.


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


enzyme_display_name: phenylethanolamine N-methyltransferase

organism: Unknown

substrate_name: Unknown

enzyme: phenylethanolamine N-methyltransferase

substrate: Unknown


organism: Bos taurus

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

proof_lines:
competitive with phenylethanolamine
noncompetitive with phenylethanolamine


organism: Columba livia

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Homo sapiens

substrate_name: phenylethanolamine

proof_lines: purified in the absence of reducing agent, dimer, His-tagged

proof_lines: radiochemical assay, inhibition constants are determined using four concentrations of phenylethanolamine as the variable substrate, and three concentrations of inhibitor

substrate: phenylethanolamine


substrate_name: norepinephrine

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

substrate: norepinephrine


organism: Oryctolagus cuniculus

proof_lines:
enzyme form H-1
enzyme form H-2
enzyme form H-2, substrate inhibition


organism: Rattus norvegicus


sequence_variant_note: Resolved canonical sequence from UniProt REST accession lookup for P11086; E219Q reconstructed from the canonical UniProt sequence after confirming residue 219 is E. and applied mutation signature E219Q to reconstruct the assayed variant sequence.

proof_lines: mutant E219Q, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-adenosyl


sequence_source: UniProt REST accession lookup for P11086.


organism: Macaca mulatta

substrate_name: normetanephrine

substrate: normetanephrine


substrate_name: normetanephrine (enzyme found in the brain)


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature K57A to reconstruct the assayed variant sequence.

proof_lines: mutant K57A, radiochemical assay containing S-adenosyl-L-methionine and phenylethanolamine

proof_lines: mutant K57A, inhibition assay containing a fixed concentration of S-adenosyl-L-methionine and variable concentrations of the inhibitor and phenylethanolamine


proof_lines: mutant D57A, inhibition assay containing a fixed concentration of S-adenosyl-L-methionine and variable concentrations of the inhibitor and phenylethanolamine


proof_lines: mutant D267, assay containing S-adenosyl-L-methionine and 3-trifluoromethylphenylethanolamine


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature D267A to reconstruct the assayed variant sequence.

proof_lines: mutant D267A, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-adenosyl

proof_lines: mutant D267A, assay containing S-adenosyl-L-methionine and anti-9-amino-6-(trifluoromethyl)benzonorbornene


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature V53A to reconstruct the assayed variant sequence.

proof_lines: mutant V53A, radiochemical assay containing S-adenosyl-L-methionine and phenylethanolamine

proof_lines: mutant V53A, inhibition assay containing a fixed concentration of S-adenosyl-L-methionine and variable concentrations of the inhibitor and phenylethanolamine


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature D267N to reconstruct the assayed variant sequence.

proof_lines: mutant D267N, radiochemical assay containing S-adenosyl-L-methionine and phenylethanolamine


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature E219A to reconstruct the assayed variant sequence.

proof_lines: mutant E219A, radiochemical assay containing S-adenosyl-L-methionine and phenylethanolamine

proof_lines: mutant E219A, inhibition assay containing a fixed concentration of S-adenosyl-L-methionine and variable concentrations of the inhibitor and phenylethanolamine


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature E219A/D267N to reconstruct the assayed variant sequence.

proof_lines: mutant E219A and mutant D267N, radiochemical assay containing S-adenosyl-L-methionine and phenylethanolamine


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature E185D to reconstruct the assayed variant sequence.

proof_lines: mutant E185D, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-adenosyl


substrate_name: octopamine

sequence_source: UniProt P11086 FASTA direct check on 2026-06-27

proof_lines: wild type enzyme, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-aden

proof_lines: wild type enzyme, radiochemical assay containing S-adenosyl-L-methionine and phenylethanolamine

substrate: octopamine


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature E185Q to reconstruct the assayed variant sequence.

proof_lines: mutant E185Q, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-adenosyl


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature Y35F to reconstruct the assayed variant sequence.

proof_lines: mutant Y35F, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-adenosyl-


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

proof_lines: cosubstrate 3-trifluoromethylphenylethanolamine, pH 8.0, 30°C

proof_lines: cosubstrate phenylethanolamine, pH 8.0, 30°C

source_databases_merged: sabio_rk brenda skid


sequence_variant_note: Resolved canonical sequence from UniProt P11086 FASTA direct check on 2026-06-27 and applied mutation signature E185A to reconstruct the assayed variant sequence.

proof_lines: mutant E185A, assay mixture consists of 25 microl of 0.5 M phosphate buffer (pH 8.0), 5 microl of [methyl-3H]S-adenosyl-L-methionine containing approximately 2.5 X 10 00000 dpm, varying amounts of phenylethanolamine and unlabeled S-adenosyl


enzyme_display_name: 7-deoxyloganetin glucosyltransferase

organism: Catharanthus roseus

proof_lines: kcat is 0.0355 sec(-1) for 7-deoxyloganetin. kcat is 0.0320 sec(-1) for UPD-glucose.

enzyme: 7-deoxyloganetin glucosyltransferase


organism: Gardenia jasminoides

substrate_name: genipin

proof_lines: kcat is 1.04 sec(-1) for genipin. kcat is 0.13 sec(-1) for 7-deoxyloganetin. kcat is 0.16 sec(-1) for UPD-glucose.

substrate: genipin


sequence_source: UniProtKB:F8WLS6 direct accession lookup on 2026-06-27 (UniProtKB reviewed (Swiss-Prot); length 487; CRC64 A6E423A362B9E0CF)


sequence_source: UniProtKB:F8WKW5 direct accession lookup on 2026-06-27 (UniProtKB unreviewed (TrEMBL); length 493; CRC64 4110C8F69F3661CB)


enzyme_display_name: tagatose-6-phosphate kinase

enzyme: tagatose-6-phosphate kinase


organism: Lactococcus lactis subsp. lactis

substrate_name: ATP; D-Tagatose 6-phosphate

substrate: ATP; D-Tagatose 6-phosphate


organism: Staphylococcus aureus

substrate_name: ATP

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: fructose 6-phosphate

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

substrate: fructose 6-phosphate


enzyme_display_name: beta-N-acetylgalactosaminidase

organism: Paenibacillus sp.

sequence_source: UniProtKB:E9RH20 REST lookup on 2026-06-27 returned inactive/deleted record without replacement sequence

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

enzyme: beta-N-acetylgalactosaminidase


organism: Bacillus sp. (in: firmicutes)


organism: Akkermansia muciniphila (strain ATCC BAA-835 / DSM 22959 / JCM 33894 / BCRC 81048 / CCUG 64013 / CIP 107961 / Muc)

substrate_name: pNP-GlcNAc (at pH 7.0 and 37 degrees Celsius)

proof_lines: kcat is 51.39 sec(-1) and kcat/KM is 1.73 M(-1)sec(-1) with pNP-GlcNAc as substrate.


organism: Mycobacterium tuberculosis

substrate_name: NADH

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NADPH

proof_lines: diaphorase activity with ferricyanide, pH 7.2, 30°C

substrate: NADH


enzyme_display_name: 5-aminolevulinate synthase

substrate_name: succinyl-CoA

enzyme: 5-aminolevulinate synthase

substrate: succinyl-CoA


substrate_name: glycine

substrate: glycine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: succinyl-CoA; glycine

sequence_source: UniProtKB:P22557 direct REST lookup on 2026-06-27

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: apparent value, pH and temperature not specified in the publication

substrate: succinyl-CoA; glycine


organism: Mus musculus

sequence_source: UniProtKB:P08680 direct REST lookup on 2026-06-27; canonical sequence retained as context only

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 7.5; 291.15 K; cofactor CoA


sequence_source: UniProtKB:P08680 direct REST lookup on 2026-06-27


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Rhodobacter capsulatus

substrate_name: glycine; succinyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB:P18079 direct REST lookup on 2026-06-27 plus explicit residue substitutions I325M/V390Y/H391I and applied mutation signature I325M/V390Y/H391I to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, mutant enzyme I325M/V390Y/H391I

substrate: glycine; succinyl-CoA


enzyme_display_name: glutamine kinase

organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: L-glutamine (at pH 8.0 and 25 degrees Celsius)

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

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 2.5 sec(-1) with L-glutamine as substrate (PubMed:28650156, PubMed:30142271). kcat is 1.5 sec(-1) with D-glutamine as substrate. kcat is 2.1 sec(-1) with gamma-L-glutamyl hydroxamate as substrate. kcat is 0.41 sec(-1) with gamma-L-g

enzyme: glutamine kinase


organism: Campylobacter jejuni

sequence_source: UniProtKB Q0P8J6; paper-linked Cj1418c target from PMID 28650156

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


substrate_name: L-Glutamine; ATP; H2O

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

sequence_source: UniProtKB reviewed accession Q0P8J6; direct lookup 2026-06-27

substrate: L-Glutamine; ATP; H2O


substrate_name: D-Glutamine

substrate: D-Glutamine


substrate_name: gamma-L-glutamyl hydrazide

substrate: gamma-L-glutamyl hydrazide


substrate_name: L-glutamine

assay_conditions_summary: pH 8; 355.15 K; cofactor ATP

substrate: L-glutamine


substrate_name: gamma-L-glutamyl hydroxamate

substrate: gamma-L-glutamyl hydroxamate


enzyme_display_name: trimethyltridecatetraene synthase

organism: Zea mays

sequence_source: UniProtKB reviewed accession A0A1D6F9Y9 (C92C6_MAIZE), fetched during targeted PMID/gene follow-up

proof_lines: pH and temperature not specified in the publication

enzyme: trimethyltridecatetraene synthase


organism: Arabidopsis thaliana

substrate_name: (6E,10E)-Geranyllinalool; O2; NADPH; H+

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

substrate: (6E,10E)-Geranyllinalool; O2; NADPH; H+


substrate_name: H+; NADPH; O2; (6E,10E)-Geranyllinalool

substrate: H+; NADPH; O2; (6E,10E)-Geranyllinalool


enzyme_display_name: vancomycin aglycone glucosyltransferase

organism: Amycolatopsis orientalis

substrate_name: UDP-alpha-D-glucose

sequence_source: UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1

enzyme: vancomycin aglycone glucosyltransferase

substrate: UDP-alpha-D-glucose


substrate_name: vancomycin aglycone

substrate: vancomycin aglycone


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1 and applied mutation signature H125A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H125A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1 and applied mutation signature D332A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D332A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P96559 reviewed Swiss-Prot REST lookup 2026-06-27; sequence version 1 and applied mutation signature D13A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D13A, pH and temperature not specified in the publication


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


substrate_name: UDP-glucose

substrate: UDP-glucose


enzyme_display_name: dehydrogluconokinase

organism: Klebsiella aerogenes

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

enzyme: dehydrogluconokinase


organism: Cupriavidus necator

substrate_name: ATP

sequence_source: UniProtKB:Q0K080, cross-checked against NCBI YP_841324.1 and WP_010810288.1 on 2026-06-27

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


substrate_name: ATP; 2-Dehydro-D-gluconate

proof_lines: pH 8.0, temperature not specified in the publication

substrate: ATP; 2-Dehydro-D-gluconate


enzyme_display_name: 2-aminobenzoylacetyl-CoA thioesterase

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

substrate_name: S-ethyl-acetothioacetate

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 0.85 sec(-1) with S-ethyl-acetothioacetate as substrate. kcat is 0.36 sec(-1) with acetoacetyl-CoA as substrate. kcat is 0.022 sec(-1) with cysteamine-S-phosphate as substrate (PubMed:25960261). kcat is 7.2 min(-1) with S-(4-nitrobe

enzyme: 2-aminobenzoylacetyl-CoA thioesterase

substrate: S-ethyl-acetothioacetate


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB direct lookup for reviewed accession P20581

proof_lines: wild-type, pH 8.5, 25°C, presence of Mn2+


sequence_variant_note: Resolved canonical sequence from UniProtKB direct lookup for reviewed accession P20581 plus local E182A substitution reconstruction and applied mutation signature E182A to reconstruct the assayed variant sequence.

proof_lines: mutant E182A, pH 8.5, 25°C, presence of Mn2+


substrate_name: acetoacetyl-CoA

sequence_source: UniProtKB direct lookup for unreviewed accession A0A0H2Z6F6

assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA

proof_lines:
pH 8.2, 30°C
Raw SKiD Env: Temp=30°C, pH=8.2

substrate: acetoacetyl-CoA


enzyme_display_name: L-galactose 1-phosphate phosphatase

substrate_name: D-myoinositol 3-phosphate

enzyme: L-galactose 1-phosphate phosphatase

substrate: D-myoinositol 3-phosphate


organism: Actinidia deliciosa

substrate_name: L-Galactose 1-phosphate; H2O

sequence_source: UniProtKB REST direct accession lookup Q5U789 on 2026-06-27; active TrEMBL entry Q5U789_ACTDE.

substrate: L-Galactose 1-phosphate; H2O


substrate_name: beta-L-galactose 1-phosphate

proof_lines: pH 7.0, 30°C, 1.8 mM Mg2+, native enzyme

substrate: beta-L-galactose 1-phosphate


sequence_source: UniProtKB REST direct accession lookup Q9M8S8 on 2026-06-27; reviewed Swiss-Prot entry VTC4_ARATH.


sequence_source: UniProtKB reviewed accession P9WNH5 / HSAD_MYCTU direct lookup


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid (at pH 7.5 and at 25 degrees Celsius)


assay_conditions_summary: pH 7.4; 298.15 K; buffer 100 mM of phosphate

proof_lines: apparent value, in 100 mM of phosphate buffer (pH 7.4) with 20 mM NaCl, temperature not specified in the publication

proof_lines: in 20 mM HEPES, 80 mM NaCl, at pH 8.0 and 25°C


proof_lines: wild type enzyme, in 100 mM potassium phosphate, pH 7.5, at 25°C


proof_lines: mutant enzyme S114A, in 100 mM potassium phosphate, pH 7.5, at 25°C


organism: Gallus gallus

assay_conditions_summary: pH 8


organism: Treponema denticola

sequence_source: UniProtKB reviewed accession Q73PV9 / PURE_TREDE, direct REST lookup on 2026-06-27


substrate_name: 4-carboxy-5-aminoimidazole ribonucleotide; CO2; 5-aminoimidazole ribonucleotide

proof_lines:
50 mM Tris-HCl (pH 8.0), at 30°C
50 mM Tris-HCl (pH 8.0), at 10°C
Raw SKiD Env: Temp=30°C, pH=8


organism: Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)

substrate_name: CO(2) (at 10 degrees Celsius)

substrate: CO(2) (at 10 degrees Celsius)


enzyme_display_name: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,4-lactone-forming)

organism: Haloarcula marismortui

substrate_name: D-ribose

assay_conditions_summary: pH 8.3; 310.15 K; cofactor NADP+

column_label: Table 2: Kinetic parameters of purified xylose dehydrogenase from H. marismortui (J. Bacteriol. 2004, 186(18):6198-6207); printed column heads Substrate | Vmax (U/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1, 102), the efficiency column being tabulated in units of 10^2 s-1 mM-1. Table 2, substrate row D-Ribose; column Vmax (U/mg) = 108; column Km (mM) = 2.3; column kcat (s-1) = 360; column kcat/Km (s-1, 102) = 1.57, that is 1.57 x 10^2 s-1 mM-1. captured primary segment: Table 2, substrate row D-Ribose | construct purified xylose dehydrogenase from H. marismortui | substrate D-ribose | condition 0.1 M Tris-HCl (pH 8.3) - 1.5 M KCl at 37 C | Vmax 108 U/mg | Km 2.3 mM | kcat 360 s-1 | kcat/Km 1.57 x 10^2 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 360 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 360.0 s^(-1). Km: printed Table 2 cell 2.3 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 2.3 mM. kcat/Km: printed Table 2 cell 1.57 in a column tabulated in units of 10^2 s-1 mM-1, so the printed cell is 1.57 x 10^2 = 157.0 s^(-1)*mM^(-1); the exact quotient of this row's own printed component cells is 360 / 2.3 = 156.52173913043478 s^-1 mM^-1, which is the value the export carries, and the printed cell is that quotient written to the precision of the efficiency column.

raw_value_unit_evidence: Table 2, substrate row D-Ribose: Vmax = 108 U/mg; Km = 2.3 mM; kcat = 360 s-1; printed kcat/Km = 1.57 in a column tabulated in units of 10^2 s-1 mM-1, that is 1.57 x 10^2 s-1 mM-1.

row_label: Table 2, substrate row D-Ribose

substrate: D-ribose


substrate_name: D-Xylose

column_label: Table 2: Kinetic parameters of purified xylose dehydrogenase from H. marismortui (J. Bacteriol. 2004, 186(18):6198-6207); printed column heads Substrate | Vmax (U/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1, 102), the efficiency column being tabulated in units of 10^2 s-1 mM-1. Table 2, substrate row D-Xylose; column Vmax (U/mg) = 107; column Km (mM) = 1.2; column kcat (s-1) = 356; column kcat/Km (s-1, 102) = 2.97, that is 2.97 x 10^2 s-1 mM-1. captured primary segment: Table 2, substrate row D-Xylose | construct purified xylose dehydrogenase from H. marismortui | substrate D-xylose | condition 0.1 M Tris-HCl (pH 8.3) - 1.5 M KCl at 37 C | Vmax 107 U/mg | Km 1.2 mM | kcat 356 s-1 | kcat/Km 2.97 x 10^2 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 356 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 356.0 s^(-1). Km: printed Table 2 cell 1.2 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 1.2 mM. kcat/Km: printed Table 2 cell 2.97 in a column tabulated in units of 10^2 s-1 mM-1, so the printed cell is 2.97 x 10^2 = 297.0 s^(-1)*mM^(-1); the exact quotient of this row's own printed component cells is 356 / 1.2 = 296.6666666666667 s^-1 mM^-1, which is the value the export carries, and the printed cell is that quotient written to the precision of the efficiency column.

raw_value_unit_evidence: Table 2, substrate row D-Xylose: Vmax = 107 U/mg; Km = 1.2 mM; kcat = 356 s-1; printed kcat/Km = 2.97 in a column tabulated in units of 10^2 s-1 mM-1, that is 2.97 x 10^2 s-1 mM-1.

row_label: Table 2, substrate row D-Xylose

enzyme: D-xylose 1-dehydrogenase (NADP(+), D-xylono-1,4-lactone-forming)

substrate: D-Xylose


substrate_name: D-glucose

column_label: Table 2: Kinetic parameters of purified xylose dehydrogenase from H. marismortui (J. Bacteriol. 2004, 186(18):6198-6207); printed column heads Substrate | Vmax (U/mg) | Km (mM) | kcat (s-1) | kcat/Km (s-1, 102), the efficiency column being tabulated in units of 10^2 s-1 mM-1. Table 2, substrate row D-Glucose; column Vmax (U/mg) = 82; column Km (mM) = 64; column kcat (s-1) = 273; column kcat/Km (s-1, 102) = 0.043, that is 0.043 x 10^2 s-1 mM-1. captured primary segment: Table 2, substrate row D-Glucose | construct purified xylose dehydrogenase from H. marismortui | substrate D-glucose | condition 0.1 M Tris-HCl (pH 8.3) - 1.5 M KCl at 37 C | Vmax 82 U/mg | Km 64 mM | kcat 273 s-1 | kcat/Km 0.043 x 10^2 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 2 cell 273 s-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 273.0 s^(-1). Km: printed Table 2 cell 64 mM; the Michaelis-constant column of this table is already in millimolar, so no unit conversion applies and the paper value is 64.0 mM. kcat/Km: printed Table 2 cell 0.043 in a column tabulated in units of 10^2 s-1 mM-1, so the printed cell is 0.043 x 10^2 = 4.3 s^(-1)*mM^(-1); the exact quotient of this row's own printed component cells is 273 / 64 = 4.265625 s^-1 mM^-1, which is the value the export carries, and the printed cell is that quotient written to the precision of the efficiency column.

raw_value_unit_evidence: Table 2, substrate row D-Glucose: Vmax = 82 U/mg; Km = 64 mM; kcat = 273 s-1; printed kcat/Km = 0.043 in a column tabulated in units of 10^2 s-1 mM-1, that is 0.043 x 10^2 s-1 mM-1.

row_label: Table 2, substrate row D-Glucose

substrate: D-glucose


substrate_name: D-ribose; D-xylose; D-glucose; NAD+; NADP+


organism: Haloferax volcanii

substrate_name: NAD+; D-xylose; NADP+; D-glucose

assay_conditions_summary: pH 7.5; 315.15 K; cofactor NADP+

substrate: NAD+; D-xylose; NADP+; D-glucose


organism: Eupatorium cannabinum

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines: NAD+ functions as an enzyme-bound redoxsystem that is reduced in the first and reoxidized in the second part of the overall reaction. It functions as a coenzyme and not a cosubstrate

substrate: NAD+


organism: Senecio vernalis

substrate_name: putrescine

substrate: putrescine


substrate_name: Spermidine

smiles: NCCCCNCCCN

substrate: Spermidine


substrate_name: Putrescine; Spermidine

substrate: Putrescine; Spermidine


substrate_name: Putrescine

smiles: NCCCCN

substrate: Putrescine


enzyme_display_name: tetrahydrocannabinolic acid synthase

organism: Cannabis sativa

substrate_name: cannabigerolate

proof_lines: recombinant enzyme, in 100 mM sodium citrate (pH 5.5), at 30°C

proof_lines: at pH 6.0, temperature not specified in the publication

enzyme: tetrahydrocannabinolic acid synthase

substrate: cannabigerolate


substrate_name: cannabigerolic acid

proof_lines: kcat is 0.30 sec(-1) for cannabigerolate.

substrate: cannabigerolic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GTB6 and applied mutation signature R110A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GTB6 and applied mutation signature R108A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 5; 303.15 K; buffer 100 mM sodium citrate

proof_lines: mutant enzyme R108A, in 100 mM sodium citrate buffer (pH 5.0), at 30°C


proof_lines: wild type enzyme, in 100 mM sodium citrate buffer (pH 5.0), at 30°C


proof_lines: mutant enzyme R110A, in 100 mM sodium citrate buffer (pH 5.0), at 30°C


enzyme_display_name: sphingomyelin phosphodiesterase D

organism: Corynebacterium pseudotuberculosis

substrate_name: H2O; 1-Oleoylglycerophosphocholine

sequence_source: UniProtKB reviewed accession P20626, fetched by direct accession lookup on 2026-06-27

enzyme: sphingomyelin phosphodiesterase D

substrate: H2O; 1-Oleoylglycerophosphocholine


organism: Loxosceles intermedia

substrate_name: sphingomyelin

sequence_source: UniProtKB reviewed accession P0CE81, fetched by direct accession lookup on 2026-06-27

substrate: sphingomyelin


organism: Loxosceles laeta

sequence_source: UniProtKB reviewed accession Q8I914, fetched by direct accession lookup on 2026-06-27

proof_lines: recombinant enzyme SMase II, in HEPES-buffered saline at 37°C


sequence_source: UniProtKB reviewed accession Q8I912, fetched by direct accession lookup on 2026-06-27

proof_lines: recombinant enzyme SMase I, in HEPES-buffered saline at 37°C

proof_lines: crude enzyme, in HEPES-buffered saline at 37°C


proof_lines:
37°C, pH 7.4, sphingomyelinase P2
at pH 7.4 and 37°C


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


organism: Rattus norvegicus


enzyme_display_name: protein arginine phosphatase

substrate_name: [culpeine]-Nomega-phospho-L-arginine

enzyme: protein arginine phosphatase

substrate: [culpeine]-Nomega-phospho-L-arginine


organism: Bacillus subtilis (strain 168)

substrate_name: p-nitrophenyl-phosphate (at 37 degrees Celsius and pH 5.5)

proof_lines: kcat is 0.010 sec(-1) with pNPP as substrate (at 37 degrees Celsius and pH 5.5) (PubMed:15995210). kcat is 0.13 sec(-1) with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242). pNPP is a phosphotyrosine mimicking compound.


organism: Geobacillus stearothermophilus

substrate_name: p-nitrophenyl-phosphate (at 25 degrees Celsius and pH 7.6)

proof_lines: kcat is 1.12 sec(-1) with pNPP as substrate (at 25 degrees Celsius and pH 7.6) (PubMed:23838530) and 3.2 sec(-1) with pNPP as substrate (at 40 degrees Celsius and pH 8.0) (PubMed:23770242). pNPP is a phosphotyrosine mimicking compound.


organism: Drosophila melanogaster

substrate_name: phospho-L-arginine

sequence_source: UniProtKB Q8ING6, live TrEMBL entry Q8ING6_DROME

substrate: phospho-L-arginine


substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB S0F332, reviewed Swiss-Prot entry PAP_GEOSE

substrate: 4-nitrophenyl phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB S0F332 plus C14S reconstruction from the source mutation signature and applied mutation signature C14S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB S0F332 plus C14S reconstruction from the source mutation signature


enzyme_display_name: chondroitin 4-sulfotransferase

organism: Homo sapiens

substrate_name: PAPS

enzyme: chondroitin 4-sulfotransferase

substrate: PAPS


proof_lines:
pH 6.8, 37°C, in presence of protamine
pH 6.8, 37°C, in addition of spermine
pH 6.8, 37°C, in addition of Mn2+


proof_lines: pH 6.8, 37°C, mutant with deletion of C-terminal glycosylation site


substrate_name: 3'-phosphoadenylyl sulfate

sequence_source: UniProtKB reviewed FASTA accession Q9NPF2, retrieved by direct accession lookup on 2026-06-27.

proof_lines: pH 7.0, 37°C, recombinant enzyme expressed in Escherichia coli

proof_lines: pH 7.0, 37°C, recombinant enzyme expressed in Pichia pastoris

substrate: 3'-phosphoadenylyl sulfate


organism: Mus musculus

substrate_name: 3'-Phosphoadenylyl sulfate; Chondroitin

sequence_source: UniProtKB reviewed FASTA accession Q9JME2, retrieved by direct accession lookup on 2026-06-27.

substrate: 3'-Phosphoadenylyl sulfate; Chondroitin


sequence_source: UniProtKB reviewed FASTA accession P69478, retrieved by direct accession lookup on 2026-06-27.


enzyme_display_name: CMP-N-acetylneuraminate monooxygenase

organism: Asterias rubens

substrate_name: CMP-N-acetylneuraminate

proof_lines: pH 6.4, 25°C, soluble form of ferrocytochrome b5

proof_lines: pH 6.4, 25°C, amphiphilic form of ferrocytochrome b5

enzyme: CMP-N-acetylneuraminate monooxygenase

substrate: CMP-N-acetylneuraminate


proof_lines:
pH 7.4, 37°C, soluble system
pH 7.5, 37°C
pH 7.4, 37°C, amphiphilic system


organism: Sus scrofa

proof_lines: pH 7.4, 37°C, reconstituted system consisting of purified hydroxylase, cytochrome b5, cytochrome b5 reductase and catalase

proof_lines: pH 7.4, 37°C, purified hydroxylase in presence of Triton X-100 solubilized microsomes

proof_lines: pH 7.4, 37°C, enzyme from submaxillary gland


substrate_name: CMP-NeuAc

substrate: CMP-NeuAc


substrate_name: H+; O2; Ferrocytochrome b5; CMP-N-acetylneuraminate

sequence_source: UniProtKB Q95V11 reviewed Swiss-Prot entry CMAH_ASTRU, checked 2026-06-27 via UniProt REST


substrate_name: Ferrocytochrome b5; H+; O2; CMP-N-acetylneuraminate

sequence_source: UniProtKB Q61419 reviewed Swiss-Prot entry CMAH_MOUSE, checked 2026-06-27 via UniProt REST

assay_conditions_summary: cofactor NADH


substrate_name: cytochrome b5

proof_lines: Decreased enzyme activity in presence of 100 mM of NaCl.

substrate: cytochrome b5


enzyme_display_name: nucleoside-phosphate kinase

substrate_name: dAMP

proof_lines: isoform AMPK1, in 50 mM Tris/HCl (pH 7.4), 50 mM KCl, 5 mM MgCl2, at 37°C

proof_lines: in Tris-HCl (50 mM, pH 7.4), KCl (50 mM), MgCl2 (5 mM), at 37°C

proof_lines: isoform AMPK2, in 50 mM Tris/HCl (pH 7.4), 50 mM KCl, 5 mM MgCl2, at 37°C

enzyme: nucleoside-phosphate kinase

substrate: dAMP


substrate_name: ATP; AMP

sequence_source: UniProtKB reviewed accession Q5TCS8 direct REST check on 2026-06-27

assay_conditions_summary: cofactor ATP

substrate: ATP; AMP


organism: Gallus gallus

substrate_name: ATP

substrate: ATP


substrate_name: AMP with ATP as phosphate donor

substrate: AMP with ATP as phosphate donor


substrate_name: AMP (with ATP as phosphate donor)

substrate: AMP (with ATP as phosphate donor)


substrate_name: ThDP

assay_conditions_summary: cofactor ADP

substrate: ThDP


substrate_name: O-(alpha-L-iduronic acid 2-sulfate)-(1-4)-D-O-(alpha 2-sulfaminoglucosamine 6-sulfate)-(1-4)-L-O-(alpha-L-iduronic acid 2-sulfate)-D-O-2,5-anhydro-mannitol 6-sulfate

proof_lines:
pH dependent
recombinant protein
in presence of 7 mM NaCl


substrate_name: O-(alpha-L-Idopyranosyluronic acid 2-sulfate)-(1->4)-2,5-anhydro-D-mannitol 6-sulfate; H2O

sequence_source: UniProtKB reviewed accession P22304, direct UniProt REST lookup


substrate_name: sphingomyelin

proof_lines: recombinant enzyme SMase II, in HEPES-buffered saline at 37°C


enzyme_display_name: 2-acylglycerol O-acyltransferase

organism: Arachis hypogaea

substrate_name: oleoyl-CoA

enzyme: 2-acylglycerol O-acyltransferase

substrate: oleoyl-CoA


organism: Locusta migratoria


organism: Zonotrichia albicollis

substrate_name: linoleoyl-CoA

substrate: linoleoyl-CoA


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


substrate_name: oleoyl-CoA; 1-oleoyl-sn-glycerol

sequence_source: UniProtKB REST exact accession lookup for H9LBH7; TrEMBL entry H9LBH7_ARAHY, sequence version 1, organism Arachis hypogaea.

proof_lines: pH and temperature not specified in the publication

substrate: oleoyl-CoA; 1-oleoyl-sn-glycerol


substrate_name: sn-1-Monooleoylglycerol; Oleoyl-CoA

sequence_source: UniProtKB REST exact accession lookup for Q3SYC2; reviewed Swiss-Prot entry MOGT2_HUMAN, sequence version 2, organism Homo sapiens.

substrate: sn-1-Monooleoylglycerol; Oleoyl-CoA


enzyme_display_name: heparanase

substrate_name: fondaparinux

enzyme: heparanase

substrate: fondaparinux


substrate_name: M09 S05a, a heparin sulfate analog with a nonasaccharide with N-sulfation and a single GlcNS(6S) toward the reducing end


substrate_name: fondaparinux / heparan sulfate disaccharide source labels unresolved

sequence_source: UniProtKB reviewed accession Q9Y251 direct lookup; entry HPSE_HUMAN, Homo sapiens heparanase, EC 3.2.1.166


assay_conditions_summary: pH 5


enzyme_display_name: allantoinase

organism: Phaseolus vulgaris

substrate_name: allantoin

proof_lines: pH 7.8, 40°C, isozyme IsoI, different methods

proof_lines: pH 7.8, 40°C, isozyme IsoII, different methods

enzyme: allantoinase

substrate: allantoin


organism: Unknown

substrate_name: (S)-allantoin

substrate: (S)-allantoin


organism: Cajanus cajan


organism: Escherichia coli

proof_lines:
pH 7.4, 37°C, Zn2+-amended culture
pH 7.4, 37°C, Co2+-amended culture
pH 7.4, 37°C, Ni2+-amended culture


organism: Glycine max

substrate_name: H2O; (S)(+)-Allantoin

substrate: H2O; (S)(+)-Allantoin


organism: Lathyrus sativus


organism: Pseudomonas aeruginosa


organism: Ricinus communis


organism: Salmonella enterica

proof_lines: pH 8.0, 25°C, recombinant enzyme, in presence of phthalimide

proof_lines: pH 8.0, 25°C, recombinant enzyme, in presence of dihydroorotate


organism: Vigna radiata


organism: Vigna unguiculata subsp. cylindrica

proof_lines:
pH 7.5
pH 4


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)

substrate_name: allantoin (at 40 degrees Celsius and pH 8.0)


proof_lines:
Zn2+-activated enzyme, pH 8.0, 25°C
Mn2+-activated enzyme, pH 8.0, 25°C
Ni2+-activated enzyme, pH 8.0, 25°C


organism: Pseudomonas fluorescens

sequence_source: UniProtKB B5L363 FASTA, checked 2026-06-27


sequence_source: UniProtKB REST direct accession check, Q94AP0, 2026-06-27

column_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013), row 'AtALN': column 'Km' = 5,472; column 'kcat (s^-1)' = 879; column 'Catalytic Efficiency (s^-1 M^-1)' = 1.61 x 10^5; column 'Specific Activity (units mg^-1)' is printed but is not one of the export schema's kinetic metrics.

normalized_value_unit_evidence: Km: printed cell 5,472 uM; 5,472 uM / 1000 = 5.472 mM, equal to the catalog value. kcat: printed cell 879 s^-1; no unit conversion needed, equal to the catalog value. This catalog row does not carry a catalytic-efficiency value, so no ratio is exported or proposed here.

row_label: Table I, row 'AtALN' (Plant Physiol. 163:672-681, 2013)


substrate_name: (S)(+)-Allantoin

normalized_value_unit_evidence: Km: printed cell 5,472 uM; 5,472 uM / 1000 = 5.472 mM. kcat: printed cell 879 s^-1; no unit conversion needed. Catalytic Efficiency: printed cell 1.61 x 10^5 s^-1 M^-1; 1.61 x 10^5 s^-1 M^-1 / 1000 = 161.0 s^-1 mM^-1. This paper prints its own Catalytic Efficiency cell for this row; it is an independently reported primary value and it does not equal the quotient computed from the row's own kcat and Km (879.0 / 5.472 = 160.63596491228068). The catalog carries the quotient; this record proposes the paper's own printed value (161.0) as the catalytic-efficiency correction, per the ratio policy for an independently reported primary catalytic-efficiency cell.

raw_value_unit_evidence: Table I, row 'AtALN' (Plant Physiol. 163:672-681, 2013): Km = 5,472 uM; kcat = 879 s^-1; printed Catalytic Efficiency = 1.61 x 10^5 s^-1 M^-1.

table_label: Table I: Kinetic constants (Plant Physiol. 163:672-681, 2013)

substrate: (S)(+)-Allantoin


organism: Bacillus licheniformis

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, L0CR34, with row-specific T155Y reconstruction, 2026-06-27 and applied mutation signature T155Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, L0CR34, with row-specific T155A reconstruction, 2026-06-27 and applied mutation signature T155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, L0CR34, with row-specific S292A reconstruction, 2026-06-27 and applied mutation signature S292A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct accession check, L0CR34, with row-specific S292A reconstruction, 2026-06-27


sequence_source: UniProtKB REST direct accession check, L0CR34, with row-specific T155A reconstruction, 2026-06-27


sequence_source: UniProtKB REST direct accession check, L0CR34, with row-specific T155Y reconstruction, 2026-06-27


sequence_source: UniProtKB REST direct accession check, L0CR34, 2026-06-27

proof_lines: pH 7.5, 50°C, recombinant wild-type enzyme and mutant S292A


substrate_name: H2O; Allantoin

sequence_source: UniProtKB REST direct accession check, P77671, 2026-06-27

substrate: H2O; Allantoin


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, P77671, with row-specific R215K reconstruction, 2026-06-27 and applied mutation signature R215K to reconstruct the assayed variant sequence.

proof_lines: mutant R215K, supplementation with zinc acetate


proof_lines: wild-type allantoinase, supplementation with zinc acetate

proof_lines: selenomethionine-substituted wild-type allantoinase, no supplementation with zinc acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, P77671, with row-specific S288D reconstruction, 2026-06-27 and applied mutation signature S288D to reconstruct the assayed variant sequence.

proof_lines: mutant S288D, supplementation with zinc acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check, P77671, with row-specific S288V reconstruction, 2026-06-27 and applied mutation signature S288V to reconstruct the assayed variant sequence.

proof_lines: mutant S288V, supplementation with zinc acetate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 11.7 min(-1) for cholesterol as substrate. kcat is 1.5 min(-1) for cholest-4-en-3-one as substrate.


proof_lines: kcat is 84 min(-1) for cholest-4-en-3-one as substrate (PubMed:20843794). kcat is 16.7 min(-1) for cholesterol as substrate (PubMed:20843794). kcat is 0.0062 min(-1) for cholest-4-en-3-one as substrate (PubMed:20889498).


organism: Mycobacterium tuberculosis


sequence_source: UniProtKB reviewed accession P9WPL5 direct lookup; UniProtKB ID CP142_MYCTU; CRC64 BCFF3C23ECB5767F

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5


organism: Mycolicibacterium smegmatis

sequence_source: UniProtKB reviewed accession A0R4Q6 direct lookup; UniProtKB ID CP142_MYCS2; CRC64 9195ECA2F9D8D509

proof_lines:
at pH 7.4 and 25°C
Raw SKiD Env: Temp=25°C, pH=7.4


enzyme_display_name: very-long-chain 3-oxoacyl-CoA synthase

organism: Saccharomyces cerevisiae

substrate_name: lauroyl-CoA

assay_conditions_summary: pH 6.7; 303.15 K; cofactor CoA

proof_lines: in 10 mM Tris/maleic acid pH 6.7, 0.65 M mannitol and 0.36 mM EGTA, at 30°C

enzyme: very-long-chain 3-oxoacyl-CoA synthase

substrate: lauroyl-CoA


organism: Homo sapiens

substrate_name: alpha-Linolenoyl-CoA; Malonyl-CoA

substrate: alpha-Linolenoyl-CoA; Malonyl-CoA


substrate_name: palmitoyl-CoA

assay_conditions_summary: pH 6.8; 310.15 K; cofactor CoA

substrate: palmitoyl-CoA


substrate_name: Malonyl-CoA; Octanoyl-CoA

substrate: Malonyl-CoA; Octanoyl-CoA


substrate_name: hexadecanoyl-CoA (at 37 degrees Celsius and pH 6.8)

assay_conditions_summary: pH 6.8; cofactor CoA


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


enzyme_display_name: inosine kinase

organism: Helianthus tuberosus

substrate_name: Inosine

enzyme: inosine kinase

substrate: Inosine


organism: Limnospira platensis


organism: Mus musculus


substrate_name: guanosine

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

substrate: guanosine


organism: Exiguobacterium acetylicum


organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: ATP (at 70 degrees Celsius)

substrate: ATP (at 70 degrees Celsius)


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: guanosine (at pH 8.0 and 22 degrees Celsius)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 0.072 sec(-1) with ATP and guanosine as substrates. kcat is 0.16 sec(-1) with ATP and inosine as substrates. kcat is 0.064 sec(-1) with ATP and cytidine as substrates. kcat is 0.084 sec(-1) with ATP and adenosine as substrates. kcat


enzyme_display_name: trehalose 2-sulfotransferase

organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: 3'-phosphoadenylyl sulfate

sequence_source: source_record; direct UniProt A0QQ53 FASTA checksum match

proof_lines: kcat is 1.6 sec(-1) (PubMed:15258569). kcat is 134 min(-1) toward trehalose and 96 min(-1) toward PAPS (PubMed:15866533).

enzyme: trehalose 2-sulfotransferase

substrate: 3'-phosphoadenylyl sulfate


sequence_source: Direct UniProtKB lookup for source accession O53699 on 2026-06-27

proof_lines: pH 7.5, 22°C, competitive inhibitor with regard to 3-phosphoadenylyl sulfate

proof_lines: pH 7.5, 22°C, noncompetitive inhibitor with regard to trehalose


substrate_name: alpha,alpha-trehalose

sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup for source accession P84151 plus E36Q substitution reconstructed on 2026-06-27 and applied mutation signature E36Q to reconstruct the assayed variant sequence.

substrate: alpha,alpha-trehalose


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup for source accession P84151 plus E33A substitution reconstructed on 2026-06-27 and applied mutation signature E33A to reconstruct the assayed variant sequence.


sequence_source: Direct UniProtKB lookup for source accession P84151 on 2026-06-27

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


sequence_source: Direct UniProtKB lookup for source accession P84151 plus E36Q substitution reconstructed on 2026-06-27


sequence_source: Direct UniProtKB lookup for source accession P84151 plus E33A substitution reconstructed on 2026-06-27


organism: Escherichia coli

substrate_name: dATP

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines:
pH 7.2, 30°C, guanosine kinase reaction
pH 7.2, 30°C
pH 7.2, 30°C, inosine kinase reaction

substrate: dATP


organism: Rattus norvegicus

assay_conditions_summary: cofactor CoA


substrate_name: Unknown

substrate: Unknown


organism: Arachis hypogaea

substrate_name: oleoyl-CoA

sequence_source: UniProtKB:H9LBH7 cross-checked against NCBI Protein AEA11209.1 / EMBL JF340215.1

proof_lines: pH and temperature not specified in the publication

substrate: oleoyl-CoA


sequence_source: UniProtKB reviewed accession O53699 direct REST/FASTA lookup on 2026-06-27


enzyme_display_name: succinyl-CoA:mesaconate CoA transferase

organism: Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 / VKM B-1755)

substrate_name: succinyl-CoA (in the presence of 10 mM mesaconate)

enzyme: succinyl-CoA:mesaconate CoA transferase


organism: Haloarcula hispanica

substrate_name: mesaconate

sequence_source: UniProtKB reviewed accession G0HQ31 (MCT_HALHT), fetched via UniProt REST on 2026-06-27

assay_conditions_summary: pH 7.8; 310.15 K; cofactor CoA

substrate: mesaconate


substrate_name: succinyl-CoA

substrate: succinyl-CoA


proof_lines:
37°C, pH 7.8
37°C, pH 7.8, 1 mM succinyl-CoA
37°C, pH 7.8, 5 mM succinyl-CoA


enzyme_display_name: FMN hydrolase

organism: Arabidopsis thaliana

substrate_name: FMN

sequence_source: source_record; direct UniProt accession check for Q84VZ1 matched the selected source sequence

assay_conditions_summary: cofactor FMN

proof_lines: kcat is 0.59 sec(-1) for FMN (PubMed:22002057). kcat is 2.80 sec(-1) for 5-amino-6-(5-phospho-D-ribitylamino)uracil (PubMed:27490826).

enzyme: FMN hydrolase

substrate: FMN


organism: Capra hircus

assay_conditions_summary: pH 5; 323.15 K; cofactor FMN


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

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


assay_conditions_summary: pH 5; 298.15 K; cofactor FAD


substrate_name: riboflavin (at pH 7.5)

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

assay_conditions_summary: pH 7.5; cofactor FMN

substrate: riboflavin (at pH 7.5)


sequence_source: UniProtKB reviewed entry Q84MD8 direct REST/FASTA lookup

assay_conditions_summary: pH 7.5; 303.15 K; cofactor FMN


sequence_source: UniProtKB unreviewed entry F4HQA8 direct REST/FASTA lookup

assay_conditions_summary: pH 8; 303.15 K; cofactor FMN


enzyme_display_name: D-dopachrome decarboxylase

substrate_name: D-dopachrome

enzyme: D-dopachrome decarboxylase

substrate: D-dopachrome


sequence_source: UniProtKB reviewed accession P30046, D-dopachrome decarboxylase, Homo sapiens, EC 4.1.1.84

proof_lines:
pH 6.2, 23°C
Raw SKiD Env: Temp=25°C, pH=6.5


sequence_source: UniProtKB reviewed accession P30046 plus PMID 9480844 P1A mutation context

sequence_variant_note: Mutation signature P1A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_source: UniProtKB reviewed accession P80254, D-dopachrome decarboxylase, Rattus norvegicus, EC 4.1.1.84


enzyme_display_name: cellobiose phosphorylase

organism: Unknown

substrate_name: cellobiose

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

enzyme: cellobiose phosphorylase

substrate: cellobiose


organism: Acetivibrio thermocellus

sequence_source: UniProtKB Q8VP44 canonical sequence direct lookup; retrieved 2026-06-27.

proof_lines: synthetic reaction, wild-type, pH 7.5, 45°C

proof_lines: phosphorolytic reaction, wild-type, pH 7.5, 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8VP44 canonical sequence reconstructed with selected mutation signature S497G; retrieved 2026-06-27. and applied mutation signature S497G to reconstruct the assayed variant sequence.

proof_lines: synthetic reaction, mutant S497G, pH 7.5, 45°C

proof_lines: phosphorolytic reaction, mutant S497G, pH 7.5, 50°C


organism: Caldicellulosiruptor bescii

sequence_source: UniProtKB direct lookup B9MNR3 (2026-06-27) returned no live sequence.


organism: Cellulomonas uda

substrate_name: lactose

sequence_source: UniProtKB Q7WTR6 canonical sequence direct lookup; retrieved 2026-06-27.

column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'CP', lactose phosphorolysis block: column 'kcat (s^-1)' = 0.109; column 'Km (mM)' = 228; column 'kcat/Km (M^-1 s^-1)' = 0.48.

normalized_value_unit_evidence: kcat: printed Table III cell 0.109 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 0.109 s^(-1). Km: printed Table III cell 228 mM; the column head prints mM, so no unit conversion applies and the paper value is 228.0 mM. kcat/Km: printed Table III cell 0.48 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.48 / 1000 = 0.00048 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row CP (wild-type), lactose phosphorolysis block: kcat = 0.109 s^-1; Km = 228 mM; printed kcat/Km = 0.48 M^-1 s^-1.

row_label: Table III, row CP (wild-type), lactose phosphorolysis columns

substrate: lactose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q7WTR6 and applied mutation signature T508A/N667T to reconstruct the assayed variant sequence.

column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'LP2', lactose phosphorolysis block: column 'kcat (s^-1)' = 0.53; column 'Km (mM)' = 254; column 'kcat/Km (M^-1 s^-1)' = 2.07.

normalized_value_unit_evidence: kcat: printed Table III cell 0.53 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 0.53 s^(-1). Km: printed Table III cell 254 mM; the column head prints mM, so no unit conversion applies and the paper value is 254.0 mM. kcat/Km: printed Table III cell 2.07 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.07 / 1000 = 0.00207 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row LP2 (T508A/N667T), lactose phosphorolysis block: kcat = 0.53 s^-1; Km = 254 mM; printed kcat/Km = 2.07 M^-1 s^-1.

row_label: Table III, row LP2 (T508A/N667T), lactose phosphorolysis columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature T508I/N667A; retrieved 2026-06-27. and applied mutation signature T508I/N667A to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 37°C, recombinant mutant T508I/N667A


column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'LP2', cellobiose phosphorolysis block: column 'kcat (s^-1)' = 2.61; column 'Km (mM)' = 2.9; column 'kcat/Km (M^-1 s^-1)' = 904.

normalized_value_unit_evidence: kcat: printed Table III cell 2.61 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 2.61 s^(-1). Km: printed Table III cell 2.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 2.9 mM. kcat/Km: printed Table III cell 904 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 904 / 1000 = 0.904 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row LP2 (T508A/N667T), cellobiose phosphorolysis block: kcat = 2.61 s^-1; Km = 2.9 mM; printed kcat/Km = 904 M^-1 s^-1.

row_label: Table III, row LP2 (T508A/N667T), cellobiose phosphorolysis columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature T508A/N667T; retrieved 2026-06-27. and applied mutation signature T508A/N667T to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 37°C, recombinant mutant T508A/N667T


column_label: Table III. Kinetic parameters of wild-type CP and enzyme variants for phosphorolysis of cellobiose and lactose (Protein Engineering, Design & Selection 2009, 22(7):393-399), enzyme row 'CP', cellobiose phosphorolysis block: column 'kcat (s^-1)' = 13.2; column 'Km (mM)' = 2.9; column 'kcat/Km (M^-1 s^-1)' = 4557.

normalized_value_unit_evidence: kcat: printed Table III cell 13.2 s^-1; the column head prints s^-1, so no unit conversion applies and the paper value is 13.2 s^(-1). Km: printed Table III cell 2.9 mM; the column head prints mM, so no unit conversion applies and the paper value is 2.9 mM. kcat/Km: printed Table III cell 4557 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4557 / 1000 = 4.557 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row CP (wild-type), cellobiose phosphorolysis block: kcat = 13.2 s^-1; Km = 2.9 mM; printed kcat/Km = 4557 M^-1 s^-1.

row_label: Table III, row CP (wild-type), cellobiose phosphorolysis columns


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature A397V/T508A/A512T/D557N/N667T/G681S; retrieved 2026-06-27. and applied mutation signature A397V/T508A/A512T/D557N/N667T/G681S to reconstruct the assayed variant sequence.

proof_lines: pH 6.6, 37°C, recombinant mutant A397V/T508A/A512T/D557N/N667T/G681S


sequence_source: UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature T508I/N667A; retrieved 2026-06-27.


proof_lines: pH 6.6, 37°C, recombinant wild-type enzyme


sequence_source: UniProtKB Q7WTR6 canonical sequence reconstructed with selected mutation signature A397V/T508A/A512T/D557N/N667T/G681S; retrieved 2026-06-27.


organism: Thermoclostridium stercorarium


organism: Thermosipho africanus

substrate_name: D-glucose

assay_conditions_summary: pH 7.5; 348.15 K; buffer a 200 microlitre reaction of 50 mM Tris-HCl

column_label: Table 3: Kinetic parameters for the synthetic reaction catalyzed by TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 3, row d-Glucose; column Km (mM) = 14.3; column kcat (s-1) = 30.3; column kcat/Km (s-1 mM-1) = 2.12. captured primary segment: d-Glucose | Km 14.3 mM | kcat 30.3 s-1 | kcat / Km 2.12 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 30.3 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 30.3 s^(-1); the exported value is 30.3 s^(-1). Km: printed Table 3 cell 14.3 mM; the column head prints mM, so no unit conversion applies and the paper value is 14.3 mM; the exported value is 14.3 mM. kcat/Km: printed Table 3 cell 2.12 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 2.12 s^(-1)*mM^(-1); the exported value 2.1188811188811187 s^(-1)*mM^(-1) is the full-precision quotient 30.3 / 14.3 = 2.1188811188811187 of the same two printed cells, and the printed efficiency cell 2.12 is that quotient written to the two decimals Table 3 uses.

raw_value_unit_evidence: Table 3, row d-Glucose: Km = 14.3 mM; kcat = 30.3 s-1; printed kcat/Km = 2.12 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 3, row d-Glucose

substrate: D-glucose


substrate_name: cellopentaose; D-xylose; cellotriose; D-glucose; cellotetraose; cellobiose; alpha-D-glucose 1-phosphate


substrate_name: cellopentaose

assay_conditions_summary: pH 7.5; 348.15 K; buffer a 40 microlitre reaction of 100 mM sodium phosphate

column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellopentaose; column Km (mM) = 0.060; column kcat (s-1) = 0.34; column kcat/Km (s-1 mM-1) = 5.67. captured primary segment: Cellopentaose | Km 0.060 mM | kcat 0.34 s-1 | kcat / Km 5.67 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.34 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.34 s^(-1); the exported value is 0.34 s^(-1). Km: printed Table 4 cell 0.060 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.06 mM; the exported value is 0.06 mM. kcat/Km: printed Table 4 cell 5.67 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 5.67 s^(-1)*mM^(-1); the exported value 5.666666666666667 s^(-1)*mM^(-1) is the full-precision quotient 0.34 / 0.060 = 5.666666666666667 of the same two printed cells, and the printed efficiency cell 5.67 is that quotient written to the two decimals Table 4 uses.

raw_value_unit_evidence: Table 4, row Cellopentaose: Km = 0.060 mM; kcat = 0.34 s-1; printed kcat/Km = 5.67 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellopentaose

substrate: cellopentaose


column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellobiose; column Km (mM) = 0.120; column kcat (s-1) = 0.23; column kcat/Km (s-1 mM-1) = 1.92. captured primary segment: Cellobiose | Km 0.120 mM | kcat 0.23 s-1 | kcat / Km 1.92 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.23 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.23 s^(-1); the exported value is 0.23 s^(-1). Km: printed Table 4 cell 0.120 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.12 mM; the exported value is 0.12 mM. kcat/Km: printed Table 4 cell 1.92 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 1.92 s^(-1)*mM^(-1); the exported value 1.9166666666666667 s^(-1)*mM^(-1) is the full-precision quotient 0.23 / 0.120 = 1.9166666666666667 of the same two printed cells, and the printed efficiency cell 1.92 is that quotient written to the two decimals Table 4 uses.

raw_value_unit_evidence: Table 4, row Cellobiose: Km = 0.120 mM; kcat = 0.23 s-1; printed kcat/Km = 1.92 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellobiose


substrate_name: D-Xylose

column_label: Table 3: Kinetic parameters for the synthetic reaction catalyzed by TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 3, row d-Xylose; column Km (mM) = 25.7; column kcat (s-1) = 1.37; column kcat/Km (s-1 mM-1) = 0.05. captured primary segment: d-Xylose | Km 25.7 mM | kcat 1.37 s-1 | kcat / Km 0.05 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.37 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 1.37 s^(-1); the exported value is 1.37 s^(-1). Km: printed Table 3 cell 25.7 mM; the column head prints mM, so no unit conversion applies and the paper value is 25.7 mM; the exported value is 25.7 mM. kcat/Km: printed Table 3 cell 0.05 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 0.05 s^(-1)*mM^(-1); the exported value 0.053307392996108954 s^(-1)*mM^(-1) is the full-precision quotient 1.37 / 25.7 = 0.053307392996108954 of the same two printed cells, and the printed efficiency cell 0.05 is that quotient written to the two decimals Table 3 uses.

raw_value_unit_evidence: Table 3, row d-Xylose: Km = 25.7 mM; kcat = 1.37 s-1; printed kcat/Km = 0.05 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 3, row d-Xylose

substrate: D-Xylose


substrate_name: cellotetraose

column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellotetraose; column Km (mM) = 0.062; column kcat (s-1) = 0.49; column kcat/Km (s-1 mM-1) = 7.91. captured primary segment: Cellotetraose | Km 0.062 mM | kcat 0.49 s-1 | kcat / Km 7.91 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.49 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.49 s^(-1); the exported value is 0.49 s^(-1). Km: printed Table 4 cell 0.062 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.062 mM; the exported value is 0.062 mM. kcat/Km: printed Table 4 cell 7.91 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 7.91 s^(-1)*mM^(-1); the exported value 7.903225806451613 s^(-1)*mM^(-1) is the quotient 0.49 / 0.062 = 7.903225806451613 of the two printed component cells, whereas the paper's own printed efficiency cell is 7.91; the printed cell governs and kcat_over_km is corrected to 7.91 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, row Cellotetraose: Km = 0.062 mM; kcat = 0.49 s-1; printed kcat/Km = 7.91 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellotetraose

substrate: cellotetraose


substrate_name: cellotriose

column_label: Table 4: Kinetic parameters for the phosphorolytic reaction of TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 4, row Cellotriose; column Km (mM) = 0.094; column kcat (s-1) = 0.28; column kcat/Km (s-1 mM-1) = 2.98. captured primary segment: Cellotriose | Km 0.094 mM | kcat 0.28 s-1 | kcat / Km 2.98 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.28 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 0.28 s^(-1); the exported value is 0.28 s^(-1). Km: printed Table 4 cell 0.094 mM; the column head prints mM, so no unit conversion applies and the paper value is 0.094 mM; the exported value is 0.094 mM. kcat/Km: printed Table 4 cell 2.98 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 2.98 s^(-1)*mM^(-1); the exported value 2.9787234042553195 s^(-1)*mM^(-1) is the full-precision quotient 0.28 / 0.094 = 2.9787234042553195 of the same two printed cells, and the printed efficiency cell 2.98 is that quotient written to the two decimals Table 4 uses.

raw_value_unit_evidence: Table 4, row Cellotriose: Km = 0.094 mM; kcat = 0.28 s-1; printed kcat/Km = 2.98 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 4, row Cellotriose

substrate: cellotriose


substrate_name: alpha-D-glucose 1-phosphate

column_label: Table 3: Kinetic parameters for the synthetic reaction catalyzed by TaCBP (Scientific Reports 2017, volume 7, article 4849); printed column heads Substrate | Km (mM) | kcat (s-1) | kcat/Km (s-1 mM-1). Table 3, row G-1-P; column Km (mM) = 1.57; column kcat (s-1) = 7.61; column kcat/Km (s-1 mM-1) = 4.85. captured primary segment: G-1-P | Km 1.57 mM | kcat 7.61 s-1 | kcat / Km 4.85 s-1 mM-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 7.61 s-1; the column head prints s-1, so no unit conversion applies and the paper value is 7.61 s^(-1); the exported value is 7.61 s^(-1). Km: printed Table 3 cell 1.57 mM; the column head prints mM, so no unit conversion applies and the paper value is 1.57 mM; the exported value is 1.57 mM. kcat/Km: printed Table 3 cell 4.85 s-1 mM-1; the column head prints s-1 mM-1, so no unit conversion applies and the printed cell is 4.85 s^(-1)*mM^(-1); the exported value 4.8471337579617835 s^(-1)*mM^(-1) is the full-precision quotient 7.61 / 1.57 = 4.8471337579617835 of the same two printed cells, and the printed efficiency cell 4.85 is that quotient written to the two decimals Table 3 uses.

raw_value_unit_evidence: Table 3, row G-1-P: Km = 1.57 mM; kcat = 7.61 s-1; printed kcat/Km = 4.85 s-1 mM-1 (the fourth column head prints the unit s-1 mM-1).

row_label: Table 3, row G-1-P

substrate: alpha-D-glucose 1-phosphate


organism: Thermotoga neapolitana


substrate_name: Phosphate; Cellobiose; Phosphate; Cellobiose; D-Glucose; D-Glucose 1-phosphate


substrate_name: Cellobiose

assay_conditions_summary: pH 5.5; 358.15 K; buffer PC (sodium phosphate-sodium citrate; cofactor NADPH

column_label: Results, Characterization of CbpA, journal page 5175 (PDF page 4), left column, final sentence of the paragraph (J. Bacteriol. 2000, 182(18): 5172-5179); measurement CbpA phosphorolysis of cellobiose; construct recombinant wild-type CbpA of Thermotoga neapolitana expressed in Escherichia coli; substrate cellobiose; single reported measurement; condition pH 5.5, 85 C (358.15 K); the cellobiose phosphorylase assay incubated the enzyme at 85 C in PC (sodium phosphate-sodium citrate) buffer (pH 5.5) with cellobiose and measured the glucose 1-phosphate formed by phosphorolysis through a coupled enzyme assay following NADPH at 340 nm; the kinetic constants were determined by fitting data to the Michaelis-Menten equation using linear regression. Km 1.42 mM. kcat 26.3 s^-1. kcat/Km 18.3 s^-1 mM^-1. captured primary segment: Results, Characterization of CbpA (journal page 5175, PDF page 4, left column) | construct recombinant wild-type CbpA of Thermotoga neapolitana expressed in Escherichia coli | substrate cellobiose | condition cellobiose phosphorylase assay in PC buffer (pH 5.5) at 85 C | Km 1.42 mM | kcat 26.3 s^-1 | kcat/Km 18.3 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed value 1.42 mM; already in millimolar, so no unit conversion applies and the paper value is 1.42 mM. kcat: printed value 26.3 s^-1; already per second, so no unit conversion applies and the paper value is 26.3 s^(-1). kcat/Km: printed value 18.3 s^-1 mM^-1; already per second per millimolar, so no unit conversion applies and the printed value is 18.3 s^(-1)*mM^(-1). Quotient disclosure for this measurement: 26.3 / 1.42 = 18.52112676056338 s^-1 mM^-1.

raw_value_unit_evidence: Results, Characterization of CbpA (journal page 5175, PDF page 4, left column): the Km for cellobiose was 1.42 mM, the kcat was 26.3 s^-1, and kcat/Km was 18.3 s^-1 mM^-1.

substrate: Cellobiose


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


organism: Cellulomonas gilvus

proof_lines: enzyme assay at 37°C in 50 mM Tris/HCl (pH 7.0)


substrate_name: methyl beta-D-glucoside

substrate: methyl beta-D-glucoside


proof_lines: pH 6.6, 30°C, recombinant His6-tagged enzyme

proof_lines: in presence of saturating concentrations of phosphate


organism: Ruminococcus albus


enzyme_display_name: FAD diphosphatase

substrate_name: FAD; H2O

sequence_source: UniProtKB reviewed entry P93740 / NUD23_ARATH, sequence version 2, accessed 2026-06-27

assay_conditions_summary: cofactor FAD

enzyme: FAD diphosphatase

substrate: FAD; H2O


organism: Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E)


organism: Chlamydomonas reinhardtii

substrate_name: FMN / FAD (30 degrees Celsius, pH 7.0)

assay_conditions_summary: pH 7; cofactor FAD

proof_lines: kcat is 0.103 sec(-1) with FMN as substrate (at 30 degrees Celsius and at pH 7.0) (PubMed:36273586). kcat is 0.395 sec(-1) with FAD as substrate (at 30 degrees Celsius and at pH 7.0) (PubMed:36273586).

substrate: FMN / FAD (30 degrees Celsius, pH 7.0)


organism: Homo sapiens

substrate_name: multiple FMN/FAD/ATP/NaPPi contexts

assay_conditions_summary: pH 7.5; cofactor FAD

proof_lines: kcat is 0.69 sec(-1) for FAD synthase activity using enzyme purified from E.coli (at 37 degrees Celsius and at pH 7.5) (PubMed:21951714). kcat is 0.69 sec(-1) for FAD synthase activity using enzyme purified from E.coli (at 37 degrees Celsiu

proof_lines: kcat is 0.042 sec(-1) for FAD synthase activity using C-terminal region (329-587) purified from E.coli (at 37 degrees Celsius and at pH 7.5) (PubMed:23443125). kcat is 0.0037 sec(-1) for the reverse pyrophosphorolytic reaction using C-termi

substrate: multiple FMN/FAD/ATP/NaPPi contexts


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: FAD with magnesium or cobalt ions (30 degrees Celsius, pH 7.0)

proof_lines: kcat is 0.2 sec(-1) with FAD as substrate in presence of magnesium ions (at 30 degrees Celsius and at pH 7.0) (PubMed:29902190). kcat is 0.38 sec(-1) with FAD as substrate in presence of cobalt ions (at 30 degrees Celsius and at pH 7.0) (Pu


substrate_name: FAD

substrate: FAD


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-glucosamine

substrate: D-glucosamine


organism: Saccharophagus degradans

substrate_name: cellobiose


organism: Thermotoga maritima

substrate_name: D-glucose


organism: unidentified


proof_lines: pH 7.0, temperature not specified in the publication


organism: Rattus norvegicus


enzyme_display_name: ferredoxin--NAD(+) reductase

organism: Bacillus subtilis

substrate_name: NADH; Oxidized ferredoxin

assay_conditions_summary: cofactor NADP+

enzyme: ferredoxin--NAD(+) reductase

substrate: NADH; Oxidized ferredoxin


organism: Acidaminococcus fermentans

substrate_name: oxidized [2Fe-2S] ferredoxin

proof_lines: at pH 6.8, temperature not specified in the publication

substrate: oxidized [2Fe-2S] ferredoxin


organism: Acinetobacter sp.

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines: pH and temperature not specified in the publication

substrate: NADH


organism: Clostridium acetobutylicum

substrate_name: NAD+; Reduced ferredoxin; H+

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Reduced ferredoxin; H+


organism: Methylosinus trichosporium OB3b


organism: Mycobacterium sp.

substrate_name: oxidized ferredoxin

assay_conditions_summary: pH 8.6; cofactor NADH

substrate: oxidized ferredoxin


substrate_name: ferricytochrome c

proof_lines: recombinant ferredoxin with N-terminal His-tag, pH 8.6

proof_lines: recombinant ferredoxin with C-terminal His-tag, pH 8.6

substrate: ferricytochrome c


organism: Pseudomonas putida


organism: Pseudomonas sp.

assay_conditions_summary: cofactor NADPH


enzyme_display_name: feruloyl-CoA hydratase/lyase

organism: Pseudomonas fluorescens

substrate_name: feruloyl-CoA

sequence_source: source_record; direct UniProtKB O69762 check

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 3.72 sec(-1) with feruloyl-CoA as substrate.

enzyme: feruloyl-CoA hydratase/lyase

substrate: feruloyl-CoA


assay_conditions_summary: 303.15 K; cofactor CoA


sequence_source: direct UniProtKB O69762 exact accession lookup


sequence_variant_note: Resolved canonical sequence from direct UniProtKB O69762 exact accession lookup plus S123A one-based residue reconstruction and applied mutation signature S123A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from direct UniProtKB O69762 exact accession lookup plus Y239F one-based residue reconstruction and applied mutation signature Y239F to reconstruct the assayed variant sequence.


enzyme_display_name: allantoicase

substrate_name: allantoate

proof_lines: Vmax of the reaction with allantoate as substrate is nine times higher than that with ureidoglycolate.

enzyme: allantoicase

substrate: allantoate


organism: Burkholderia cepacia

substrate_name: (-)-Ureidoglycolate; H2O; Allantoate

sequence_source: UniProtKB Q39F96 direct accession lookup

substrate: (-)-Ureidoglycolate; H2O; Allantoate


organism: Chlamydomonas reinhardtii

substrate_name: Allantoate

sequence_source: UniProtKB P82678 direct accession lookup

substrate: Allantoate


substrate_name: H2O; Allantoate; Ureidoglycolate

sequence_source: UniProtKB P82678 direct lookup after parsing the source expression ((P82678)*3)*2 as a P82678 candidate

substrate: H2O; Allantoate; Ureidoglycolate


organism: Mus musculus

sequence_source: UniProtKB Q9JHX6 direct accession lookup


organism: Xenopus laevis

substrate_name: H2O; Allantoate

sequence_source: UniProtKB Q9W6S5 direct accession lookup

substrate: H2O; Allantoate


sequence_source: UniProtKB reviewed accession P82678 (ALLC_CHLRE); organism Chlamydomonas reinhardtii; EC 3.5.3.4; references PMID 10860551 and DOI 10.1006/abbi.2000.1833.


organism: Streptomyces viridiviolaceus


sequence_source: UniProtKB reviewed accession Q9W6S5 (ALLC_XENLA); organism Xenopus laevis; EC 3.5.3.4; references PMID 10864446 and DOI 10.1006/abbi.2000.1863.


enzyme_display_name: 13-deoxydaunorubicin hydroxylase

organism: Streptomyces sp. (strain C5)

substrate_name: daunorubicin (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 0.63 sec(-1) for oxidation on 13-dihydrodaunorubicin. kcat is 0.024 sec(-1) for hydroxylation on 13-deoxydaunorubicin. kcat is 0.00026 sec(-1) for oxidation on 13-dihydrocarminomycin. kcat is 0.00012 sec(-1) for hydroxylation on dau

enzyme: 13-deoxydaunorubicin hydroxylase


organism: Streptomyces sp.

sequence_source: UniProtKB reviewed accession Q59971 (DOXA_STRS5), sequence version 1; direct REST lookup 2026-06-27


substrate_name: daunorubicin

substrate: daunorubicin


organism: Aquifex aeolicus

sequence_source: UniProtKB accession O67625 direct lookup (UniProtKB reviewed (Swiss-Prot); Aquifex aeolicus (strain VF5); 4-hydroxy-3-methylbut-2-enyl diphosphate reductase; EC 1.17.7.4; length 289)

proof_lines:
recombinant enzyme, pH 7.5, 60°C
Raw SKiD Env: Temp=60°C, pH=7.5


enzyme_display_name: chlorate reductase

organism: Azospira oryzae

substrate_name: bromate

sequence_source: UniProtKB accession G8QM55 direct lookup (UniProtKB unreviewed (TrEMBL); Azospira oryzae (strain ATCC BAA-33 / DSM 13638 / PS); DMSO reductase family type II enzyme, molybdopterin subunit; EC not annotated; length 927)

enzyme: chlorate reductase

substrate: bromate


organism: Haloferax mediterranei

substrate_name: Chlorate

substrate: Chlorate


organism: Triticum aestivum

substrate_name: S-Adenosyl-L-methionine; Tricetin

sequence_source: UniProtKB accession Q38J50 direct lookup (UniProtKB reviewed (Swiss-Prot); Triticum aestivum; Tricetin 3',4',5'-O-trimethyltransferase; EC 2.1.1.169; length 356)

substrate: S-Adenosyl-L-methionine; Tricetin