substrate_name: 4-nitrophenyl propionate

column_label: Table 1 (Kinetic parameters of EstFa_R and its AQGF mutant), AQGF block, row 'pNP propionate'; column 'kcat (s^-1)' = 59 ± 4; column 'Km (mM)' = 0.70 ± 0.14; column 'kcat/Km (s^-1 mM^-1)' = 84.6.

normalized_value_unit_evidence: kcat: printed Table 1 cell 59 ± 4 s^-1; the cell is already in s^-1, so no unit conversion applies, and the paper value is 59.0 s^(-1), which is the value the catalog already carries. Km: printed Table 1 cell 0.70 ± 0.14 mM; the cell is already in mM, so no unit conversion applies, and the paper value is 0.7 mM, which is the value the catalog already carries. kcat/Km: printed Table 1 cell 84.6 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and the paper value is 84.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, AQGF block, row 'pNP propionate': kcat = 59 ± 4 s^-1; Km = 0.70 ± 0.14 mM; printed kcat/Km = 84.6 s^-1 mM^-1.

row_label: Table 1, AQGF (N248A/P256Q/E257G/S283F) block, row 'pNP propionate'

substrate: 4-nitrophenyl propionate


enzyme_display_name: carboxylesterase

organism: Ferroplasma acidiphilum

substrate_name: 4-nitrophenyl butyrate

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q2PCE5 and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of EstFa_R and its AQGF mutant), AQGF block, row 'pNP butyrate'; column 'kcat (s^-1)' = 101 ± 7; column 'Km (mM)' = 0.48 ± 0.11; column 'kcat/Km (s^-1 mM^-1)' = 211.

normalized_value_unit_evidence: kcat: printed Table 1 cell 101 ± 7 s^-1; the cell is already in s^-1, so no unit conversion applies, and the paper value is 101.0 s^(-1), which is the value the catalog already carries. Km: printed Table 1 cell 0.48 ± 0.11 mM; the cell is already in mM, so no unit conversion applies, and the paper value is 0.48 mM, which is the value the catalog already carries. kcat/Km: printed Table 1 cell 211 s^-1 mM^-1; the cell is already in s^-1 mM^-1, so no unit conversion applies, and the paper value is 211.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, AQGF block, row 'pNP butyrate': kcat = 101 ± 7 s^-1; Km = 0.48 ± 0.11 mM; printed kcat/Km = 211 s^-1 mM^-1.

row_label: Table 1, AQGF (N248A/P256Q/E257G/S283F) block, row 'pNP butyrate'

table_label: Table 1: Kinetic parameters of EstFa_R and its AQGF mutant (J. Biol. Chem. 2014, 289(35):24499-24510)

data_origin: experimental

enzyme: carboxylesterase

substrate: 4-nitrophenyl butyrate

status: corrected

source: oed


substrate_name: 4-nitrophenyl acetate

verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q2PCE5 canonical sequence plus N248A/P256Q/E257G/S283F and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

substrate: 4-nitrophenyl acetate

status: unverified


organism: Geobacillus stearothermophilus

substrate_name: p-Nitrophenyl caproate

mutation_signature: Unknown

sequence_source: UniProtKB direct accession lookup: Q8GCC7

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

substrate: p-Nitrophenyl caproate


sequence_source: UniProtKB direct accession lookup: Q06174


substrate_name: H2O; p-Nitrophenyl caproate

kcat_over_km_display: Not reported

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

substrate: H2O; p-Nitrophenyl caproate


organism: Amycolatopsis mediterranei (strain S699)

substrate_name: p-nitrophenyl palmitate (p-NPP) (at pH 8.0 and 60 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

assay_conditions_summary: pH 8

proof_lines: kcat is 1468 sec(-1) with p-nitrophenyl palmitate (p-NPP) as substrate (at pH 8.0 and 60 degrees Celsius).

source: uniprot


organism: Glycine max

substrate_name: 2,7-dihydroxy-4'-methoxyisoflavanone (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 1.6 sec(-1) with 2,7-dihydroxy-4'-methoxyisoflavanone, 5.3 sec(-1) with 2,7,4'-trihydroxyisoflavanone and 18.1 sec(-1) with 2,5,7,4'-tetrahydroxyisoflavanone as substrates, respectively (at pH 7.5 and 30 degrees Celsius).


organism: Glycyrrhiza echinata

proof_lines: kcat is 9.8 sec(-1) with 2,7-dihydroxy-4'-methoxyisoflavanone, 0.12 sec(-1) with 2,7,4'-trihydroxyisoflavanone and 0.19 sec(-1) with 2,5,7,4'-tetrahydroxyisoflavanone as substrates, respectively (at pH 7.5 and 30 degrees Celsius).

substrate: 2,7-dihydroxy-4'-methoxyisoflavanone (at pH 7.5 and 30 degrees Celsius)


organism: Homo sapiens

substrate_name: p-nitrophenyl acetate

proof_lines: kcat is 59 min(-1), 29 min(-1), 90 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

substrate: p-nitrophenyl acetate


substrate_name: cocaine

proof_lines: kcat is 43 min(-1), 49 min(-1), 150 min(-1) with 2-arachidonoylglycerol, prostaglandin F2alpha 1-glyceryl ester and prostaglandin E2 1-glyceryl ester as substrates, respectively.

substrate: cocaine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: triacetin

proof_lines: kcat is 581.2 sec(-1) for triacetin. kcat is 223.7 sec(-1) for tributyrin. kcat is 122.9 sec(-1) for tricaproin. kcat is 15.6 sec(-1) for tricaprylin. kcat is 501.8 sec(-1) for p-nitrophenyl acetate. kcat is 119.7 sec(-1) for p-nitrophenyl

substrate: triacetin


substrate_name: pNP-myristate

proof_lines: kcat is 1312 sec(-1) with pNP-myristate as substrate.

substrate: pNP-myristate


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: p-nitrophenyl butyrate

proof_lines: The N-terminal esterase domain, when expressed alone, shows activities five to ten times higher than those of the complete enzyme EstP towards all tested substrates, whereas substrate affinity and the activity profiles are still the same.

substrate: p-nitrophenyl butyrate


organism: Rattus norvegicus

substrate_name: retinyl palmitate

proof_lines: kcat is 0.19 min(-1) with retinyl palmitate as substrate.

substrate: retinyl palmitate


proof_lines: kcat is 0.45 min(-1) with retinyl palmitate as substrate.


substrate_name: oleic acid

proof_lines: kcat is 0.22 min(-1) with retinyl palmitate as substrate.

substrate: oleic acid


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: pNP-acetate (at pH 7 and 70 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 1.0 sec(-1) with pNP-acetate as substrate. kcat is 14.9 sec(-1) with pNP-butyrate as substrate. kcat is 10.2 sec(-1) with pNP-valerate as substrate. kcat is 1.6 sec(-1) with pNP-octanoate as substrate. kcat is 1.3 sec(-1) with pNP-d


sequence_source: UniProtKB REST direct accession lookup (Q06174)


organism: Geobacillus thermoleovorans

substrate_name: H2O; p-Nitrophenyl laurate

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

unit: mol/min

substrate: H2O; p-Nitrophenyl laurate


substrate_name: Irinotecan

sequence_source: UniProtKB REST direct accession lookup (P23141)

substrate: Irinotecan


sequence_source: UniProtKB REST direct accession lookup (O00748)


substrate_name: H2O; o-Nitrophenyl acetate

km_display: Not reported

ki_unit: mM

substrate: H2O; o-Nitrophenyl acetate


substrate_name: H2O; Irinotecan

sequence_source: UniProtKB REST direct accession lookup (Q6UWW8)

substrate: H2O; Irinotecan


sequence_source: UniProtKB REST direct accession lookup (Q4G0E9)


substrate_name: H2O; Capecitabine

substrate: H2O; Capecitabine


substrate_name: Tripropionin; H2O

substrate: Tripropionin; H2O


substrate_name: Cypermethrin

column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'Cypermethrin (B3)'; column 'Km(uM)' = 20; column 'kcat(min-1)' = 1.3; column 'kcat/Km(uM-1 min1)' = 0.07.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'Cypermethrin (B3)': Km = 20 uM; kcat = 1.3 min^-1; printed kcat/Km = 0.07 uM^-1 min^-1.

table_label: Table 5: Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates (Arch Biochem Biophys 2006;445(1):115-123)

substrate: Cypermethrin


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'A6'; column 'Km(uM)' = 1.8; column 'kcat(min-1)' = 0.25; column 'kcat/Km(uM-1 min1)' = 0.14.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'A6': Km = 1.8 uM; kcat = 0.25 min^-1; printed kcat/Km = 0.14 uM^-1 min^-1.


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-2'; substrate row 'Cypermethrin (B3)'; column 'Km(uM)' = 9.1; column 'kcat(min-1)' = 4.0; column 'kcat/Km(uM-1 min-1)' = 0.44.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-2', substrate row 'Cypermethrin (B3)': Km = 9.1 uM; kcat = 4.0 min^-1; printed kcat/Km = 0.44 uM^-1 min^-1.


column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-1'; substrate row 'A8'; column 'Km(uM)' = 1.5; column 'kcat(min-1)' = 0.30; column 'kcat/Km(uM-1 min1)' = 0.20.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-1', substrate row 'A8': Km = 1.5 uM; kcat = 0.30 min^-1; printed kcat/Km = 0.20 uM^-1 min^-1.


substrate_name: H2O; 4-Nitrophenyl acetate

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

column_label: Table 5. Kinetic constants of the recombinant hCE-1 and hCE-2 for various substrates. Enzyme block 'hCE-2'; substrate row 'pNPA'; column 'Km(uM)' = 31; column 'kcat(min-1)' = 4200; column 'kcat/Km(uM-1 min-1)' = 140.

normalized_value_unit_evidence: Km: printed Table 5 cell 31 uM; 31 / 1000 = 0.031 mM; the exported value is 0.0009000000000000001 mM. kcat: printed Table 5 cell 4200 min^-1; 4200 / 60 = 70.0 s^(-1); the exported value is 70.0 s^(-1). kcat/Km: printed Table 5 cell 140 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 140 x 1000 / 60 = 2333.3333333333335 s^-1 mM^-1; the catalog carries no catalytic-efficiency value for this row, so the printed cell is kept as paper evidence only.

raw_value_unit_evidence: Table 5, enzyme block 'hCE-2', substrate row 'pNPA': Km = 31 uM; kcat = 4200 min^-1; printed kcat/Km = 140 uM^-1 min^-1.

substrate: H2O; 4-Nitrophenyl acetate


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:
isoform hCE-2, pH 8.0, 37°C
isoform hCE-1, pH 8.0, 37°C
enzyme from liver cytosol

source_databases_merged: sabio_rk brenda skid


substrate_name: p-Nitrophenyl acetate

row_label: Table 5, enzyme block 'hCE-2', substrate row 'pNPA'

substrate: p-Nitrophenyl acetate


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl octanoate; H2O

sequence_source: RCSB 1EVQ polymer entity mapped to UniProtKB Q7SIG1

substrate: p-Nitrophenyl octanoate; H2O


organism: Bacillus subtilis

substrate_name: H2O; p-Nitrophenyl butyrate

substrate: H2O; p-Nitrophenyl butyrate


organism: Mus musculus

substrate_name: cis-Permethrin; H2O

substrate: cis-Permethrin; H2O


enzyme_display_name: tyrosinase

organism: Agaricus bisporus

substrate_name: O2; L-Dopa

assay_conditions_summary: pH 7; 298.15 K; buffer phosphate

proof_lines: pH and temperature not specified in the publication

source_db: brenda

enzyme: tyrosinase

substrate: O2; L-Dopa


organism: Prunus persica

substrate_name: (+)-Catechin; O2

proof_lines: membrane-bound (PPO-B) peach polyphenol oxidase without SDS

proof_lines: membrane-bound (PPO-B) peach polyphenol oxidase with 2 mM SDS

proof_lines: soluble (PPO-S) peach polyphenol oxidase without SDS

substrate: (+)-Catechin; O2


organism: Solanum tuberosum

substrate_name: L-Dopa

proof_lines: with catechol as a substrate, at pH 6.8 and 25°C

proof_lines: with 4-methylcatechol as a substrate, at pH 6.8 and 25°C

substrate: L-Dopa

source: brenda


sequence_source: UniProtKB exact accession O42713 REST lookup on 2026-07-01

proof_lines: Sigma mushroom tyrosinase (SMT, crude powder, lot 105k7026)

proof_lines: Worthington mushroom tyrosinase (WMT, crude powder, lot 33H6588Q)


organism: Bos taurus

substrate_name: O2; L-Noradrenaline

substrate: O2; L-Noradrenaline


organism: Concholepas concholepas


substrate_name: L-Tyrosine; O2

sequence_source: UniProtKB exact accession P14679 REST lookup on 2026-07-01

substrate: L-Tyrosine; O2


organism: Pholiota nameko

substrate_name: O2; 4-Cresol

sequence_source: UniProtKB exact accession A7BHQ9 REST lookup on 2026-07-01

substrate: O2; 4-Cresol


organism: Saccharomyces cerevisiae

substrate_name: O2; Epinephrine

substrate: O2; Epinephrine


enzyme_display_name: laccase

organism: Bacillus sp.

substrate_name: O2; 2,6-Dimethoxyphenol

sequence_source: UniProtKB:B9W2C5 direct lookup

enzyme: laccase

substrate: O2; 2,6-Dimethoxyphenol


substrate_name: O2; Syringaldazine

substrate: O2; Syringaldazine


organism: Bacillus sp. HR03


organism: Bacillus sp. LS03


organism: Bacillus sp. SL-1

sequence_source: UniProtKB:A0A165W3F6 direct lookup


sequence_source: UniProtKB:P07788 direct lookup


substrate_name: Syringaldazine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature L431F to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: Syringaldazine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature R146K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature R476K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 direct lookup and applied mutation signature T480A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A386JCD3 direct lookup


organism: Ochrobactrum sp. 531


organism: Paenibacillus glucanolyticus

sequence_source: UniProtKB exact accession A0A165SC98 REST lookup, retrieved 2026-07-01


organism: Pleurotus ostreatus

sequence_source: UniProtKB exact accession O60199 REST lookup, retrieved 2026-07-01


organism: Pseudomonas fluorescens

sequence_source: UniProtKB exact accession Q4KCN4 REST lookup, retrieved 2026-07-01


organism: Pseudomonas sp.


organism: Rheinheimera sp.


organism: Rhodococcus erythropolis

substrate_name: 2,6-Dimethoxyphenol; O2

substrate: 2,6-Dimethoxyphenol; O2


organism: Stenotrophomonas maltophilia


organism: Streptomyces californicus


substrate_name: O2; Potassium ferrocyanide

substrate: O2; Potassium ferrocyanide


organism: Streptomyces coelicolor

substrate_name: O2; Osmium complex

sequence_source: UniProtKB:Q9XAL8 direct accession check (REST, 2026-07-01)

substrate: O2; Osmium complex


organism: Streptomyces cyaneus


organism: Streptomyces griseoflavus

sequence_source: UniProtKB:A0A0M4FJ81 direct accession check (REST, 2026-07-01)


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature I170A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the SgfSL variants), ABTS block, protein row 'I170A'; column 'Km (mM)' = 0.63 ± 0.11; column 'kcat (s-1)' = 0.70 ± 0.20; column 'kcat/Km (mM-1 s-1)' = 1.11; column 'Activity nM O2 min-1 ug-1' = 0.11 ± 0.01.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.70 under the column head kcat (s-1); the cell is already in s^-1, so no unit conversion applies and the canonical value is 0.7 s^(-1). Km: printed Table 3 cell 0.63 under the column head Km (mM); the cell is already in mM, so no unit conversion applies and the canonical value is 0.63 mM. kcat/Km: printed Table 3 cell 1.11 under the column head kcat/Km (mM-1 s-1); the cell is already in mM^-1 s^-1, so no unit conversion applies and the printed cell carries over as 1.11 s^-1 mM^-1, while the full-precision quotient of the same line's two printed component cells is 0.70 / 0.63 = 1.111111111111111 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, ABTS block, protein row 'I170A': Km = 0.63 mM; kcat = 0.70 s-1; printed kcat/Km = 1.11 mM-1 s-1.

table_label: Table 3: Kinetic parameters of the SgfSL variants (Int. J. Mol. Sci. 2019, volume 20, article 3184, page 6); printed column heads Substrate | Protein | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1) | Activity nM O2 min-1 ug-1

status: verified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature M199A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'Met199Ala'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.35 ± 0.02; column 'kcat (s-1)' = 54 ± 1; column 'kcat/Km(s-1 mM-1)' = 155.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.35 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.35 mM. kcat: printed Table 2 cell 54 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 54.0 s^(-1). kcat/Km: printed Table 2 cell 155 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 155.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 54 / 0.35 = 154.2857142857143 s^-1 mM^-1, which is the value the export stores for kcat_over_km (154.2857142857143); the paper's own printed efficiency cell is 155.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'Met199Ala': Km = 0.35 ± 0.02 mM; kcat = 54 ± 1 s^-1; printed kcat/Km = 155 s^-1 mM^-1; printed pHopt = 4.0.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81 canonical sequence plus mutation_signature reconstruction (2026-07-01) and applied mutation signature M199G/R240H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature M199G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block '2.6-DMP', protein row 'Met199Gly'; column 'pHopt' = 8.0; column 'Km(mM)' = 0.67 ± 0.12; column 'kcat (s-1)' = 3.39 ± 0.17; column 'kcat/Km(s-1 mM-1)' = 5.07.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.67 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.67 mM. kcat: printed Table 2 cell 3.39 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 3.39 s^(-1). kcat/Km: printed Table 2 cell 5.07 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 5.07 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 3.39 / 0.67 = 5.059701492537314 s^-1 mM^-1, which is the value the export stores for kcat_over_km (5.059701492537314); the paper's own printed efficiency cell is 5.07 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block '2.6-DMP', protein row 'Met199Gly': Km = 0.67 ± 0.12 mM; kcat = 3.39 ± 0.17 s^-1; printed kcat/Km = 5.07 s^-1 mM^-1; printed pHopt = 8.0.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81 canonical sequence plus mutation_signature reconstruction (2026-07-01) and applied mutation signature H165A/R240H to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'Met199Ala'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.32 ± 0.05; column 'kcat (s-1)' = 33 ± 2; column 'kcat/Km(s-1 mM-1)' = 102.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.32 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.32 mM. kcat: printed Table 2 cell 33 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 33.0 s^(-1). kcat/Km: printed Table 2 cell 102 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 102.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 33 / 0.32 = 103.125 s^-1 mM^-1, which is the value the export stores for kcat_over_km (103.125); the paper's own printed efficiency cell is 102.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'Met199Ala': Km = 0.32 ± 0.05 mM; kcat = 33 ± 2 s^-1; printed kcat/Km = 102 s^-1 mM^-1; printed pHopt = 4.0.


sequence_source: UniProtKB:A0A0M4FJ81 canonical sequence plus mutation_signature reconstruction (2026-07-01)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature Y230A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block '2.6-DMP', protein row 'Tyr230Ala'; column 'pHopt' = 8.5; column 'Km(mM)' = 0.76 ± 0.03; column 'kcat (s-1)' = 1.68 ± 0.07; column 'kcat/Km(s-1 mM-1)' = 2.22.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.76 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.76 mM. kcat: printed Table 2 cell 1.68 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 1.68 s^(-1). kcat/Km: printed Table 2 cell 2.22 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 2.22 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 1.68 / 0.76 = 2.2105263157894735 s^-1 mM^-1, which is the value the export stores for kcat_over_km (2.2105263157894735); the paper's own printed efficiency cell is 2.22 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block '2.6-DMP', protein row 'Tyr230Ala': Km = 0.76 ± 0.03 mM; kcat = 1.68 ± 0.07 s^-1; printed kcat/Km = 2.22 s^-1 mM^-1; printed pHopt = 8.5.


assay_conditions_summary: pH 3.5; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'Tyr230Ala'; column 'pHopt' = 3.5; column 'Km(mM)' = 0.17 ± 0.04; column 'kcat (s-1)' = 29 ± 3; column 'kcat/Km(s-1 mM-1)' = 169.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.17 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.17 mM. kcat: printed Table 2 cell 29 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 29.0 s^(-1). kcat/Km: printed Table 2 cell 169 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 169.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 29 / 0.17 = 170.58823529411762 s^-1 mM^-1, which is the value the export stores for kcat_over_km (170.58823529411762); the paper's own printed efficiency cell is 169.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'Tyr230Ala': Km = 0.17 ± 0.04 mM; kcat = 29 ± 3 s^-1; printed kcat/Km = 169 s^-1 mM^-1; printed pHopt = 3.5.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'SgfSLwt'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.36 ± 0.07; column 'kcat (s-1)' = 15 ± 1; column 'kcat/Km(s-1 mM-1)' = 42.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.36 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.36 mM. kcat: printed Table 2 cell 15 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 15.0 s^(-1). kcat/Km: printed Table 2 cell 42 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 42.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 15 / 0.36 = 150.0 s^-1 mM^-1, which is the value the export stores for kcat_over_km (150.0); the paper's own printed efficiency cell is 42.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'SgfSLwt': Km = 0.36 ± 0.07 mM; kcat = 15 ± 1 s^-1; printed kcat/Km = 42 s^-1 mM^-1; printed pHopt = 4.0.


organism: Thermus sp.


organism: Thermus thermophilus


substrate_name: Guaiacol

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

substrate: Guaiacol


organism: Trametes versicolor

substrate_name: O2; Methyl syringate

substrate: O2; Methyl syringate


organism: unknown prokaryotic organism


organism: Acidobacteriaceae


organism: Acinetobacter baumannii

substrate_name: O2; Guaiacol

substrate: O2; Guaiacol


organism: Aeromonas hydrophila


organism: alpha proteobacterium Q-1


organism: Amycolatopsis sp.

sequence_source: UniProtKB:J9PBQ8 direct accession lookup on 2026-07-01


organism: Aquifex aeolicus


organism: Bacillus altitudinis


organism: Bacillus amyloliquefaciens


organism: Bacillus licheniformis

sequence_source: UniProtKB:Q65MU7 direct accession lookup on 2026-07-01


sequence_source: UniProtKB:H8WGE4 direct accession lookup on 2026-07-01


organism: Bacillus pumilus

sequence_source: UniProtKB:I3XLC2 direct accession lookup on 2026-07-01


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'Tyr230Ala'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.31 ± 0.01; column 'kcat (s-1)' = 86 ± 1; column 'kcat/Km(s-1 mM-1)' = 278.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.31 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.31 mM. kcat: printed Table 2 cell 86 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 86.0 s^(-1). kcat/Km: printed Table 2 cell 278 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 278.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 86 / 0.31 = 277.4193548387097 s^-1 mM^-1, which is the value the export stores for kcat_over_km (277.4193548387097); the paper's own printed efficiency cell is 278.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'Tyr230Ala': Km = 0.31 ± 0.01 mM; kcat = 86 ± 1 s^-1; printed kcat/Km = 278 s^-1 mM^-1; printed pHopt = 4.0.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block '2.6-DMP', protein row 'Met199Ala'; column 'pHopt' = 8.0; column 'Km(mM)' = 0.83 ± 0.08; column 'kcat (s-1)' = 1.30 ± 0.05; column 'kcat/Km(s-1 mM-1)' = 1.55.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.83 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.83 mM. kcat: printed Table 2 cell 1.30 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 1.3 s^(-1). kcat/Km: printed Table 2 cell 1.55 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 1.55 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 1.30 / 0.83 = 1.566265060240964 s^-1 mM^-1, which is the value the export stores for kcat_over_km (1.566265060240964); the paper's own printed efficiency cell is 1.55 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block '2.6-DMP', protein row 'Met199Ala': Km = 0.83 ± 0.08 mM; kcat = 1.30 ± 0.05 s^-1; printed kcat/Km = 1.55 s^-1 mM^-1; printed pHopt = 8.0.


sequence_source: UniProtKB REST canonical sequence for A0A0M4FJ81


sequence_variant_note: Resolved canonical sequence from UniProtKB REST canonical sequence for A0A0M4FJ81 and applied mutation signature M199G/R240H to reconstruct the assayed variant sequence.


column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'Met199Gly'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.25 ± 0.02; column 'kcat (s-1)' = 66 ± 2; column 'kcat/Km(s-1 mM-1)' = 261.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.25 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.25 mM. kcat: printed Table 2 cell 66 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 66.0 s^(-1). kcat/Km: printed Table 2 cell 261 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 261.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 66 / 0.25 = 264.0 s^-1 mM^-1, which is the value the export stores for kcat_over_km (264.0); the paper's own printed efficiency cell is 261.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'Met199Gly': Km = 0.25 ± 0.02 mM; kcat = 66 ± 2 s^-1; printed kcat/Km = 261 s^-1 mM^-1; printed pHopt = 4.0.


organism: Streptomyces lividans


organism: Streptomyces sp. C1


organism: Streptomyces sviceus

sequence_source: UniProtKB REST canonical sequence for B5HSR1


organism: Streptomyces viridosporus

sequence_source: UniProtKB REST canonical sequence for J9PBR2


organism: Thermobifida fusca


organism: Unknown


organism: Achromobacter xylosoxidans


organism: Acremonium sp.


organism: Agaricus bisporus


organism: Alcaligenes faecalis


organism: Alkalihalobacillus ligniniphilus


organism: Bacillus coagulans


proof_lines: pH 7.0, 22°C, recombinant enzyme, with 25% v/v DMSO

proof_lines: pH 6.5, 22°C, recombinant enzyme, with 0.8% v/v DMSO


organism: Bacillus sp.


organism: Bacillus subtilis

proof_lines:
pH 7, holoCotA
pH 3, holoCotA
pH 7.5, 37°C


organism: Carica papaya


organism: Citrobacter freundii


organism: Corynebacterium efficiens


organism: Desulfovibrio sp. A2


organism: Enterobacter ludwigii


organism: Geobacillus thermopakistaniensis


organism: Klebsiella pneumoniae


organism: Kocuria sp.


organism: Kurthia huakuii


organism: Lactobacillus plantarum


organism: Thioalkalivibrio sp.


organism: Trametes hirsuta

proof_lines: pH 4.5, 50°C, enzyme conjugated with 1.1 kDa PEG


organism: Trametes polyzona

proof_lines: pH 5.0, temperature not specified in the publication


organism: Trametes sp.

proof_lines: pH 5.0, 30°C, surface display laccase (SDL) biocatalyst (where the enzyme laccase is displayed on the surface of biological cells through synthetic biology)


organism: Trametes versicolor

substrate_name: O2; Syringic acid

proof_lines: enzyme conjugated with chitosan of 214 kDa

proof_lines: enzyme conjugated with chitosan of 505 kDa

substrate: O2; Syringic acid


organism: Lepista nuda


organism: Lysobacter sp. T-15


organism: Myrothecium verrucaria


organism: Pleurotus nebrodensis


organism: Pseudomonas sp. LBC1

substrate_name: o-Tolidine; O2

substrate: o-Tolidine; O2


organism: Shewanella putrefaciens


organism: Shigella dysenteriae


organism: Sporothrix carnis


organism: Streptomyces coelicolor

substrate_name: Small laccase (SLAC)

substrate: Small laccase (SLAC)


organism: Streptomyces griseorubens


organism: Thielavia sp.


organism: basidiomycete PM1

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 3.0, temperature not specified in the publication, engineered enzyme 7D5

proof_lines: pH 4.0, temperature not specified in the publication, engineered enzyme 7D5


organism: Escherichia coli

proof_lines:
pH 5, 30°C
presence of 0.25 mM Cu2+, pH 5, 30°C
presence of 0.1 mM Cu2+, pH 5, 30°C


organism: Ganoderma lucidum


organism: Geobacillus sp. JS12


organism: Geobacillus sp. WSUCF1


organism: Klebsiella pneumoniae


organism: Klebsiella sp. 601


organism: Marinomonas mediterranea

sequence_source: UniProtKB REST direct accession check on 2026-07-01: Q9KJB8

proof_lines: recombinant His-tagged enzyme MmPPOA-695, pH 5.0, 25°C


organism: uncultured bacterium

sequence_source: GenBank KP752045.1 CDS translation; protein_id AKN79754.1; PMID 30568647


enzyme_display_name: dUTP diphosphatase

organism: Mycobacterium tuberculosis

substrate_name: dUTP

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json) and applied mutation signature T138ter to reconstruct the assayed variant sequence.

mutation_type: truncation

proof_lines: mutant enzyme T138STOP, at pH 7.5 and 20°C

enzyme: dUTP diphosphatase

substrate: dUTP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json) and applied mutation signature R140K/H145W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R140K/H145W, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json) and applied mutation signature G143ter to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G143STOP, at pH 7.5 and 20°C


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:P9WNS5 direct accession lookup (https://rest.uniprot.org/uniprotkb/P9WNS5.json)

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

source: skid


organism: Plasmodium falciparum

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

sequence_source: UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json)

proof_lines: Ki above 0.01 mM, pH and temperature not specified in the publication

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json) and applied mutation signature F46A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json) and applied mutation signature I117A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8II92 direct accession lookup (https://rest.uniprot.org/uniprotkb/Q8II92.json) and applied mutation signature K96A to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme K96A, at pH 8.0 and 25°C
mutant enzyme K96A, at pH 8.0 and 25°


proof_lines:
mutant enzyme F46A, at pH 8.0 and 25°C
mutant enzyme F46A, at pH 8.0 and 25°


proof_lines:
mutant enzyme I117A, at pH 8.0 and 25°C
mutant enzyme I117A, at pH 8.0 and 25°


proof_lines:
wild type enzyme, at pH 8.0 and 25°C
wild type enzyme, at pH 8.0 and 25°


organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33317 and applied mutation signature R111A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the wild-type and mutant DUT1 proteins (Biochem J. 2011; 437(2):243-253, author manuscript); row 'Protein R111A' with variable substrate 'dUTP'; column 'Km (uM)' = 31.5; column 'h' = 1.3; column 'Vmax (units/mg)' = 10.9; column 'kcat (s^-1)' = 3.3; column 'kcat/Km (M^-1 . s^-1)' = 1.0×10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 31.5 uM; 31.5 / 1000 = 0.0315 mM; the exported value is 0.0315 mM. kcat: printed Table 2 cell 3.3 s^-1; already in s^-1, so no unit conversion applies; the exported value is 3.3 s^(-1). kcat/Km: the paper prints the cell 1.0×10^5 M^-1 s^-1 in the kcat/Km (M^-1 . s^-1) column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.0×10^5 / 1000 = 100.0 s^-1 mM^-1. The catalog carries 104.76190476190476 s^(-1)*mM^(-1), the full-precision quotient of the same two printed cells (3.3 / 0.0315), and the printed cell is that quotient rounded to the precision the paper prints, so the quotient is left as it is.

raw_value_unit_evidence: Table 2, row 'Protein R111A' with variable substrate 'dUTP': Km = 31.5 uM; kcat = 3.3 s^-1; printed kcat/Km = 1.0×10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33317 and applied mutation signature Y88A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the wild-type and mutant DUT1 proteins (Biochem J. 2011; 437(2):243-253, author manuscript); row 'Protein Y88A' with variable substrate 'dUTP'; column 'Km (uM)' = 41.0; column 'h' = 1.9; column 'Vmax (units/mg)' = 24.5; column 'kcat (s^-1)' = 7.4; column 'kcat/Km (M^-1 . s^-1)' = 1.8×10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 41.0 uM; 41.0 / 1000 = 0.041 mM; the exported value is 0.041 mM. kcat: printed Table 2 cell 7.4 s^-1; already in s^-1, so no unit conversion applies; the exported value is 7.4 s^(-1). kcat/Km: the paper prints the cell 1.8×10^5 M^-1 s^-1 in the kcat/Km (M^-1 . s^-1) column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.8×10^5 / 1000 = 180.0 s^-1 mM^-1. The catalog carries 180.4878048780488 s^(-1)*mM^(-1), the full-precision quotient of the same two printed cells (7.4 / 0.041), and the printed cell is that quotient rounded to the precision the paper prints, so the quotient is left as it is.

raw_value_unit_evidence: Table 2, row 'Protein Y88A' with variable substrate 'dUTP': Km = 41.0 uM; kcat = 7.4 s^-1; printed kcat/Km = 1.8×10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P33317 and applied mutation signature Q114A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the wild-type and mutant DUT1 proteins (Biochem J. 2011; 437(2):243-253, author manuscript); row 'Protein Q114A' with variable substrate 'dUTP'; column 'Km (uM)' = 14.2; column 'h' = 1.1; column 'Vmax (units/mg)' = 4.4; column 'kcat (s^-1)' = 1.3; column 'kcat/Km (M^-1 . s^-1)' = 0.9×10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 14.2 uM; 14.2 / 1000 = 0.0142 mM; the exported value is 0.0142 mM. kcat: printed Table 2 cell 1.3 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.3 s^(-1). kcat/Km: the paper prints the cell 0.9×10^5 M^-1 s^-1 in the kcat/Km (M^-1 . s^-1) column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.9×10^5 / 1000 = 90.0 s^-1 mM^-1. The catalog carries 91.54929577464789 s^(-1)*mM^(-1), the full-precision quotient of the same two printed cells (1.3 / 0.0142), and the printed cell is that quotient rounded to the precision the paper prints, so the quotient is left as it is.

raw_value_unit_evidence: Table 2, row 'Protein Q114A' with variable substrate 'dUTP': Km = 14.2 uM; kcat = 1.3 s^-1; printed kcat/Km = 0.9×10^5 M^-1 s^-1.


enzyme_name_source: UniProtKB direct accession P33317

substrate_name: dITP

sequence_source: UniProtKB direct accession P33317 REST lookup (2026-07-01)

column_label: Table 2: Kinetic parameters of the wild-type and mutant DUT1 proteins (Biochem J. 2011; 437(2):243-253, author manuscript); row 'Protein Wild-type' with variable substrate 'dITP'; column 'Km (uM)' = 44.7; column 'h' = 1.5; column 'Vmax (units/mg)' = 4.4; column 'kcat (s^-1)' = 1.3; column 'kcat/Km (M^-1 . s^-1)' = 2.9×10^4.

normalized_value_unit_evidence: Km: printed Table 2 cell 44.7 uM; 44.7 / 1000 = 0.0447 mM; the exported value is 0.0447 mM. kcat: printed Table 2 cell 1.3 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.3 s^(-1). kcat/Km: the paper prints the cell 2.9×10^4 M^-1 s^-1 in the kcat/Km (M^-1 . s^-1) column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9×10^4 / 1000 = 29.0 s^-1 mM^-1. The catalog carries 29.082774049217004 s^(-1)*mM^(-1), the full-precision quotient of the same two printed cells (1.3 / 0.0447), and the printed cell is that quotient rounded to the precision the paper prints, so the quotient is left as it is.

raw_value_unit_evidence: Table 2, row 'Protein Wild-type' with variable substrate 'dITP': Km = 44.7 uM; kcat = 1.3 s^-1; printed kcat/Km = 2.9×10^4 M^-1 s^-1.

substrate: dITP


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession P33317 REST lookup (2026-07-01) and applied mutation signature Q114A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q114A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C


substrate_name: UTP; dUTP

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession P33317 REST lookup (2026-07-01) and applied mutation signature Y88A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y88A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C

substrate: UTP; dUTP


substrate_name: UTP

column_label: Table 2: Kinetic parameters of the wild-type and mutant DUT1 proteins (Biochem J. 2011; 437(2):243-253, author manuscript); row 'Protein Y88A' with variable substrate 'UTP'; column 'Km (uM)' = 35.0; column 'h' = 1.6; column 'Vmax (units/mg)' = 17.4; column 'kcat (s^-1)' = 5.3; column 'kcat/Km (M^-1 . s^-1)' = 1.5×10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 35.0 uM; 35.0 / 1000 = 0.035 mM; the exported value is 0.035 mM. kcat: printed Table 2 cell 5.3 s^-1; already in s^-1, so no unit conversion applies; the exported value is 5.3 s^(-1). kcat/Km: the paper prints the cell 1.5×10^5 M^-1 s^-1 in the kcat/Km (M^-1 . s^-1) column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5×10^5 / 1000 = 150.0 s^-1 mM^-1. The catalog carries 151.42857142857142 s^(-1)*mM^(-1), the full-precision quotient of the same two printed cells (5.3 / 0.035), and the printed cell is that quotient rounded to the precision the paper prints, so the quotient is left as it is.

raw_value_unit_evidence: Table 2, row 'Protein Y88A' with variable substrate 'UTP': Km = 35.0 uM; kcat = 5.3 s^-1; printed kcat/Km = 1.5×10^5 M^-1 s^-1.

substrate: UTP


column_label: Table 2: Kinetic parameters of the wild-type and mutant DUT1 proteins (Biochem J. 2011; 437(2):243-253, author manuscript); row 'Protein Wild-type' with variable substrate 'dUTP'; column 'Km (uM)' = 13.2; column 'h' = 2.4; column 'Vmax (units/mg)' = 31.7; column 'kcat (s^-1)' = 9.6; column 'kcat/Km (M^-1 . s^-1)' = 7.4×10^5.

normalized_value_unit_evidence: Km: printed Table 2 cell 13.2 uM; 13.2 / 1000 = 0.0132 mM; the exported value is 0.0132 mM. kcat: printed Table 2 cell 9.6 s^-1; already in s^-1, so no unit conversion applies; the exported value is 9.6 s^(-1). kcat/Km: the paper prints the cell 7.4×10^5 M^-1 s^-1 in the kcat/Km (M^-1 . s^-1) column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.4×10^5 / 1000 = 740.0 s^-1 mM^-1. That printed cell is the paper's own fitted catalytic-efficiency value and is carried here as the paper value 740.0 s^(-1)*mM^(-1). The catalog carries 727.2727272727273 s^(-1)*mM^(-1), which is the full-precision quotient of the two printed component cells (9.6 / 0.0132).

raw_value_unit_evidence: Table 2, row 'Protein Wild-type' with variable substrate 'dUTP': Km = 13.2 uM; kcat = 9.6 s^-1; printed kcat/Km = 7.4×10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession P33317 REST lookup (2026-07-01) and applied mutation signature R111A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R111A, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C


substrate_name: dITP; dUTP

proof_lines: wild type enzyme, in 50 mM HEPES (pH 7.5), 5 mM MgCl2, 1 mM MnCl2, 0.5 mM NiCl2, at 30°C

substrate: dITP; dUTP


substrate_name: dITP; dUTP; UTP

substrate: dITP; dUTP; UTP


enzyme_name_source: UniProtKB direct accession Q8SDV3

organism: Staphylococcus phage phi11

substrate_name: Unknown

sequence_source: UniProtKB direct accession Q8SDV3 REST lookup (2026-07-01)

substrate: Unknown


enzyme_display_name: dUTPase

enzyme_name_source: UniProtKB direct accession A0EWK2

organism: Staphylococcus phage phinm1

sequence_source: UniProtKB direct accession A0EWK2 REST lookup (2026-07-01)

enzyme: dUTPase


enzyme_name_source: UniProtKB direct accession A0A480PG39

organism: Sus scrofa

sequence_source: UniProtKB direct accession A0A480PG39 REST lookup (2026-07-01)

proof_lines: wild-type, 25°C, pH 7.5, presence of K+, Mg2+


enzyme_name_source: UniProtKB direct accession Q77J78

organism: white spot syndrome virus

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature R24T/S115R/D170G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature K150E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature R24T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession Q77J78 REST lookup (2026-07-01) and applied mutation signature K150A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB direct accession Q77J78 REST lookup (2026-07-01)


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature K150E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature R158E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature D170L to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTD170L'; column 'kcat (s-1)' = 0.53; column 'Km (uM)' = 7.1; column 'kcat/Km (M-1 s-1)' = 7.5 x 10^4; column 'Relative efficiency (%)' = 1.7. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.53 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.53 s^(-1). Km: printed Table 1 cell 7.1 in a column headed Km (uM); 1 uM is 0.001 mM, so 7.1 / 1000 = 0.0071 mM. kcat/Km: printed Table 1 cell 7.5 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 75000 / 1000 = 75 s^-1 mM^-1. The exported values are kcat 0.53 s^(-1) and Km 0.0071 mM and kcat_over_km 74.64788732394366 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTD170L': kcat = 0.53 s-1; Km = 7.1 uM; printed kcat/Km = 7.5 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTD170L'

table_label: Table 1: Enzyme kinetics data (J. Biol. Chem. 2018, 293(3):1088-1099). Printed column heads: Enzyme; kcat (s-1); Km (uM); kcat/Km (M-1 s-1); Relative efficiency (%).


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature Δ170 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines: mutant enzyme DELTA170-171, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R158A to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR158A'; column 'kcat (s-1)' = 3.2; column 'Km (uM)' = 2.6; column 'kcat/Km (M-1 s-1)' = 1.2 x 10^6; column 'Relative efficiency (%)' = 28. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.2 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.2 s^(-1). Km: printed Table 1 cell 2.6 in a column headed Km (uM); 1 uM is 0.001 mM, so 2.6 / 1000 = 0.0026 mM. kcat/Km: printed Table 1 cell 1.2 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1200000 / 1000 = 1200 s^-1 mM^-1. The exported values are kcat 3.2 s^(-1) and Km 0.0026 mM and kcat_over_km 1230.769230769231 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR158A': kcat = 3.2 s-1; Km = 2.6 uM; printed kcat/Km = 1.2 x 10^6 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTR158A'


sequence_source: UniProtKB Q77J78 FASTA direct lookup

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

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTWT'; column 'kcat (s-1)' = 7.4; column 'Km (uM)' = 1.7; column 'kcat/Km (M-1 s-1)' = 4.4 x 10^6; column 'Relative efficiency (%)' = 100. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.4 s^(-1). Km: printed Table 1 cell 1.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 1.7 / 1000 = 0.0017 mM. kcat/Km: printed Table 1 cell 4.4 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4400000 / 1000 = 4400 s^-1 mM^-1. The exported values are kcat 7.4 s^(-1) and Km 0.0017 mM and kcat_over_km 4352.941176470588 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTWT': kcat = 7.4 s-1; Km = 1.7 uM; printed kcat/Km = 4.4 x 10^6 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTWT'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature R158A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature S115R to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTS115R'; column 'kcat (s-1)' = 2.6; column 'Km (uM)' = 4.5; column 'kcat/Km (M-1 s-1)' = 5.8 x 10^5; column 'Relative efficiency (%)' = 13. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.6 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.6 s^(-1). Km: printed Table 1 cell 4.5 in a column headed Km (uM); 1 uM is 0.001 mM, so 4.5 / 1000 = 0.0045 mM. kcat/Km: printed Table 1 cell 5.8 x 10^5 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 580000 / 1000 = 580 s^-1 mM^-1. The exported values are kcat 2.6 s^(-1) and Km 0.0045 mM and kcat_over_km 577.7777777777778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTS115R': kcat = 2.6 s-1; Km = 4.5 uM; printed kcat/Km = 5.8 x 10^5 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTS115R'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature D170G to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTD170G'; column 'kcat (s-1)' = 6.2; column 'Km (uM)' = 2.1; column 'kcat/Km (M-1 s-1)' = 3.0 x 10^6; column 'Relative efficiency (%)' = 68. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.2 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 6.2 s^(-1). Km: printed Table 1 cell 2.1 in a column headed Km (uM); 1 uM is 0.001 mM, so 2.1 / 1000 = 0.0021 mM. kcat/Km: printed Table 1 cell 3.0 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3000000 / 1000 = 3000 s^-1 mM^-1. The exported values are kcat 6.2 s^(-1) and Km 0.0021 mM and kcat_over_km 2952.3809523809527 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTD170G': kcat = 6.2 s-1; Km = 2.1 uM; printed kcat/Km = 3.0 x 10^6 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTD170G'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature S115R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature R161K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature D170G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 FASTA direct lookup plus row-specific mutation reconstruction and applied mutation signature F166Y to reconstruct the assayed variant sequence.


organism: Dictyostelium discoideum

proof_lines: kcat is 9.3 sec(-1) with dUTP as substrate.


organism: Escherichia coli (strain K12)

proof_lines: kcat is 21 sec(-1) with dUTP as substrate, and 15 sec(-1) with dTTP as substrate.


organism: Homo sapiens

proof_lines: kM is identical for both isoform 2 and isoform 3.


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


organism: Human gammaherpesvirus 4

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P03195 (2026-07-01) and applied mutation signature C4S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C4S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P03195 and applied mutation signature C4S to reconstruct the assayed variant sequence.

column_label: Table 2 (Enzymatic activity assays); enzyme row 'C4S'; column 'Assay' = Cresol red; column 'Km' with unit head uM = 0.6; column 'kcat' with unit head s^-1 = 1.7; column 'kcat/Km' with unit head M^-1 s^-1 = 2.8 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.7 s^-1; no unit conversion applies, so the canonical value is 1.7 s^(-1). Km: printed Table 2 cell 0.6 uM; 0.6 / 1000 = 0.0006 mM. kcat/Km: printed Table 2 cell 2.8 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^6 / 1000 = 2800.0 s^-1 mM^-1. The exported kcat/Km 2833.3333333333335 s^(-1)*mM^(-1) is the exact quotient 1.7 / 0.0006 of the two printed component cells of this same Table 2 line, and the printed efficiency cell is that quotient carried at the precision the table prints, so the exported ratio is kept and the printed cell stands as evidence of it.

raw_value_unit_evidence: Table 2, enzyme row 'C4S', Assay column 'Cresol red': printed Km cell 0.6 carrying the table's own Km unit head uM; printed kcat cell 1.7 carrying the kcat unit head s^-1; printed kcat/Km cell 2.8 x 10^6 carrying the kcat/Km unit head M^-1 s^-1. The error terms printed beside the central values are not transcribed.

table_label: Table 2: Enzymatic activity assays (J. Biol. Chem. 2009, 284(37):25280-25289)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P03195 (2026-07-01) and applied mutation signature D131N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D131N, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_source: UniProtKB direct accession lookup P03195 (2026-07-01)

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


organism: Leishmania major

substrate_name: dUDP

sequence_source: UniProtKB direct accession lookup O15826 (2026-07-01)

substrate: dUDP


substrate_name: dATP

substrate: dATP


substrate_name: H2O; dUTP

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

substrate: H2O; dUTP


substrate_name: dGTP

substrate: dGTP


substrate_name: dTTP

substrate: dTTP


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB direct accession lookup Q58502 (2026-07-01)


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P9WNS5 (2026-07-01) and applied mutation signature D28N/H145W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D28N/H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


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

proof_lines: DELTA-loop mutant enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C


sequence_source: UniProtKB direct accession lookup P9WNS5 (2026-07-01)

proof_lines: wild type enzyme, in 1 mM HEPES pH 7.5, 100 mM KCl, and 5 mM MgCl2, at 20°C

proof_lines: pH 7.5, 25°C, recombinant wild-type and mutant enzymes


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup P9WNS5 (2026-07-01) and applied mutation signature H145W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H145W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


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

proof_lines: mutant enzyme D49N/F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


proof_lines: mutant enzyme F158A, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


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

proof_lines: wild type enzyme, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


proof_lines: at 25°C in 25 mM MES, 5 mM NaCl, 25 mM MgCl2, 1 mM beta-mercaptoethanol, at pH 7.0

proof_lines: pH and temperature not specified in the publication


organism: Human alphaherpesvirus 1

proof_lines: enzyme from herpes simplex virus type 1 infected KB cells


organism: Human alphaherpesvirus 2


proof_lines: pH 7.6, 25°C, recombinant enzyme, in presence of 1 mM MgCl2


proof_lines:
pH 8, 25°C
above


organism: Orthopoxvirus vaccinia


organism: Paramecium bursaria Chlorella virus 1


organism: Plasmodium falciparum


organism: Shrimp white spot syndrome virus


organism: Spbetavirus SPbeta


organism: Thermococcus pacificus


proof_lines:
wild-type, pH 7.5, 75°C
wild-type, pH 7.5, 95°C


organism: Trypanosoma brucei


organism: Trypanosoma cruzi


organism: Acholeplasma laidlawii


organism: Allium cepa


organism: Bacillus subtilis


organism: Campylobacter jejuni


organism: Drosophila melanogaster


organism: Dugesia ryukyuensis

proof_lines: in the presence of 5 mM Mg2+, at pH 8.2 and 25°C

proof_lines: in the presence of 5 mM Mn2+, at pH 8.2 and 25°C


organism: equine infectious anemia virus


organism: Escherichia coli


proof_lines: mutant enzyme T22R/R116S, at pH 7.5 and 20°C


proof_lines: pH 7.5, 25°C, in the presence of VO2+ or bis(acetylacetonato)oxovanadium(IV)

proof_lines: pH 7.5, 25°C, in the absence of added metal ions


organism: Homo sapiens

proof_lines: mutant enzyme F158W, in 1 mM HEPES pH 7.5 containing 100 mM KCl and 5 mM MgCl2, at 20°C


organism: white spot syndrome virus

sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature V160D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R24T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R161K to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR161K'; column 'kcat (s-1)' = 0.053; column 'Km (uM)' = 5.4; column 'kcat/Km (M-1 s-1)' = 9.8 x 10^3; column 'Relative efficiency (%)' = 0.23. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.053 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.053 s^(-1). Km: printed Table 1 cell 5.4 in a column headed Km (uM); 1 uM is 0.001 mM, so 5.4 / 1000 = 0.0054 mM. kcat/Km: printed Table 1 cell 9.8 x 10^3 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9800 / 1000 = 9.8 s^-1 mM^-1. The exported values are kcat 0.053 s^(-1) and Km 0.0054 mM and kcat_over_km 9.814814814814815 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR161K': kcat = 0.053 s-1; Km = 5.4 uM; printed kcat/Km = 9.8 x 10^3 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTR161K'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature D34N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R24T/S115R/D170G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R24T/S115R/D170G, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R24T/S115R to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR24T/S115R'; column 'kcat (s-1)' = 0.51; column 'Km (uM)' = 6.7; column 'kcat/Km (M-1 s-1)' = 7.6 x 10^4; column 'Relative efficiency (%)' = 1.8. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.51 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.51 s^(-1). Km: printed Table 1 cell 6.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 6.7 / 1000 = 0.0067 mM. kcat/Km: printed Table 1 cell 7.6 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 76000 / 1000 = 76 s^-1 mM^-1. The exported values are kcat 0.51 s^(-1) and Km 0.0067 mM and kcat_over_km 76.11940298507463 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR24T/S115R': kcat = 0.51 s-1; Km = 6.7 uM; printed kcat/Km = 7.6 x 10^4 in a column headed kcat/Km (M-1 s-1).


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature D170L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature F166Y to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme DELTA134-153, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature R158W to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTR158W'; column 'kcat (s-1)' = 3.1; column 'Km (uM)' = 3.2; column 'kcat/Km (M-1 s-1)' = 9.7 x 10^5; column 'Relative efficiency (%)' = 22. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.1 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 3.1 s^(-1). Km: printed Table 1 cell 3.2 in a column headed Km (uM); 1 uM is 0.001 mM, so 3.2 / 1000 = 0.0032 mM. kcat/Km: printed Table 1 cell 9.7 x 10^5 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 970000 / 1000 = 970 s^-1 mM^-1. The exported values are kcat 3.1 s^(-1) and Km 0.0032 mM and kcat_over_km 968.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTR158W': kcat = 3.1 s-1; Km = 3.2 uM; printed kcat/Km = 9.7 x 10^5 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTR158W'


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R158W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R24T/S115R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R24T/S115R, at pH 7.5 and 20°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q77J78 and applied mutation signature D34N to reconstruct the assayed variant sequence.

column_label: Table 1 (Enzyme kinetics data), printed enzyme row 'wDUTD34N'; column 'kcat (s-1)' = 0.92; column 'Km (uM)' = 13; column 'kcat/Km (M-1 s-1)' = 7.1 x 10^4; column 'Relative efficiency (%)' = 1.6. The value printed after the plus/minus sign beside the kcat and Km cells of this line is the printed S.E. and is not an exported metric.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.92 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.92 s^(-1). Km: printed Table 1 cell 13 in a column headed Km (uM); 1 uM is 0.001 mM, so 13 / 1000 = 0.013 mM. kcat/Km: printed Table 1 cell 7.1 x 10^4 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 71000 / 1000 = 71 s^-1 mM^-1. The exported values are kcat 0.92 s^(-1) and Km 0.013 mM and kcat_over_km 70.76923076923077 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, printed enzyme row 'wDUTD34N': kcat = 0.92 s-1; Km = 13 uM; printed kcat/Km = 7.1 x 10^4 in a column headed kcat/Km (M-1 s-1).

row_label: Table 1, printed enzyme row 'wDUTD34N'


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

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 in a column headed kcat (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.4 s^(-1). Km: printed Table 1 cell 1.7 in a column headed Km (uM); 1 uM is 0.001 mM, so 1.7 / 1000 = 0.0017 mM. kcat/Km: printed Table 1 cell 4.4 x 10^6 in a column headed kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4400000 / 1000 = 4400 s^-1 mM^-1. The exported values are kcat 7.4 s^(-1) and Km 0.0017 mM; this export row stores no kcat_over_km field.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q77J78 direct accession lookup (accessed 2026-07-01); RCSB 5Y5O entity mapping to Q77J78 and PMID 29187596 and applied mutation signature R158E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P06968 direct lookup on 2026-07-01 and applied mutation signature D90N to reconstruct the assayed variant sequence.

proof_lines: D90N mutant enzyme, pH 7.8, room temperature


sequence_source: UniProtKB reviewed accession P06968 direct lookup on 2026-07-01


sequence_source: UniProtKB reviewed accession P33316 direct lookup on 2026-07-01

proof_lines: recombinant wild-type and mutant enzymes

proof_lines: pH 7.4, 20°C, recombinant wild-type enzyme


sequence_source: UniProtKB reviewed accession P33316-2 direct lookup on 2026-07-01


sequence_source: UniProtKB reviewed accession P33316-1 direct lookup on 2026-07-01


assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.2 M Tris

proof_lines: in 0.2 M Tris buffer (pH 7.4), 16 mM MgCl2, at 37°C


organism: Human gammaherpesvirus 4

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature R268A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature D131S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D131S, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P03195 direct lookup on 2026-07-01 and applied mutation signature D131S/G78D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D131S/G78D, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_source: UniProtKB reviewed accession P03195 direct lookup on 2026-07-01

proof_lines: wild type enzyme, without MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C

proof_lines: wild type enzyme, without MgCl2, with dithiothreitol, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C

proof_lines: wild type enzyme, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P03195 and applied mutation signature D131N to reconstruct the assayed variant sequence.

column_label: Table 2 (Enzymatic activity assays); enzyme row 'D131N'; column 'Assay' = Enzcheck; column 'Km' with unit head uM = 7; column 'kcat' with unit head s^-1 = 0.04; column 'kcat/Km' with unit head M^-1 s^-1 = 0.006 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.04 s^-1; no unit conversion applies, so the canonical value is 0.04 s^(-1). Km: printed Table 2 cell 7 uM; 7 / 1000 = 0.007 mM. kcat/Km: printed Table 2 cell 0.006 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.006 x 10^6 / 1000 = 6.0 s^-1 mM^-1. The exported kcat/Km 5.714285714285714 s^(-1)*mM^(-1) is the exact quotient 0.04 / 0.007 of the two printed component cells of this same Table 2 line, and the printed efficiency cell is that quotient carried at the precision the table prints, so the exported ratio is kept and the printed cell stands as evidence of it.

raw_value_unit_evidence: Table 2, enzyme row 'D131N', Assay column 'Enzcheck': printed Km cell 7 carrying the table's own Km unit head uM; printed kcat cell 0.04 carrying the kcat unit head s^-1; printed kcat/Km cell 0.006 x 10^6 carrying the kcat/Km unit head M^-1 s^-1. The error terms printed beside the central values are not transcribed.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P03195 and applied mutation signature D131S/G78D to reconstruct the assayed variant sequence.

column_label: Table 2 (Enzymatic activity assays); enzyme row 'D131S/G78D'; column 'Assay' = Enzcheck; column 'Km' with unit head uM = 9; column 'kcat' with unit head s^-1 = 0.18; column 'kcat/Km' with unit head M^-1 s^-1 = 0.02 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.18 s^-1; no unit conversion applies, so the canonical value is 0.18 s^(-1). Km: printed Table 2 cell 9 uM; 9 / 1000 = 0.009 mM. kcat/Km: printed Table 2 cell 0.02 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.02 x 10^6 / 1000 = 20.0 s^-1 mM^-1. The exported kcat/Km 20.0 s^(-1)*mM^(-1) is the exact quotient 0.18 / 0.009 of the two printed component cells of this same Table 2 line, and the printed efficiency cell is that quotient carried at the precision the table prints, so the exported ratio is kept and the printed cell stands as evidence of it.

raw_value_unit_evidence: Table 2, enzyme row 'D131S/G78D', Assay column 'Enzcheck': printed Km cell 9 carrying the table's own Km unit head uM; printed kcat cell 0.18 carrying the kcat unit head s^-1; printed kcat/Km cell 0.02 x 10^6 carrying the kcat/Km unit head M^-1 s^-1. The error terms printed beside the central values are not transcribed.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P03195 and applied mutation signature D131S to reconstruct the assayed variant sequence.

column_label: Table 2 (Enzymatic activity assays); enzyme row 'D131S'; column 'Assay' = Enzcheck; column 'Km' with unit head uM = 5.2; column 'kcat' with unit head s^-1 = 0.04; column 'kcat/Km' with unit head M^-1 s^-1 = 0.008 x 10^6.

normalized_value_unit_evidence: kcat: printed Table 2 cell 0.04 s^-1; no unit conversion applies, so the canonical value is 0.04 s^(-1). Km: printed Table 2 cell 5.2 uM; 5.2 / 1000 = 0.0052 mM. kcat/Km: printed Table 2 cell 0.008 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.008 x 10^6 / 1000 = 8.0 s^-1 mM^-1. The exported kcat/Km 7.6923076923076925 s^(-1)*mM^(-1) is the exact quotient 0.04 / 0.0052 of the two printed component cells of this same Table 2 line, and the printed efficiency cell is that quotient carried at the precision the table prints, so the exported ratio is kept and the printed cell stands as evidence of it.

raw_value_unit_evidence: Table 2, enzyme row 'D131S', Assay column 'Enzcheck': printed Km cell 5.2 carrying the table's own Km unit head uM; printed kcat cell 0.04 carrying the kcat unit head s^-1; printed kcat/Km cell 0.008 x 10^6 carrying the kcat/Km unit head M^-1 s^-1. The error terms printed beside the central values are not transcribed.


proof_lines: mutant enzyme R268A, with 1 mM MgCl2, in 0.5 mM bicine-NaOH, pH 7.8, at 25°C


organism: African swine fever virus (strain Badajoz 1971 Vero-adapted)

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


organism: Bacillus subtilis (strain 168)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: arylamine N-acetyltransferase

substrate_name: Acetyl-CoA; 2-Aminofluorene

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: using control cholangiocarcinoma KKU-100 cells after treatment with the mixture of inflammatory cytokines for 48 h, Vmax: 135.7 pmol/min/mg. A significant decrease in Vmax is shown but without affecting Km, implying a change in the amount o

enzyme: arylamine N-acetyltransferase

substrate: Acetyl-CoA; 2-Aminofluorene


enzyme_display_name: pyruvate kinase

organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ADP

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

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Escherichia coli (strain K12)

substrate_name: aniline

substrate: aniline


substrate_name: 2-aminofluorene (measured with the enzyme encoded by allele NAT2*4)


organism: Mycolicibacterium smegmatis

substrate_name: isoniazid

substrate: isoniazid


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: acetyl-CoA (in the presence of N-hydroxy-Glu-P-1)

assay_conditions_summary: cofactor CoA


organism: Enterobius vermicularis

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


proof_lines:
strain 54.8, pH 7.4, 37°C
strain K-12, pH 7.4, 37°C


organism: Gallus gallus

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Helicobacter pylori


substrate_name: sulfamethazine

substrate: sulfamethazine


organism: Klebsiella aerogenes

substrate_name: 3-aminobenzoic acid

substrate: 3-aminobenzoic acid


organism: Anisakis simplex


organism: Bacillus cereus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: mutant enzyme E123D, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C

proof_lines: mutant enzyme E123D, apparent value, at pH 7.5 and 25°C


proof_lines: wild type enzyme, apparent value, with 4-aminosalicylic acid as cosubstrate, at pH 7.5 and 25°C

proof_lines: wild type enzyme, apparent value, at pH 7.5 and 25°C


proof_lines:
Vmax: 2.1 micromol/min/mg
Vmax: 0.17 micromol/min/mg


organism: Bacteroides sp.

substrate_name: p-Aminobenzoic acid

substrate: p-Aminobenzoic acid


organism: Bos taurus


organism: Candida albicans


organism: Citrobacter amalonaticus


organism: Citrobacter farmeri


organism: Citrobacter freundii

substrate_name: 4-aminosalicylic acid

substrate: 4-aminosalicylic acid


organism: Citrobacter koseri

substrate_name: 5-aminosalicylic acid

substrate: 5-aminosalicylic acid


organism: Columba sp.

substrate_name: serotonin

substrate: serotonin


organism: Serratia marcescens


organism: Vibrio vulnificus

proof_lines: pH 7.5, temperature not specified in the publication


organism: Wickerhamomyces ciferrii

substrate_name: dodecylamine

substrate: dodecylamine


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 94 sec(-1) with 3-amino-4-hydroxybenzoic acid as substrate. kcat is 66 sec(-1) with 4-amino-3-hydroxybenzoic acid as substrate. kcat is 44 sec(-1) with hydralazine as substrate. kcat is 70 sec(-1) with 2-amino-4-methylphenol as subs


organism: Klebsiella oxytoca


organism: Klebsiella pneumoniae


organism: Klebsiella pneumoniae subsp. rhinoscleromatis


organism: Lactobacillus acidophilus


organism: Mesocricetus auratus

substrate_name: anisidine

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

proof_lines: cosubstrate acetyl-CoA, mutant Y190A, pH 7.0, 25°C

proof_lines: cosubstrate 4-nitrophenyl acetate, mutant Y190A, pH 7.0, 25°C

substrate: anisidine


substrate_name: 4-nitrophenyl acetate

proof_lines: cosubstrate 4-nitrophenyl acetate, wild-type, pH 7.0, 25°C

proof_lines: cosubstrate acetyl-CoA, wild-type, pH 7.0, 25°C

substrate: 4-nitrophenyl acetate


substrate_name: 4-aminobenzoyl glutamic acid

proof_lines: cosubstrate acetyl-CoA, mutant Y190F, pH 7.0, 25°C

proof_lines: cosubstrate 4-nitrophenyl acetate, mutant Y190F, pH 7.0, 25°C

substrate: 4-aminobenzoyl glutamic acid


proof_lines: cosubstrate 4-nitrophenyl acetate, mutant Y190I, pH 7.0, 25°C

proof_lines: cosubstrate acetyl-CoA, mutant Y190I, pH 7.0, 25°C


organism: Mesorhizobium loti

substrate_name: PAS

substrate: PAS


substrate_name: p-Aminosalicylic acid

substrate: p-Aminosalicylic acid


organism: Morganella morganii


organism: Musca domestica

substrate_name: tyramine

substrate: tyramine


organism: Mycobacterium marinum

assay_conditions_summary: pH 8; 301.15 K; cofactor CoA

proof_lines: chimeric enzyme, replacement of the third domain of Mycobacterium marinum enzyme with that from Mycobacterium tuberculosis, pH 8.0, 28°C

proof_lines: chimeric enzyme, replacement of the third domain of Mycobacterium tuberculosis enzyme with that from Mycobacterium marinum, pH 8.0, 28°C


organism: Mycobacterium tuberculosis


organism: Mycobacteroides abscessus


organism: Nocardia farcinica


organism: Pseudomonas aeruginosa

proof_lines: concentration p-anisidine: 200 nM, reaction: acetyl-CoA + p-anisidine


organism: Rattus norvegicus

substrate_name: Phenylethylamine

proof_lines: liver brain

substrate: Phenylethylamine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
strain 60.62, pH 7.4, 37°C
strain YG1024, pH 7.4, 37°C
strain TA98, pH 7.4, 37°C


organism: Mesorhizobium japonicum


organism: Mycobacterium smegmatis

substrate_name: Acetyl-CoA; Isoniazid

substrate: Acetyl-CoA; Isoniazid


organism: Mycolicibacterium smegmatis


substrate_name: isoniazid

substrate: isoniazid


proof_lines:
recombinant isozyme Nat3
recombinant isozyme Nat2
recombinant isozyme Nat1


organism: Streptomyces griseus


organism: Tsukamurella paurometabola

substrate_name: malonyl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: cosubstrate 5-aminosalicylate, pH 7.5, temperature not specified in the publication

substrate: malonyl-CoA


organism: African swine fever virus

substrate_name: dUTP

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

substrate: dUTP


proof_lines: mutant Q120A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant R149A, 25°C, pH 7.5, presence of K+, Mg2+


organism: Arabidopsis thaliana

proof_lines:
at pH 7.6 and 25°C
Raw SKiD Env: Temp=25°C, pH=7.6


organism: Dictyostelium discoideum

substrate_name: H2O; dUTP

substrate: H2O; dUTP


proof_lines: full-length protein, pH not specified in the publication, temperature not specified in the publication

proof_lines: core protein lacking N-terminal residues 1-37, pH not specified in the publication, temperature not specified in the publication


organism: Drosophila virilis


organism: Escherichia coli

proof_lines: wild-type enzyme, pH 7.8, room temperature


proof_lines: mutant L89A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant I90A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: wild-type, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant D29A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant F154A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant S73A, 25°C, pH 7.5, presence of K+, Mg2+


proof_lines: mutant S72A, 25°C, pH 7.5, presence of K+, Mg2+


organism: Aquifex aeolicus

proof_lines:
wild-type, pH 7.5, 75°C
wild-type, pH 7.5, 95°C


organism: Mesocricetus auratus

proof_lines: pH 7.0, 25°C, with cofactor 4-nitrophenyl acetate, recombinant wild-type enzyme

proof_lines: pH 7.0, 25°C, with cofactor acetyl-CoA, recombinant wild-type enzyme


proof_lines: pH 7.0, 25°C, recombinant mutant R64W, with 4-aminobenzoic acid

proof_lines: pH 7.0, 25°C, recombinant mutant R64W, with 4-nitrophenyl acetate


proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme, with 4-aminobenzoic acid

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme, with 4-nitrophenyl acetate


proof_lines: pH 7.0, 23°C, isozyme NAT2, with 4-nitrophenyl acetate


organism: Fusarium verticillioides

substrate_name: acetyl-CoA

proof_lines: pH 7.5, temperature not specified in the publication

substrate: acetyl-CoA


organism: Homo sapiens

substrate_name: 4-amino-3-methylbenzoic acid

assay_conditions_summary: pH 7; 296.15 K; cofactor ATP

proof_lines: pH 7.0, 23°C, isozyme NAT1, with 4-nitrophenyl acetate

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

substrate: 4-amino-3-methylbenzoic acid


substrate_name: 4-Aminobenzoic acid

proof_lines: Hep-G2 cells, presence of alpha-solanine, pH 7.5, 37°C

substrate: 4-Aminobenzoic acid


proof_lines: variant NAT2 4, pH 7.4, temperature not specified in the publication


organism: Bacillus anthracis

proof_lines:
apparent KM
isoenzyme BanatC


proof_lines:
apparent KM
isoenzyme BanatB


substrate_name: hydralazine

substrate: hydralazine


proof_lines: artificial full-length enzyme, pH 7.5, 37°C


organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ATP

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

substrate: Phosphoenolpyruvate; ADP


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor ATP


enzyme_display_name: prostaglandin-endoperoxide synthase

substrate_name: linoleic acid

assay_conditions_summary: pH 7.4; 297.15 K; buffer 100 mM Tris-HCl

proof_lines: isozyme PGHS-2, in 100 mM Tris-HCl buffer (pH 7.4), at 24°C

proof_lines: purified isoform PGHS-1, method: direct, O2

proof_lines: purified isoform PGHS-1, method: direct, arachidonate

enzyme: prostaglandin-endoperoxide synthase

substrate: linoleic acid


organism: Mus musculus

substrate_name: arachidonate

substrate: arachidonate


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


enzyme_display_name: dye decolorizing peroxidase

organism: Amycolatopsis sp.

proof_lines: pH and temperature not specified in the publication

enzyme: dye decolorizing peroxidase


organism: Auricularia auricula-judae

substrate_name: veratrylglycerol-beta-guaiacyl ether

substrate: veratrylglycerol-beta-guaiacyl ether


organism: Anabaena sp.

assay_conditions_summary: pH 4; 310.15 K; buffer 50 mM citrate

proof_lines: in 50 mM citrate buffer (pH 4.0-4.4), at 37°C


substrate_name: pyrogallol

proof_lines:
at pH 4.0 and 25°C
at pH 3.0 and 25°C

substrate: pyrogallol


organism: Bjerkandera adusta

substrate_name: Reactive Blue 19

substrate: Reactive Blue 19


organism: Irpex lacteus


organism: Amycolatopsis sp. ATCC 39116

proof_lines:
at pH 5.0 and 25°C
at pH 3.0 and 25°C


proof_lines:
wild type enzyme, at pH 3.0 and 25°C
wild type enzyme, at pH 3.5 and 25°C
wild type enzyme, at pH 3.0 and 30°C


substrate_name: Reactive Blue 5

proof_lines:
mutant enzyme W377S, at pH 3.5 and 25°C
mutant enzyme W377S, at pH 3.0 and 25°C
mutant enzyme W377S, at pH 2.5 and 25°C

substrate: Reactive Blue 5


organism: Saccharomonospora viridis

substrate_name: Reactive Yellow 2

substrate: Reactive Yellow 2


organism: Pseudomonas aeruginosa


organism: Thermobifida fusca YX

assay_conditions_summary: pH 3.5; 298.15 K; buffer 25 mM citrate

proof_lines: in 25 mM citrate buffer (pH 3.5), at 25°C


organism: Pleurotus sapidus

proof_lines:
at pH 4.0 and 30°C
at pH 4.5 and 30°C
at pH 3.8 and 30°C


organism: Shewanella oneidensis MR-1

assay_conditions_summary: pH 3.2; 298.15 K; buffer 25 mM citrate

proof_lines: in 25 mM citrate buffer, pH 3.2, at 25°C


organism: Thermomonospora curvata

substrate_name: guaiacol

proof_lines: with guaiacol as cosubstrate, mutant enzyme H312C, at pH 3.0 and 22°C

substrate: guaiacol


organism: Homo sapiens

substrate_name: O2; Arachidonate; Reduced acceptor

substrate: O2; Arachidonate; Reduced acceptor


substrate_name: Arachidonic acid; O2

substrate: Arachidonic acid; O2


substrate_name: Reactive Blue 4

proof_lines: with hydroquinone as cosubstrate, wild type enzyme, at pH 3.0 and 22°C

proof_lines: with guaiacol as cosubstrate, wild type enzyme, at pH 3.0 and 22°C

substrate: Reactive Blue 4


proof_lines: purified isoform PGHS-2, method: coupled, homo-vanilic acid

proof_lines: purified isoform PGHS-2, method: direct, O2

proof_lines: purified isoform PGHS-2, method: direct, arachidonate


proof_lines: pH 8.0, 25°C, COX-2 wild-type COX-2 and mutant N580A


proof_lines: with guaiacol as cosubstrate, mutant enzyme D220A, at pH 3.0 and 22°C


organism: Ovis aries

substrate_name: t-Butylhydroperoxide

smiles: CC(C)(C)OO

substrate: t-Butylhydroperoxide


substrate_name: Ethyl hydroperoxide

smiles: CCOO

substrate: Ethyl hydroperoxide


substrate_name: 15-HPETE; Guaiacol

substrate: 15-HPETE; Guaiacol


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)O)OO


smiles: OO


proof_lines: purified isoform PGHS-1, method: direct, O2

proof_lines: purified isoform PGHS-1, method: direct, arachidonate

proof_lines: purified isoform PGHS-1, method: coupled, homo-vanilic acid


organism: Salvelinus fontinalis

substrate_name: O2; alpha-Linolenate; Reduced acceptor

substrate: O2; alpha-Linolenate; Reduced acceptor


organism: Dictyostelium discoideum


enzyme_display_name: abscisate beta-glucosyltransferase

organism: Solanum lycopersicum

substrate_name: UDPglucose; Abscisate

enzyme: abscisate beta-glucosyltransferase

substrate: UDPglucose; Abscisate


enzyme_display_name: beta-galactosidase

organism: Aspergillus niger

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

enzyme: beta-galactosidase

substrate: 2-nitrophenyl beta-D-galactopyranoside


substrate_name: H2O; Lactose

substrate: H2O; Lactose


organism: Aspergillus oryzae

proof_lines:
pH 4.5, 60°C
Raw SKiD Env: Temp=60°C, pH=4.5
Raw SKiD Env: Temp=60°C, pH=5


substrate_name: 2-nitrophenyl beta-D-galactoside

substrate: 2-nitrophenyl beta-D-galactoside


organism: Bacillus coagulans

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: Bacillus subtilis

substrate_name: H2O; p-Nitrophenyl-beta-D-galactoside

substrate: H2O; p-Nitrophenyl-beta-D-galactoside


organism: Bacteroides ovatus


organism: Arthrobacter sp.


substrate_name: o-nitrophenyl beta-D-galactopyranoside

proof_lines:
at 5°C
at 18°C
at 10°C

substrate: o-nitrophenyl beta-D-galactopyranoside


proof_lines:
at 10°C
at 50°C
at 20°C


enzyme_display_name: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

organism: Escherichia coli


substrate_name: Protein N-phosphohistidine; D-Fructose

substrate: Protein N-phosphohistidine; D-Fructose


enzyme_display_name: DNA primase DnaG

substrate_name: rNTP

enzyme: DNA primase DnaG

substrate: rNTP


organism: Saccharolobus solfataricus

substrate_name: NTP

substrate: NTP


proof_lines: KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, in presence of M13 ssDNA as template, wild-type enzyme

proof_lines: KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, 1 mM Mn2+, in presence of M13 ssDNA as template, wild-type enzyme


proof_lines: KM-value is determined by measuring the priming rate at different concentrations of NTPs, 70°C, pH 8.5, in presence of M13 ssDNA as template, mutant enzyme E175Q


organism: Alicyclobacillus acidocaldarius


substrate_name: lactulose

substrate: lactulose


organism: Arabidopsis thaliana


organism: Arthrobacter psychrolactophilus


organism: Bifidobacterium bifidum

substrate_name: Lactose; H2O

substrate: Lactose; H2O


organism: Bispora sp.

substrate_name: lactose

assay_conditions_summary: pH 1.5; buffer note 'in glycine-HCl

substrate: lactose


organism: Caldicellulosiruptor saccharolyticus

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 2-phospho-L-lactate transferase

organism: Methanocaldococcus jannaschii

enzyme: 2-phospho-L-lactate transferase


organism: Kluyveromyces lactis

substrate_name: alpha-Lactose; H2O

substrate: alpha-Lactose; H2O


organism: Kluyveromyces marxianus


organism: Lacticaseibacillus casei

substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Haloferax volcanii

proof_lines: pH 7.2, 22°C, the enzyme also shows beta-fucosidase activity


organism: Lactobacillus delbrueckii subsp. bulgaricus


organism: Limosilactobacillus reuteri

proof_lines:
recombinant enzyme, pH 6.5, 30°C
native enzyme, pH 6.5, 30°C


organism: Lactobacillus acidophilus


organism: Lactobacillus delbrueckii

proof_lines: wild type enzyme, in 100 mM sodium acetate buffer pH 5.5, at 45°C


proof_lines: mutant enzyme E491A, in HEPES buffer pH 6.5, at 45°C


organism: Escherichia coli


assay_conditions_summary: pH 7; 298.15 K; buffer 30 mM TES

proof_lines: mutant enzyme H418F, in 30 mM TES buffer, 10 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C


proof_lines: wild type enzyme, in 30 mM TES buffer, 145 mM NaCl, pH 7.0 at 25°C

proof_lines: wild type enzyme, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


proof_lines: mutant enzyme H418N, in 30 mM TES buffer, 0.01 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C

proof_lines: mutant enzyme H418N, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


proof_lines: mutant enzyme H418E, in 30 mM TES buffer, 0.01 mM Mg2+, 150 mM Na+, pH 7.0 at 25°C

proof_lines: mutant enzyme H418E, in 30 mM TES buffer, 145 mM NaCl, 0.01 mM Mg2+, pH 7.0 at 25°C


proof_lines:
native enzyme
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


enzyme_display_name: L-arabinonolactonase

organism: Halobacterium volcanii

substrate_name: H2O; L-Arabinono-1,4-lactone

enzyme: L-arabinonolactonase

substrate: H2O; L-Arabinono-1,4-lactone


substrate_name: D-xylono-gamma-lactone

substrate: D-xylono-gamma-lactone


organism: Mus musculus


organism: Oryza sativa

proof_lines: pH 3.5, 60°C, recombinant isozyme OsGal1


organism: Pantoea agglomerans


organism: Pediococcus pentosaceus


organism: Planococcus sp. (in: firmicutes)


organism: Priestia megaterium


organism: Pseudoalteromonas haloplanktis


organism: Putranjiva roxburghii

substrate_name: 4-nitrophenyl beta-D-glucopyranoside

proof_lines:
pH 4.6, 37°C, native enzyme
pH 4.6, 37°C, recombinant enzyme

substrate: 4-nitrophenyl beta-D-glucopyranoside


organism: Raphanus sativus


organism: Saccharolobus solfataricus


proof_lines: pH 7.5, 80°C, recombinant mutant enzyme F441Y


proof_lines:
Raw SKiD Env: Temp=30°C, pH=6.5
Raw SKiD Env: Temp=80°C, pH=7.5


enzyme_display_name: maleylpyruvate hydrolase

organism: Aquipseudomonas alcaligenes

enzyme: maleylpyruvate hydrolase


organism: Sphingobium sp. SYK-6

proof_lines:
pH 7.2, 23°C
Raw SKiD Env: Temp=23°C, pH=7.2


enzyme_display_name: histidine decarboxylase

organism: Clostridium perfringens

substrate_name: L-Histidine

enzyme: histidine decarboxylase

substrate: L-Histidine


enzyme_display_name: asparaginase

organism: Saccharomyces cerevisiae

substrate_name: H2O; L-Asparagine

enzyme: asparaginase

substrate: H2O; L-Asparagine


organism: Solanum lycopersicum


organism: Synechocystis sp.


organism: Homo sapiens

substrate_name: L-histidine

proof_lines: pH and temperature not specified in the publication

substrate: L-histidine


proof_lines: mutant C179S/Y334F/C417S, product imidazole acetaldehyde, pH 6.5, 37°C


proof_lines: mutant C179S/C417S, product histamine, pH 6.5, 37°C


organism: Lactobacillus buchneri


organism: Sulfolobus solfataricus


organism: Trichoderma reesei

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: uncultured microorganism

substrate_name: 4-nitrophenyl beta-D-fucopyranoside

proof_lines: pH 6.0, 60°C, additive: 25 mM cellobiose

proof_lines: pH 6.0, 60°C, additive: 250 mM D-galactose

substrate: 4-nitrophenyl beta-D-fucopyranoside


organism: Arabidopsis thaliana


organism: Escherichia coli

substrate_name: L-Aspartyl-beta-hydroxamate; H2O

substrate: L-Aspartyl-beta-hydroxamate; H2O


organism: Mycobacterium tuberculosis


organism: Nostoc sp.


organism: Rattus norvegicus

substrate_name: H2O; L-Aspartic acid beta-(7-amido-4-methylcoumarin)


organism: Lactobacillus sp.


assay_conditions_summary: pH 7


organism: Morganella morganii

proof_lines: mutant C53S/C330S/C340S, product histamine, pH 6.5, 37°C


proof_lines: mutant C53S/Y260F/C330S/C340S, product imidazole acetaldehyde, pH 6.5, 37°C


organism: Staphylococcus epidermidis


organism: Azospirillum brasilense


organism: Mus musculus


organism: Oenococcus oeni


organism: Variovorax paradoxus


organism: Homo sapiens

substrate_name: arachidonic acid

proof_lines:
isozyme 1 and 2
isozyme 2
native enzyme

substrate: arachidonic acid


organism: Kluyveromyces lactis

substrate_name: o-nitrophenyl-beta-D-galactoside

proof_lines:
isoenzyme betaG41
isoenzyme betaG630
isoenzyme betaG550

substrate: o-nitrophenyl-beta-D-galactoside


proof_lines:
pH 7.5, 30°C, isozyme BGT I
pH 7.5, 35°C, isozyme BGT I
pH 7.5, 30°C, isozyme BGT II


organism: Unknown


organism: Irpex lacteus

substrate_name: veratryl alcohol

assay_conditions_summary: pH 2

proof_lines: pH 2.0, temperature not specified in the publication

proof_lines: pH 3.0, temperature not specified in the publication

proof_lines: pH 4.0, temperature not specified in the publication

substrate: veratryl alcohol


proof_lines: native wild type enzyme, at pH 2.0 and 25°C

proof_lines: recombinant wild type enzyme, at pH 4.5 and 25°C

proof_lines: recombinant wild type enzyme, at pH 2.0 and 25°C


organism: Physeter macrocephalus

substrate_name: guaiacol

substrate: guaiacol


organism: Pleurotus ostreatus

proof_lines:
at pH 6.0 and 28°C
at pH 4.0 and 30°C


organism: Pseudomonas putida

substrate_name: Acid Blue 62

proof_lines: with 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 5.0 and 30°C

substrate: Acid Blue 62


proof_lines: mutant enzyme E188K/A142V, at pH 5.5 and 25°C


proof_lines: mutant enzyme E188K/A142V/H125Y, at pH 5.5 and 25°C

proof_lines: mutant enzyme E188K/A142V/H125Y, at pH 8.0 and 25°C

proof_lines: mutant enzyme E188K/A142V/H125Y, at pH 8.5 and 25°C