sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation E276Q reconstructed after residue check and applied mutation signature E276Q to reconstruct the assayed variant sequence.

proof_lines: mutant E276Q, pH not specified in the publication, temperature not specified in the publication


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

substrate_name: dTTP

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

substrate: dTTP

source: uniprot


enzyme_display_name: trehalose-phosphatase

organism: Escherichia coli (strain K12)

substrate_name: Tre6P (with magnesium ions as cofactor and at pH 9)

assay_conditions_summary: pH 9

enzyme: trehalose-phosphatase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: trehalose-6-phosphate (at 37 degrees Celsius and pH 7.5)


organism: Oryza sativa subsp. japonica

substrate_name: trehalose 6-phosphate

substrate: trehalose 6-phosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: trehalose 6-phosphate (at pH 6.0)

assay_conditions_summary: pH 6

substrate: trehalose 6-phosphate (at pH 6.0)


enzyme_display_name: histone acetyltransferase

organism: Homo sapiens

substrate_name: succinyl-CoA

source_db: brenda

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

sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q92830

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

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

source_databases_merged: brenda skid

enzyme: histone acetyltransferase

substrate: succinyl-CoA

source: brenda


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q92793

proof_lines: against P300, pH and temperature not specified in the publication

substrate: Unknown


organism: Saccharomyces cerevisiae

substrate_name: Acetyl-CoA; Histone

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

sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q03330

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; Histone


substrate_name: Acetyl-CoA

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

data_origin: experimental

substrate: Acetyl-CoA

status: unverified

source: oed


substrate_name: acetyl-CoA

sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649 and applied mutation signature C304A to reconstruct the assayed variant sequence.

mutation_type: substitution


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649 and applied mutation signature C304S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649 and applied mutation signature E338Q to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: serotonin

substrate: serotonin


organism: Zea mays

substrate_name: core histones

substrate: core histones


enzyme_display_name: oxaloacetate decarboxylase

organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)

enzyme: oxaloacetate decarboxylase


enzyme_display_name: adenosylmethionine decarboxylase

substrate_name: S-adenosyl-L-methionine

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

enzyme: adenosylmethionine decarboxylase

substrate: S-adenosyl-L-methionine


substrate_name: S-adenosyl-L-methionine (at 25 degrees Celsius in the presence of 0.01 M MgCl(2))


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


organism: Trypanosoma brucei brucei

substrate_name: S-adenosyl-L-methionine (at 37 degrees Celsius)


organism: Trypanosoma cruzi

substrate_name: S-adenosyl-L-methionine (at pH 7.5)

substrate: S-adenosyl-L-methionine (at pH 7.5)


enzyme_display_name: malyl-CoA lyase

organism: Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

substrate_name: (S)-malyl-CoA (cleavage reaction)

enzyme: malyl-CoA lyase

substrate: (S)-malyl-CoA (cleavage reaction)


organism: Rhodobacter capsulatus

substrate_name: L-malyl-CoA

substrate: L-malyl-CoA


enzyme_display_name: glucarate dehydratase

substrate_name: idarate

enzyme: glucarate dehydratase

substrate: idarate


enzyme_display_name: nitrile hydratase

organism: Rhodococcus rhodochrous

substrate_name: 3-cyanopyridine (at pH 7.0 and 20 degrees Celsius)

enzyme: nitrile hydratase


enzyme_display_name: L-fuculose-phosphate aldolase

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

substrate_name: dihydroxyacetone phosphate (DHAP)

enzyme: L-fuculose-phosphate aldolase

substrate: dihydroxyacetone phosphate (DHAP)


organism: Pseudomonas putida (strain ATCC 700007 / DSM 6899 / JCM 31910 / BCRC 17059 / LMG 24140 / F1)

substrate_name: oxaloacetate (in presence of 1 mM of magnesium)


organism: Pseudomonas straminea


organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

substrate_name: glyoxylate (for L-malyl-CoA formation)

substrate: glyoxylate (for L-malyl-CoA formation)


organism: Chloroflexus aurantiacus

substrate_name: (S)-malyl-CoA (for L-malyl-CoA lyase activity)


enzyme_display_name: tyrosine 3-monooxygenase

substrate_name: tetrahydrobiopterin

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

proof_lines: E332D phosphorylated mutant protein, pH 7.2, 30°C

proof_lines: E332D mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C

enzyme: tyrosine 3-monooxygenase

substrate: tetrahydrobiopterin


proof_lines: A297L phosphorylated mutant protein, pH 7.2, 30°C

proof_lines: mutant enzyme A297L, pH and temperature not specified in the publication


sequence_source: UniProt P07101 canonical FASTA, retrieved 2026-06-04 via UniProt REST


proof_lines: Y371F phosphorylated mutant protein, pH 7.2, 30°C

proof_lines: Y371F mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C


organism: Bos taurus

substrate_name: O2; L-Tyrosine; Tetrahydrobiopterin

sequence_source: UniProtKB:P17289 reviewed FASTA via rest.uniprot.org on 2026-06-04

substrate: O2; L-Tyrosine; Tetrahydrobiopterin


organism: Homo sapiens

substrate_name: Tetrahydrobiopterin; L-Tyrosine; O2

sequence_source: UniProtKB:P07101 reviewed FASTA via rest.uniprot.org on 2026-06-04

substrate: Tetrahydrobiopterin; L-Tyrosine; O2


proof_lines: L294A phosphorylated mutant protein, pH 7.2, 30°C


proof_lines: F300Y phosphorylated mutant protein, pH 7.2, 30°C


proof_lines: F300A phosphorylated mutant protein, pH 7.2, 30°C


proof_lines: wild type protein, in the presence of 0.01 mM dopamine, pH 7.2, 30°C

proof_lines: wild type, phosphorylated protein, pH 7.2, 30°C


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

proof_lines: L294Y phosphorylated mutant protein, pH 7.2, 30°C


substrate_name: L-tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E362G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E362G, pH and temperature not specified in the publication

substrate: L-tyrosine


proof_lines: mutant enzyme K366L, pH and temperature not specified in the publication


proof_lines: mutant enzyme E365G, pH and temperature not specified in the publication


proof_lines: mutant enzyme E362R/E365R, pH and temperature not specified in the publication


proof_lines: mutant enzyme R37E/R38E, pH and temperature not specified in the publication


proof_lines: mutant enzyme D361N, pH and temperature not specified in the publication


proof_lines: mutant enzyme S368A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature K169E/L479A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme K169E/L479A, dimer


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature E114K to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme E114K, tetramer


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature D467G to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme D467G, tetramer > dimer

proof_lines: pH 7.0, 30°C, mutant enzyme D467G dimer > tetramer


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature R410P to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme R410P, tetramer > dimer


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P04177; reconstructed variant from selected source mutation note. and applied mutation signature F309A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant F309A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P04177; reconstructed variant from selected source mutation note. and applied mutation signature F300A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant F300A


proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant V379D


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425S, in 50 mM HEPES (pH 7.0), at 30°C


substrate_name: L-phenylalanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425E, in 50 mM HEPES (pH 7.0), at 30°C

substrate: L-phenylalanine


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425N, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature Q424A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q424A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425T, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425Y, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425H, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature Q426A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q426A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S40E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S40E


sequence_source: UniProtKB P04177 FASTA fetched during review.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S19A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S19A


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S19E/S40E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S19E/S40E


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S40A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S40A


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S8A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S8A


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S19E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S19E


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S31A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S31A


verification_status: corrected

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

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04177 and applied mutation signature D425V to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'D425V TyrH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 1.24; column 'Ktyr (µM)' = 45; column 'V/Ktyr (µM-1 min-1)' = 0.028. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'D425V TyrH': Ktyr = 45 uM; Vmax for tyrosine hydroxylation = 1.24 min^-1; V/Ktyr = 0.028 uM^-1 min^-1.

row_label: Table 3, enzyme row 'D425V TyrH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)

status: corrected


substrate_name: L-Tyrosine

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/V379D PheH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 1.2; column 'Ktyr (µM)' = 146; column 'V/Ktyr (µM-1 min-1)' = 8.2 x 10^-3. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/V379D PheH': Ktyr = 146 uM; Vmax for tyrosine hydroxylation = 1.2 min^-1; V/Ktyr = 8.2 x 10^-3 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/V379D PheH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)

substrate: L-Tyrosine

status: verified


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04176; variant reconstructed by worker residue check and applied mutation signature H264Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H264Q


table_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661)


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04177; variant reconstructed by worker residue check and applied mutation signature H331E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H331E


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04177; variant reconstructed by worker residue check and applied mutation signature H336E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H336E


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04177; variant reconstructed by worker residue check and applied mutation signature H336Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H336Q


substrate_name: L-Phenylalanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 direct FASTA lookup on 2026-06-04 plus Y371F reconstruction from PMID 9819237 and applied mutation signature Y371F to reconstruct the assayed variant sequence.

substrate: L-Phenylalanine


sequence_source: UniProtKB P04177 direct FASTA lookup on 2026-06-04


sequence_source: UniProtKB P04177 direct FASTA lookup on 2026-06-04 plus Y371F reconstruction from PMID 9819237

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant Y371F


organism: Saccharomyces cerevisiae

substrate_name: acetyl-CoA

sequence_source: UniProtKB Q07794 direct FASTA lookup on 2026-06-04

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425R substitution from canonical sequence and applied mutation signature D425R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425R, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed T427A substitution from canonical sequence and applied mutation signature T427A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T427A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425M substitution from canonical sequence and applied mutation signature D425M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425M, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425C substitution from canonical sequence and applied mutation signature D425C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425C, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425L substitution from canonical sequence and applied mutation signature D425L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425L, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425K substitution from canonical sequence and applied mutation signature D425K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425K, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425A substitution from canonical sequence and applied mutation signature D425A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed Y423A substitution from canonical sequence and applied mutation signature Y423A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y423A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04177 and applied mutation signature Q310H to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'Q310H TyrH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 128; column 'Ktyr (µM)' = 54; column 'V/Ktyr (µM-1 min-1)' = 2.37. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'Q310H TyrH': Ktyr = 54 uM; Vmax for tyrosine hydroxylation = 128 min^-1; V/Ktyr = 2.37 uM^-1 min^-1.

row_label: Table 3, enzyme row 'Q310H TyrH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/Y277H/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/Y277H/V379D PheH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 1.83; column 'Ktyr (µM)' = 1310; column 'V/Ktyr (µM-1 min-1)' = 1.4 x 10^-3. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/Y277H/V379D PheH': Ktyr = 1310 uM; Vmax for tyrosine hydroxylation = 1.83 min^-1; V/Ktyr = 1.4 x 10^-3 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/Y277H/V379D PheH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04177 and applied mutation signature H323Y to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H323Y TyrH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 159; column 'Ktyr (µM)' = 92; column 'V/Ktyr (µM-1 min-1)' = 1.73. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H323Y TyrH': Ktyr = 92 uM; Vmax for tyrosine hydroxylation = 159 min^-1; V/Ktyr = 1.73 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H323Y TyrH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


sequence_variant_note: Resolved canonical sequence from UniProt REST P04176 canonical sequence reconstructed with mutation Y277H and applied mutation signature Y277H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant Y277H


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected SABIO-RK mutant note S31E and applied mutation signature S31E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S31E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected SABIO-RK mutant note S8E and applied mutation signature S8E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S8E


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

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant TyrHpS31


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425I and applied mutation signature D425I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425I, in 50 mM HEPES (pH 7.0), at 30°C


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

proof_lines: wild type enzyme, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425G and applied mutation signature D425G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425G, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425Q and applied mutation signature D425Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425Q, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425F and applied mutation signature D425F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425F, in 50 mM HEPES (pH 7.0), at 30°C


enzyme_display_name: Histone acetyltransferase RTT109

sequence_variant_note: Resolved canonical sequence from direct UniProt REST lookup for Q07794 on 2026-06-04 and applied mutation signature D287N to reconstruct the assayed variant sequence.

enzyme: Histone acetyltransferase RTT109


substrate_name: histone H3 tail peptide

sequence_variant_note: Resolved canonical sequence from direct UniProt REST lookup for Q07794 on 2026-06-04 and applied mutation signature D287A/D288A to reconstruct the assayed variant sequence.

substrate: histone H3 tail peptide


sequence_variant_note: Resolved canonical sequence from direct UniProt REST lookup for Q07794 on 2026-06-04 and applied mutation signature D288N to reconstruct the assayed variant sequence.


sequence_source: direct UniProt REST lookup for Q07794 on 2026-06-04


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetoacetyl-CoA

proof_lines: kcat is 4.8 sec(-1) with acetoacetyl-CoA as substrate.

enzyme: acetyl-CoA C-acyltransferase

substrate: acetoacetyl-CoA


organism: Escherichia coli (strain K12)

substrate_name: a synthetic histone H3K9 acetyllysine peptide

proof_lines: kcat is 0.135 sec(-1) for acetyllysine peptide. kcat is 0.242 sec(-1) for succinyllysine peptide.


substrate_name: NAD

proof_lines: kcat is 0.08 sec(-1) for histone H4 H4K16la.

substrate: NAD


proof_lines: kcat is 0.0049 sec(-1) for N6-tetradecanoyl-L-lysyl-peptide (myristoylated peptide) (PubMed:23552949). kcat is 0.0027 sec(-1) for N6-hexadecanoyl-L-lysyl-peptide (palmitoylated peptide) (PubMed:23552949). kcat is 0.0020 sec(-1) for N6-tetra


substrate_name: a peptide of H3 biotinylated at 'Lys-9'

proof_lines: kcat is 0.0019 sec(-1) for the delipoylation of H3 'Lys-9'. kcat is 0.0005 sec(-1) for the debiotinylation of H3 'Lys-9'. kcat is 0.0018 sec(-1) for the delipoylation of DLAT 'Lys-259'.

substrate: a peptide of H3 biotinylated at 'Lys-9'


substrate_name: an peptide acetylated on lysine

proof_lines: kcat is 0.275 sec(-1) with a peptide acetylated on lysine as substrate (PubMed:25704306). kcat is 0.018 sec(-1) with a peptide myristoylated on lysine as substrate (PubMed:25704306).

substrate: an peptide acetylated on lysine


substrate_name: phenylalanine

substrate: phenylalanine


proof_lines: kcat is 1.27 min(-1) with N(6)-acetyl-L-lysyl-[HupB] as substrate.


organism: Proteus mirabilis (strain HI4320)

proof_lines: kcat is 0.225 sec(-1) for a N6-(2-hydroxyisobutyryl)lysine peptide.


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Arabidopsis thaliana

substrate_name: pimeloyl-CoA (at pH 7.5 and 30 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: kcat is 0.1 sec(-1) with pimeloyl-CoA as substrate. kcat is 0.11 sec(-1) with L-alanine as substrate.

enzyme: 8-amino-7-oxononanoate synthase


substrate_name: pimeloyl-CoA (at pH 7.7 and 25 degrees Celsius)

assay_conditions_summary: pH 7.7; cofactor CoA

proof_lines: kcat is 0.007 sec(-1) and 0.0036 sec(-1) with L-alanine and D-alanine as substrate, respectively, and pimeloyl-CoA as co-substrate.


proof_lines: kcat is 172 min(-1) with acetyl-CoA as substrate (PubMed:27382063). kcat is 173 min(-1) with a histone H4 peptide as substrate (PubMed:27382063). kcat is 15 min(-1) with a histone H4K16 peptide as substrate (PubMed:33467728).


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: acetyl-CoA (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone)

proof_lines: kcat is 0.11 sec(-1) with acetyl-CoA as substrate (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone) (PubMed:20560668). kcat is 0.19 sec(-1) with acetyl-CoA as substrate (at pH 7.0, 25 degrees Celsius in the presence of VPS7


substrate_name: lipid I

substrate: lipid I


substrate_name: tRNA(Tyr)

proof_lines: kcat is 0.00121 sec(-1) with tRNA(Tyr) and guanine as substrates.

substrate: tRNA(Tyr)


organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

proof_lines: kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates.


enzyme_display_name: N(1)-aminopropylagmatine synthase

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

substrate_name: agmatine

proof_lines: kcat is 2.09 sec(-1) for aminopropyl transferase activity with cadaverine as amine acceptor. kcat is 0.18 sec(-1) for aminopropyl transferase activity with putrescine as amine acceptor. kcat is 0.1 sec(-1) for aminopropyl transferase activi

enzyme: N(1)-aminopropylagmatine synthase

substrate: agmatine


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: agmatine (at pH 9 and 70 degrees Celsius)

proof_lines: kcat is 0.3 sec(-1) for aminopropyl transferase activity with putrescine as substrate (at pH 9 and 70 degrees Celsius). kcat is 0.28 sec(-1) for aminopropyl transferase activity with agmatine as substrate (at pH 9 and 70 degrees Celsius). k


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: norspermidine (at pH 9 and 37 degrees Celsius)

sequence_source: source_record; direct UniProt REST exact match to Q5SK28

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de


enzyme_display_name: adenosyl-fluoride synthase

organism: Actinoplanes sp. (strain N902-109)

substrate_name: S-adenosyl-L-methionine

sequence_source: source_record; direct UniProt REST exact match to R4LHX8

enzyme: adenosyl-fluoride synthase

substrate: S-adenosyl-L-methionine


organism: Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1)

sequence_source: source_record; direct UniProt REST exact match to W8JNL4


organism: Streptantibioticus cattleyicolor

substrate_name: SAM (at pH 7.8 and degrees Celsius)

sequence_source: source_record; direct UniProt REST exact match to Q70GK9

proof_lines: kcat is 0.07 sec(-1) for 5'-FDA synthase activity with SAM as substrate(at pH 7.9 and 37 degrees Celsius). kcat is 0.06 sec(-1) for 5'-FDA synthase activity with fluoride as substrate (at pH 7.9 and 37 degrees Celsius).

substrate: SAM (at pH 7.8 and degrees Celsius)


organism: Streptomyces sp

substrate_name: S-adenosyl-L-methionine (for fluorinase activity)

sequence_source: source_record; direct UniProt REST exact match to W0W999

proof_lines: kcat is 0.262 min(-1) for fluorinase activity (PubMed:24449539). kcat is 0.22 min(-1) for fluorinase activity (PubMed:27739177). kcat is 0.017 min(-1) for SAM hydrolase activity (PubMed:36996195). kcat is 0.008 min(-1) for chlorinase activi


enzyme_display_name: serine--glyoxylate transaminase

substrate_name: alanine (with recombinant enzyme, in the presence of 20 mM glyoxylate)

sequence_source: source_record; direct UniProt REST exact match to Q56YA5

proof_lines: kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for L-alanine.

enzyme: serine--glyoxylate transaminase


enzyme_display_name: histidinol-phosphate transaminase

substrate_name: histidinol phosphate

proof_lines: kcat is 426 sec(-1) with histidinol phosphate as substrate. kcat is 220 sec(-1) with phenylalanine as substrate. kcat is 3100 sec(-1) with tyrosine as substrate.

enzyme: histidinol-phosphate transaminase

substrate: histidinol phosphate


enzyme_display_name: ribokinase

substrate_name: D-ribose

assay_conditions_summary: cofactor ATP

enzyme: ribokinase

substrate: D-ribose


organism: Leishmania major

substrate_name: ATP

proof_lines: kcat is 10.2 sec(-1) with ATP as substrate and 10.8 sec(-1) with ribose as substrate.

substrate: ATP


proof_lines: kcat is 7.3 sec(-1) with glucose-1-phosphate as substrate. kcat is 7.9 sec(-1) with dTTP as substrate.


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

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


enzyme_display_name: arylesterase

organism: Gluconobacter oxydans

substrate_name: phenyl acetate

sequence_source: UniProtKB Q5FSJ2 direct REST lookup on 2026-06-04

enzyme: arylesterase

substrate: phenyl acetate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: S-methyl thiobutanoate

smiles: CCCC(=O)SC

substrate: S-methyl thiobutanoate


substrate_name: 2-naphthyl butanoate

assay_conditions_summary: pH 7

substrate: 2-naphthyl butanoate


organism: Homo sapiens

proof_lines:
enzyme variant Q192
enzyme variant R192


substrate_name: 2-naphthyl acetate

assay_conditions_summary: pH 8

proof_lines: pH 8.0, recombinant genetic variant G1B11

proof_lines: pH 8.0, recombinant genetic variant G1A7

proof_lines: pH 8.0, recombinant genetic variant G2C2

substrate: 2-naphthyl acetate


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P27169 direct REST lookup on 2026-06-04 and applied mutation signature G11S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature E314A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature N133S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature E313A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST P27169 canonical sequence; no single variant sequence reconstructed

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

proof_lines: mutant G11A or mutant G11C, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature F222Y to reconstruct the assayed variant sequence.

proof_lines:
pH 8.0, 25°C, mutant enzyme F222Y
mutant F222Y, pH 8.0, 25°C


sequence_source: UniProt REST Q15166 canonical sequence


substrate_name: Phenylacetic acid; H2O

sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature H115Q/H134Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant H115Q/H134Q

substrate: Phenylacetic acid; H2O


substrate_name: H2O; Phenylacetic acid

sequence_source: UniProt REST P27169 canonical sequence

assay_conditions_summary: pH 8; 298.15 K; buffer pH 8

proof_lines: isoform PON1, pH and temperature not specified in the publication

substrate: H2O; Phenylacetic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with H134Q reconstructed after residue check on 2026-06-04 and applied mutation signature H134Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant H134Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with H115Q reconstructed after residue check on 2026-06-04 and applied mutation signature H115Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant H115Q


substrate_name: naphthalen-2-yl acetate

sequence_source: UniProtKB P27169 canonical FASTA checked on 2026-06-04

proof_lines: wild type enzyme, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 8.0), at 25°C

substrate: naphthalen-2-yl acetate


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with Q192R reconstructed after residue check on 2026-06-04 and applied mutation signature Q192R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q192R, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 8.0), at 25°C


sequence_source: NCBI GenBank KC456194.1 / protein AGZ62947.1 translation, with UniProtKB P27169 as the human PON1 accession context

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with H115W reconstructed after residue check on 2026-06-04 and applied mutation signature H115W to reconstruct the assayed variant sequence.


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


sequence_source: UniProtKB P27169 FASTA with H115W reconstructed after residue check on 2026-06-04


substrate_name: 4-nitrophenyl propionate

sequence_variant_note: Resolved canonical sequence from uniprot:Q15165 and applied mutation signature S311C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S311C, at pH 8.5 and 40Â°C

substrate: 4-nitrophenyl propionate


mutation_type: deletion

proof_lines: mutant enzyme 123-124del, at pH 8.5 and 40Â°C


sequence_variant_note: Resolved canonical sequence from uniprot:Q15165 and applied mutation signature A148G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A148G, at pH 8.5 and 40Â°C


organism: Lacticaseibacillus casei

substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


organism: Lactobacillus casei

substrate_name: p-Nitrophenyl acetate; H2O

substrate: p-Nitrophenyl acetate; H2O


organism: Lactobacillus helveticus


substrate_name: H2O; Nafamostat

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

assay_conditions_summary: pH 7.4; 303.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication

substrate: H2O; Nafamostat


organism: Unknown


organism: Mus musculus

sequence_source: UniProtKB reviewed FASTA accession Q62087, direct REST check 2026-06-04


sequence_source: UniProtKB reviewed FASTA accession P52430, direct REST check 2026-06-04

proof_lines: wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C

proof_lines: wild type enzyme, in 20 mM Tris-HCl and 0.9 mM CaCl2, at pH 8 and 25°C


organism: Oryctolagus cuniculus

sequence_source: UniProtKB reviewed FASTA accession Q9BGN0, direct REST check 2026-06-04


organism: Pseudomonas fluorescens

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant D99E C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant F227I C-terminal His6-tagged


sequence_source: UniProtKB reviewed FASTA accession P22862, direct REST check 2026-06-04

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


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant L29P C-terminal His6-tagged


substrate_name: H2O; p-Nitrophenyl acetate

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant T122P C-terminal His6-tagged

substrate: H2O; p-Nitrophenyl acetate


enzyme_display_name: arsenate reductase (thioredoxin)

organism: Bacillus subtilis (strain 168)

substrate_name: arsenate (in the presence of KCl)

proof_lines: kcat is 96 min(-1) in the presence of KCl (PubMed:16797027). kcat is 80 min(-1) in the presence of NaCl (PubMed:16797027). kcat is 120 min(-1) in the presence of Na(2)SO(4) (PubMed:16797027). kcat is 95 min(-1) in the presence of K(2)SO(4)

enzyme: arsenate reductase (thioredoxin)

substrate: arsenate (in the presence of KCl)


organism: Staphylococcus aureus

substrate_name: arsenate (below 1 mM arsenate)

proof_lines: kcat is 4.5 min(-1) with arsenate as substrate (at 2 uM arsenate) and kcat is 9.9 min(-1) with arsenate as substrate (at 10 mM arsenate) (PubMed:10606519). kcat is 54 min(-1) in the presence of KCl (PubMed:12682056, PubMed:16797027). kcat i

substrate: arsenate (below 1 mM arsenate)


enzyme_display_name: lactaldehyde dehydrogenase

organism: Escherichia coli (strain K12)

substrate_name: L-lactaldehyde

proof_lines: kcat is 761 sec(-1) with L-lactaldehyde as substrate (PubMed:27671251). kcat is 52 sec(-1) with glycolaldehyde as substrate (PubMed:31850327). kcat is 1100 min(-1) with glycolaldehyde as substrate. kcat is 37 min(-1) with acetaldehyde as su

enzyme: lactaldehyde dehydrogenase

substrate: L-lactaldehyde


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

substrate_name: propionaldehyde (at pH 7.5)

proof_lines: As the lactaldehyde used was a mixture of D and L isomers, the kinetic parameters do not reflect the possible stereospecificity of the enzyme.

substrate: propionaldehyde (at pH 7.5)


substrate_name: acetoacetyl-CoA

proof_lines: kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1) for octanoyl-CoA hydrolysis (PubMed:254

substrate: acetoacetyl-CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: CoA

proof_lines: kcat is 0.725 sec(-1) for 3,22-dioxochol-4-en-24-oyl-CoA substrate (PubMed:25482540). kcat is 0.076 sec(-1) for AcAcCoA substrate (PubMed:19822655). kcat is 0.018 sec(-1) for CoA substrate (PubMed:19822655).

substrate: CoA


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant Y69M C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant M95T C-terminal His6-tagged


organism: Rattus norvegicus

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant S74A


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant S74T


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant S74C


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


substrate_name: phenyl acetate

proof_lines: wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C

substrate: phenyl acetate


organism: Saccharolobus islandicus

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Saccharolobus solfataricus

sequence_source: UniProtKB B5BLW5 direct lookup on 2026-06-04; local identity cache preserved the same source_record sequence.

assay_conditions_summary: pH 7; 333.15 K; buffer 100 mM sodium phosphate

proof_lines: recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB Q4J6Z8 direct lookup on 2026-06-04.


organism: Sulfolobus islandicus

sequence_source: UniProtKB C4KKZ9 direct lookup on 2026-06-04.

assay_conditions_summary: pH 8; 298.15 K; buffer activity

column_label: Retained PLOS PDF page 8, Table 4, pNP-acetate (VIII), SisLac columns: kcat 0.20 +/- 0.01; Km 124 +/- 36 uM; kcat/Km 1.6 (+/- 0.5) x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Table 4: kcat 0.20 s^-1; Km 124 uM = 0.124 mM; independently printed kcat/Km 1.6 x 10^3 M^-1 s^-1 = 1.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 cells: kcat 0.20 +/- 0.01 s^-1; Km 124 +/- 36 uM; independently printed kcat/Km central value 1.6 x 10^3 M^-1 s^-1 with reported uncertainty +/- 0.5 x 10^3 M^-1 s^-1.

row_label: pNP-acetate (VIII) / SisLac

table_label: Table 4. Esterase activity of SisLac.


organism: uncultured organism

substrate_name: 1-naphthyl acetate

sequence_source: UniProtKB G0YFD9 direct lookup on 2026-06-04.

substrate: 1-naphthyl acetate


organism: Vulcanisaeta moutnovskia

sequence_source: UniProtKB F0QXN6 direct lookup on 2026-06-04.


enzyme_display_name: cyclomaltodextrin glucanotransferase

organism: Bacillus circulans

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context and applied mutation signature F183N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F183N

enzyme: cyclomaltodextrin glucanotransferase


sequence_source: UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context

sequence_variant_note: Mutation signature E264A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant E264A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F259N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context and applied mutation signature F183S with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F183S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context and applied mutation signature F183S/F259N with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F183S/F259N


sequence_source: UniProtKB:P43379 FASTA


sequence_variant_note: Mutation signature K232L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant K232L


sequence_variant_note: Mutation signature K232Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant K232Q


organism: Paenibacillus macerans

substrate_name: sophoricoside

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

proof_lines: mutant enzyme A156V/L174P/A166Y, at pH 6.0 and 50°C

substrate: sophoricoside


organism: Shouchella lehensis

substrate_name: soluble starch

sequence_source: UniProtKB:A0A060M208 direct REST lookup on 2026-06-04

proof_lines:
free enzyme, pH 6, 60°C
crosslinked enzyme, pH 6, 60°C

substrate: soluble starch


substrate_name: alpha-Cyclodextrin

sequence_source: UniProtKB:P26827 direct REST lookup on 2026-06-04

substrate: alpha-Cyclodextrin


substrate_name: beta-Cyclodextrin

substrate: beta-Cyclodextrin


substrate_name: alpha-Methyl-D-glucopyranoside

substrate: alpha-Methyl-D-glucopyranoside


substrate_name: Glucose

substrate: Glucose


substrate_name: Maltose

substrate: Maltose


substrate_name: Starch

substrate: Starch


organism: Niallia circulans

substrate_name: maltodextrin

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature A599V/Y633A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

substrate: maltodextrin


sequence_source: UniProtKB:P43379 direct REST lookup 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47W with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47W, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_source: UniProtKB:O52766 direct REST lookup 2026-06-04

proof_lines: wild-type, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47V with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47V, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47F, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47L with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47L, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_source: UniProtKB:P04830 direct REST lookup 2026-06-04

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


sequence_source: UniProtKB:A0A097CPM3 plus mature-chain L600E reconstruction

sequence_variant_note: Mutation signature L600E matches the mutant residue at offset +7 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain L600Y reconstruction and applied mutation signature L600Y with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain L600R reconstruction and applied mutation signature L600R with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A097CPM3 REST sequence

proof_lines:
wild-type, pH 6.5, 50°C
wild type enzyme, at pH 6.5 and 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain A599N/Y633A reconstruction and applied mutation signature A599N/Y633A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain A599N reconstruction and applied mutation signature A599N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain A599V reconstruction and applied mutation signature A599V to reconstruct the assayed variant sequence.


substrate_name: starch

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant A230V/H140Q

substrate: starch


sequence_source: UniProt:P43379 FASTA direct exact-accession lookup on 2026-06-04


organism: Geobacillus stearothermophilus

substrate_name: maltose, soluble starch

sequence_source: UniProtKB P31797 direct lookup; variant mapping from selected BRENDA note and UniProt mature-chain offset

sequence_variant_note: Mutation signature L277A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: maltose, soluble starch


substrate_name: soluble starch, maltose

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.

substrate: soluble starch, maltose


sequence_variant_note: Resolved canonical sequence from UniProtKB P31797 direct lookup; variant mapping from selected BRENDA note and UniProt mature-chain offset and applied mutation signature L277M/G282A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P30920 direct lookup; variant mapping from selected BRENDA note and UniProt mature-chain offset

sequence_variant_note: Mutation signature A230V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant A230V


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant K232E


sequence_variant_note: Mutation signature F283L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant F283L


sequence_source: UniProtKB P30920 direct lookup

proof_lines: pH 6.0, 60°C, beta-cyclization activity, wild-type enzyme


sequence_variant_note: Mutation signature H140Q matches the mutant residue at offset +13 and the reference residue at offset -8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant H140Q


enzyme_display_name: succinyl-CoA:acetate CoA-transferase

organism: Acetobacter aceti

substrate_name: acetate

proof_lines: kcat is 280 sec(-1) with acetate. kcat is 201 sec(-1) with succinyl-CoA. kcat is 75 sec(-1) with acetyl-CoA. kcat is 36.5 sec(-1) with acetoacetate. kcat is 70.9 sec(-1) with succinate.

enzyme: succinyl-CoA:acetate CoA-transferase

substrate: acetate


proof_lines: kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as


organism: Pseudomonas fluorescens

proof_lines: kcat is 9 sec(-1) with ethyl acetate as substrate. kcat is 25 sec(-1) with methyl acetate as substrate. kcat is 100 sec(-1) with peracetic acid as substrate. kcat is 0.12 sec(-1) with acetic acid as substrate. kcat is 0.094 sec(-1) with hyd


substrate_name: phenyl acetate (PA)

proof_lines: kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(

substrate: phenyl acetate (PA)


enzyme_display_name: trehalose-phosphatase

organism: Brugia malayi

substrate_name: trehalose 6-phosphate

proof_lines: kcat is 24 sec(-1) for trehalose 6-phosphate.

enzyme: trehalose-phosphatase

substrate: trehalose 6-phosphate


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

substrate_name: Tre6P (at pH 8 and 50 degrees Celsius)

proof_lines: kcat is 10 sec(-1) and 0.8 sec(-1) for Tre6P and pNPP, respectively (at pH 8 and 50 degrees Celsius).

substrate: Tre6P (at pH 8 and 50 degrees Celsius)


enzyme_display_name: pyridoxal phosphatase

organism: Escherichia coli (strain K12)

substrate_name: PLP (in the presence of Mg(2+) and at pH 9)

proof_lines: kcat is 1.0 sec(-1) with PLP as substrate (PubMed:16990279). kcat is 1.7 sec(-1) with PLP as substrate (PubMed:39133002). kcat is 0.1 sec(-1) with PNP as substrate (PubMed:39133002). kcat is 5.3 sec(-1) with Fru1,6bisP as substrate (PubMed:

enzyme: pyridoxal phosphatase


substrate_name: PNP

proof_lines: kcat is 1.9 sec(-1) with PNP as substrate (PubMed:39133002). kcat is 2.4 sec(-1) with PLP as substrate (PubMed:39133002). kcat is 12 sec(-1) with PLP as substrate (PubMed:16990279). kcat is 14 sec(-1) with beta-glucose 6-phosphate as substr

substrate: PNP


organism: Homo sapiens

proof_lines: kcat is 1.52 sec(-1) for the dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 1.25 sec(-1) for the dephosphorylation of pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 0.45 sec(-1)


organism: Mus musculus

substrate_name: pyridoxal 5'-phosphate

proof_lines: kcat varies between 1.5 and 2.0 sec(-1) for the dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 22 degrees Celsius).

substrate: pyridoxal 5'-phosphate


enzyme_display_name: lacto-N-biosidase

organism: Aquimarina sp. (strain TRL1)

substrate_name: pNP-LNB

proof_lines: kcat is 2.16 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 3.9 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).

enzyme: lacto-N-biosidase

substrate: pNP-LNB


organism: Bifidobacterium bifidum (strain DSM 20082 / JCM 1254 / BCRC 11844 / KCTC 3440 / E319f (Variant a))

substrate_name: lacto-N-tetraose

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

proof_lines: kcat is 41.1 sec(-1) with lacto-N-tetraose as substrate (PubMed:23479733). kcat is 89 sec(-1) with chromogenic LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as substrate (PubMed:18469123).

substrate: lacto-N-tetraose


organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)

proof_lines: kcat is 113 sec(-1) with lacto-N-tetraose (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) as substrate. kcat is 96.1 sec(-1) with LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as chromogenic substrate. kcat is 39.4 sec


organism: Paludibaculum fermentans

substrate_name: pNP-LacNAc

assay_conditions_summary: pH 6; 318.15 K; buffer pH 6

column_label: Table 6 (Kinetic parameters k cat, K M, K i and k cat/K M of AquiGH20, PadiGH20, PafeGH20, PlbaGH20 and TrdeGH20, determined at their respective optimal conditions of pH and temperature using pNP-LNB and pNP-LacNAc as substrates), enzyme row 'PafeGH20'. pNP-LacNAc column group: column 'k cat' = 17.1, column 'K M' = 1408, column 'K i' = 736, column 'k cat/K M' = 1.30 x 10^4. pNP-LNB column group of the same row: column 'k cat' = en dash, column 'K M' = en dash, column 'k cat/K M' = 6.66 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 6 cell 17.1 s-1; the printed unit is already s^-1, so no conversion is applied and the exported value is 17.1 s^(-1). Km: printed Table 6 cell 1408 uM; 1408 / 1000 = 1.408, so the exported value is 1.408 mM. kcat/Km: printed Table 6 cell 1.30 x 10^4 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.30 x 10^4 x 0.001 = 13.0 s^-1 mM^-1; the export row stores no kcat_over_km value, so this converted figure is kept as typed provenance only and no ratio metric is written.

raw_value_unit_evidence: Table 6, enzyme row 'PafeGH20', pNP-LacNAc column group: k cat = 17.1 s-1; K M = 1408 uM; K i = 736 uM; printed k cat/K M = 1.30 x 10^4 s-1 M-1. The pNP-LNB column group of the same row prints an en dash for k cat and for K M and 6.66 x 10^2 s-1 M-1 for k cat/K M.

row_label: Table 6, enzyme row 'PafeGH20', pNP-LacNAc column group (k cat, K M, K i, k cat/K M)

table_label: Table 6: Kinetic parameters k cat (s-1), K M (uM), K i (uM), and k cat/K M (s-1 M-1) of AquiGH20, PadiGH20, PafeGH20, PlbaGH20, and TrdeGH20 (Chembiochem 2025, 26(2), e202400710)

substrate: pNP-LacNAc


organism: Parabacteroides distasonis

proof_lines: kcat is 14.6 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 23.6 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).


organism: Planctomycetales bacterium (strain ZRK34)

proof_lines: kcat is 4.6 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 8.9 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).


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

proof_lines: kcat is 0.45 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 3.3 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Streptomyces sp. (strain SirexAA-E / ActE)

substrate_name: L.digitata soluble laminarin (at pH 6 and 40 degrees Celsius)

proof_lines: kcat is 138 sec(-1) with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius).

enzyme: glucan 1,3-beta-glucosidase


organism: Bacillus circulans

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 and applied mutation signature F259S with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F259S


organism: Bacillus sp. 1011

substrate_name: rutin

proof_lines:
pH 6, 60°C
ring opening reaction, pH 6, 60°C

substrate: rutin


organism: Bacillus sp. (in: firmicutes)

substrate_name: soluble starch

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

proof_lines: mutant NS182G, pH 6.0, 60°C, calculated as production of beta-cyclodextrin

substrate: soluble starch


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5U9V9 and applied mutation signature S182E with inferred residue-numbering offset +29 to reconstruct the assayed variant sequence.

proof_lines: mutant S182E, pH 6.0, 60°C, calculated as production of beta-cyclodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5U9V9 and applied mutation signature N28R with inferred residue-numbering offset +29 to reconstruct the assayed variant sequence.

proof_lines: mutant N28R, pH 6.0, 60°C, calculated as production of beta-cyclodextrin


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

proof_lines: wild-type, pH 6.0, 60°C, calculated as production of beta-cyclodextrin


organism: Bacillus sp. N-227

substrate_name: soluble corn starch

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q197W1 and applied mutation signature Y127F to reconstruct the assayed variant sequence.

substrate: soluble corn starch


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q197W1 and applied mutation signature D355R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q197W1 direct accession sequence

assay_conditions_summary: pH 6; 333.15 K; buffer pH 6


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q197W1 direct accession sequence plus PMID 28597161 mutation reconstruction and applied mutation signature R254F to reconstruct the assayed variant sequence.


organism: Geobacillus stearothermophilus

km_unit: g liter^-1

kcat_over_km_unit: liters s^-1 g^-1

sequence_source: UniProtKB:P31797 direct accession sequence

assay_conditions_summary: pH 5.5; 323.15 K; buffer 50 mM sodium phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277M with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


substrate_name: maltose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature G282A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

substrate: maltose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277F with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277T with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277F/G282A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


enzyme_display_name: angiotensin-converting enzyme 2

substrate_name: angiotensin I

proof_lines: kcat is 0.034 sec(-1) with angiotensin I as substrate. kcat is 3.5 sec(-1) with angiotensin II as substrate. kcat is 13 sec(-1) with apelin-13 as substrate. kcat is 62 sec(-1) with [des-Arg(9)]-bradykinin as substrate. kcat is 26 sec(-1) wi

enzyme: angiotensin-converting enzyme 2

substrate: angiotensin I


enzyme_display_name: beta-ureidopropionase

substrate_name: N-carbamoyl-beta-alanine

proof_lines: kcat is 0.47 sec(-1) with N-carbamoyl-beta-alanine as substrate.

enzyme: beta-ureidopropionase

substrate: N-carbamoyl-beta-alanine


enzyme_display_name: biuret amidohydrolase

organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841)

substrate_name: biuret

enzyme: biuret amidohydrolase

substrate: biuret


enzyme_display_name: 8-oxo-dGTP diphosphatase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 6.9 sec(-1) with 8-oxo-dGTP as substrate measured by the Fiske-SubbaRow assay. kcat is 5.5 sec(-1) with 8-oxo-dGTP as substrate measured by the Pi sensor assay. kcat is 11.2 sec(-1) with 8-oxo-GTP as substrate.

enzyme: 8-oxo-dGTP diphosphatase


enzyme_display_name: 2-hydroxy-dATP diphosphatase

organism: Danio rerio

substrate_name: 8-oxo-dGTP (at pH 7.5)

proof_lines: kcat is 5.4 sec(-1) with 8-oxo-dGTP as substrate (at pH 7.5) (PubMed:26862114). kcat is 12.0 sec(-1) with 2-oxo-dATP as substrate (at pH 7.5) (PubMed:26862114). kcat is 7.6 sec(-1) with dGTP as substrate (at pH 7.5) (PubMed:26862114). Shows

enzyme: 2-hydroxy-dATP diphosphatase

substrate: 8-oxo-dGTP (at pH 7.5)


organism: Homo sapiens

substrate_name: 2-oxo-dATP (at 30 degrees Celsius and pH 8.0)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 13.9 sec(-1) with 2-oxo-dATP as substrate (at 30 degrees Celsius and pH 8.0) (PubMed:10373420). kcat is 4.7 sec(-1) with 2-oxo-dATP as substrate (at 30 degrees Celsius and pH 7.2) (PubMed:10373420). kcat is 4.7 sec(-1) with 2-oxo-AT


enzyme_display_name: soluble epoxide hydrolase

substrate_name: trans-1,3-diphenylpropene oxide

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column R287Q; printed row 'KM (uM)' = 10.1; printed row 'kcat (s^-1)' = 0.076; printed row 'kcat/KM (s^-1 uM^-1)' = 0.008. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.076 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.076 s^(-1). Km: printed Table 1 cell 10.1 in a row headed KM (uM); 1 uM is 1/1000 mM, so 10.1 / 1000 = 0.0101 mM. kcat/Km: printed Table 1 cell 0.008 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.008 x 1000 = 8.0 s^(-1)*mM^(-1). The exported values are kcat 0.076 s^(-1), Km 0.0101 mM and kcat_over_km 7.524752475247525 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column R287Q: KM = 10.1 uM; kcat = 0.076 s-1; printed kcat/KM = 0.008 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.

table_label: Table 1: Kinetic parameters for WT and four sEH polymorphs (Journal of Lipid Research, Volume 55, 2014). The table prints one substrate block per assayed substrate, each block printing the rows KM, kcat and kcat/KM, and one value column per assayed enzyme form.

enzyme: soluble epoxide hydrolase

substrate: trans-1,3-diphenylpropene oxide


substrate_name: AttoPhos

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R103C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column R103C; printed row 'KM (uM)' = 14; printed row 'kcat (10^-3 s^-1)' = 5.0; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 0.36. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 5.0 x 10^-3 = 0.005 s^(-1). Km: printed Table 1 cell 14 in a row headed KM (uM); 1 uM is 1/1000 mM, so 14 / 1000 = 0.014 mM. kcat/Km: printed Table 1 cell 0.36 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.36 x 10^-3 x 1000 = 0.36 s^(-1)*mM^(-1). The exported values are kcat 0.005 s^(-1), Km 0.014 mM and kcat_over_km 0.35714285714285715 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column R103C: KM = 14 uM; kcat = 5.0 x 10^-3 s-1; printed kcat/KM = 0.36 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.

substrate: AttoPhos


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature C154Y to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column C154Y; printed row 'KM (uM)' = 7.4; printed row 'kcat (10^-3 s^-1)' = 27.0; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 3.63. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 27.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 27.0 x 10^-3 = 0.027 s^(-1). Km: printed Table 1 cell 7.4 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7.4 / 1000 = 0.0074 mM. kcat/Km: printed Table 1 cell 3.63 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.63 x 10^-3 x 1000 = 3.63 s^(-1)*mM^(-1). The exported values are kcat 0.027 s^(-1), Km 0.0074 mM and kcat_over_km 3.6486486486486482 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column C154Y: KM = 7.4 uM; kcat = 27.0 x 10^-3 s-1; printed kcat/KM = 3.63 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


substrate_name: 1-myristoyl-sn-glycerol 3-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme R287Q, at pH 7.4 and 30°C
mutant enzyme R287Q, at pH 7.4 and 37°C

substrate: 1-myristoyl-sn-glycerol 3-phosphate


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column C154Y; printed row 'KM (uM)' = 4.0; printed row 'kcat (s^-1)' = 2.55; printed row 'kcat/KM (s^-1 uM^-1)' = 0.64. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.55 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.55 s^(-1). Km: printed Table 1 cell 4.0 in a row headed KM (uM); 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM. kcat/Km: printed Table 1 cell 0.64 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.64 x 1000 = 640.0 s^(-1)*mM^(-1). The exported values are kcat 2.55 s^(-1), Km 0.004 mM and kcat_over_km 637.4999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column C154Y: KM = 4.0 uM; kcat = 2.55 s-1; printed kcat/KM = 0.64 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


substrate_name: 14,15-epoxyeicosatrienoic acid

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column C154Y; printed row 'KM (uM)' = 9.2; printed row 'kcat (s^-1)' = 15.0; printed row 'kcat/KM (s^-1 uM^-1)' = 1.6. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15.0 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 15.0 s^(-1). Km: printed Table 1 cell 9.2 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9.2 / 1000 = 0.0092 mM. kcat/Km: printed Table 1 cell 1.6 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.6 x 1000 = 1600.0 s^(-1)*mM^(-1). The exported values are kcat 15.0 s^(-1), Km 0.0092 mM and kcat_over_km 1630.4347826086957 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column C154Y: KM = 9.2 uM; kcat = 15.0 s-1; printed kcat/KM = 1.6 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.

substrate: 14,15-epoxyeicosatrienoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 and applied mutation signature K55R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature K55R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column K55R; printed row 'KM (uM)' = 5.8; printed row 'kcat (s^-1)' = 1.72; printed row 'kcat/KM (s^-1 uM^-1)' = 0.30. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.72 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.72 s^(-1). Km: printed Table 1 cell 5.8 in a row headed KM (uM); 1 uM is 1/1000 mM, so 5.8 / 1000 = 0.0058 mM. kcat/Km: printed Table 1 cell 0.30 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.30 x 1000 = 300.0 s^(-1)*mM^(-1). The exported values are kcat 1.72 s^(-1), Km 0.0058 mM and kcat_over_km 296.55172413793105 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column K55R: KM = 5.8 uM; kcat = 1.72 s-1; printed kcat/KM = 0.30 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column R287Q; printed row 'KM (uM)' = 9; printed row 'kcat (s^-1)' = 0.44; printed row 'kcat/KM (s^-1 uM^-1)' = 0.05. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.44 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.44 s^(-1). Km: printed Table 1 cell 9 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9 / 1000 = 0.009 mM. kcat/Km: printed Table 1 cell 0.05 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.05 x 1000 = 50.0 s^(-1)*mM^(-1). The exported values are kcat 0.44 s^(-1), Km 0.009 mM and kcat_over_km 48.88888888888889 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column R287Q: KM = 9 uM; kcat = 0.44 s-1; printed kcat/KM = 0.05 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


sequence_source: UniProtKB reviewed accession P34913 direct REST check

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column WT; printed row 'KM (uM)' = 9.7; printed row 'kcat (10^-3 s^-1)' = 13.1; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 1.35. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 13.1 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 13.1 x 10^-3 = 0.0131 s^(-1). Km: printed Table 1 cell 9.7 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9.7 / 1000 = 0.0097 mM. kcat/Km: printed Table 1 cell 1.35 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.35 x 10^-3 x 1000 = 1.35 s^(-1)*mM^(-1). The exported values are kcat 0.0131 s^(-1), Km 0.0097 mM and kcat_over_km 1.3505154639175259 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column WT: KM = 9.7 uM; kcat = 13.1 x 10^-3 s-1; printed kcat/KM = 1.35 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


proof_lines:
wild type enzyme, at pH 7.4 and 30°C
wild type enzyme, at pH 7.4 and 37°C


organism: Mus musculus

substrate_name: 2-Benzyl-3-phenyloxirane; H2O

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

sequence_source: UniProtKB reviewed accession P34914 direct REST check

source_databases_merged: sabio_rk brenda skid

substrate: 2-Benzyl-3-phenyloxirane; H2O


organism: Mycobacterium tuberculosis

substrate_name: Styrene oxide; H2O

sequence_source: UniProtKB reviewed accession O33283 direct REST check

substrate: Styrene oxide; H2O


organism: Rattus norvegicus

substrate_name: trans-Stilbene oxide

sequence_source: UniProtKB reviewed accession P80299 direct REST check

substrate: trans-Stilbene oxide


substrate_name: H2O; trans-Stilbene oxide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P80299 plus direct W540L reconstruction from canonical residue W540 and applied mutation signature W540L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant fusion protein W540L

substrate: H2O; trans-Stilbene oxide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P80299 plus direct H332Q reconstruction from canonical residue H332 and applied mutation signature H332Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant fusion protein H332Q


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q42566 canonical sequence retrieved 2026-06-04

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


organism: Aspergillus niger

substrate_name: H2O; p-Nitrostyrene oxide

sequence_source: UniProtKB:Q9UR30 canonical sequence retrieved 2026-06-04

substrate: H2O; p-Nitrostyrene oxide


substrate_name: p-Nitrostyrene oxide; H2O

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q9UR30 canonical sequence retrieved 2026-06-04 and applied mutation signature D348E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant D348E

substrate: p-Nitrostyrene oxide; H2O


organism: Caenorhabditis elegans

sequence_source: UniProtKB:G5EBI4 canonical sequence retrieved 2026-06-04


sequence_source: UniProtKB:G5EDL5 canonical sequence retrieved 2026-06-04


sequence_source: UniProtKB direct accession lookup G5EBI4 on 2026-06-04


sequence_source: UniProtKB direct accession lookup G5EDL5 on 2026-06-04


substrate_name: (S)-styrene oxide

sequence_source: UniProtKB direct accession lookup Q5PRC6 on 2026-06-04; mutation coordinate check performed against the returned canonical sequence

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

proof_lines: mutant enzyme E88R/T102A/M368I/K398E/G412D, at pH 6.0 and 10°C

substrate: (S)-styrene oxide


substrate_name: (R)-styrene oxide

sequence_source: UniProtKB direct accession lookup Q5PRC6 on 2026-06-04

substrate: (R)-styrene oxide


organism: Gallus gallus

sequence_source: UniProtKB direct accession lookup Q45QT1 on 2026-06-04

proof_lines: pH 7.4, 30°C, purified recombinant enzyme


organism: Glycine max

substrate_name: H2O; 9,10-Epoxystearic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup O49857 on 2026-06-04; Y255F reconstructed from the returned canonical sequence and applied mutation signature Y255F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant Y255F

substrate: H2O; 9,10-Epoxystearic acid


substrate_name: 9,10-Epoxystearic acid; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup O49857 on 2026-06-04; Y175S reconstructed from the returned canonical sequence and applied mutation signature Y175S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant Y175S

substrate: 9,10-Epoxystearic acid; H2O


sequence_source: UniProtKB direct accession lookup O49857 on 2026-06-04

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


sequence_source: UniProtKB:P80299 direct accession lookup


substrate_name: trans-Stilbene oxide; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P80299 direct accession lookup plus W334F reconstruction and applied mutation signature W334F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant fusion protein W334F

substrate: trans-Stilbene oxide; H2O


organism: Solanum tuberosum

sequence_source: UniProtKB:Q41413 direct accession lookup


organism: Strongylocentrotus purpuratus

sequence_source: UniProtKB:B2MWN2 direct accession lookup


organism: Trichoderma reesei

sequence_source: UniProtKB:G0R7E2 direct accession lookup


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


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for O49857 on 2026-06-04; variant reconstructed from selected SABIO-RK Y255H note. and applied mutation signature Y255H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant Y255H


sequence_source: UniProt REST direct accession check for P07099 on 2026-06-04.


sequence_source: UniProt REST direct accession check for P34913 on 2026-06-04.

assay_conditions_summary: pH 7.4; 310.15 K; buffer sodium phosphate

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

proof_lines: pH 7, temperature not specified in the publication


sequence_source: UniProt REST direct accession check for Q9H6B9 on 2026-06-04.


substrate_name: Epoxy Fluor 7

sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected BRENDA R287E note. and applied mutation signature R287E to reconstruct the assayed variant sequence.

substrate: Epoxy Fluor 7


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected BRENDA E254R note. and applied mutation signature E254R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected BRENDA E254R/R287E note. and applied mutation signature E254R/R287E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E254R/R287E, at pH 7.4 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected OED R103C note. and applied mutation signature R103C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P34913 FASTA and JSON fetched via UniProt REST on 2026-06-04; PMID 24771868 / PMCID PMC4031944 checked for human soluble epoxide hydrolase SNP and substrate context.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column WT; printed row 'KM (uM)' = 7; printed row 'kcat (s^-1)' = 5.0; printed row 'kcat/KM (s^-1 uM^-1)' = 0.71. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 5.0 s^(-1). Km: printed Table 1 cell 7 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7 / 1000 = 0.007 mM. kcat/Km: printed Table 1 cell 0.71 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.71 x 1000 = 710.0 s^(-1)*mM^(-1). The exported values are kcat 5.0 s^(-1), Km 0.007 mM and kcat_over_km 714.2857142857142 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column WT: KM = 7 uM; kcat = 5.0 s-1; printed kcat/KM = 0.71 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R103C to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 5.0 x 10^-3 = 0.005 s^(-1). Km: printed Table 1 cell 14 in a row headed KM (uM); 1 uM is 1/1000 mM, so 14 / 1000 = 0.014 mM. kcat/Km: printed Table 1 cell 0.36 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.36 x 10^-3 x 1000 = 0.36 s^(-1)*mM^(-1). The exported values are kcat 2.1 s^(-1), Km 0.0059 mM; this export row carries no kcat_over_km field.

row_label: Table 1, substrate block Attophos, enzyme column R103C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature C154Y to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15.0 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 15.0 s^(-1). Km: printed Table 1 cell 9.2 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9.2 / 1000 = 0.0092 mM. kcat/Km: printed Table 1 cell 1.6 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.6 x 1000 = 1600.0 s^(-1)*mM^(-1). The exported values are kcat 15.0 s^(-1), Km 0.004 mM; this export row carries no kcat_over_km field.

row_label: Table 1, substrate block 14,15-EET, enzyme column C154Y


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column R287Q; printed row 'KM (uM)' = 17; printed row 'kcat (10^-3 s^-1)' = 1.0; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 0.06. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 1.0 x 10^-3 = 0.001 s^(-1). Km: printed Table 1 cell 17 in a row headed KM (uM); 1 uM is 1/1000 mM, so 17 / 1000 = 0.017 mM. kcat/Km: printed Table 1 cell 0.06 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.06 x 10^-3 x 1000 = 0.06 s^(-1)*mM^(-1). The exported values are kcat 0.001 s^(-1), Km 0.017 mM and kcat_over_km 0.058823529411764705 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column R287Q: KM = 17 uM; kcat = 1.0 x 10^-3 s-1; printed kcat/KM = 0.06 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column R103C; printed row 'KM (uM)' = 5.9; printed row 'kcat (s^-1)' = 0.76; printed row 'kcat/KM (s^-1 uM^-1)' = 0.13. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.76 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.76 s^(-1). Km: printed Table 1 cell 5.9 in a row headed KM (uM); 1 uM is 1/1000 mM, so 5.9 / 1000 = 0.0059 mM. kcat/Km: printed Table 1 cell 0.13 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.13 x 1000 = 130.0 s^(-1)*mM^(-1). The exported values are kcat 0.76 s^(-1), Km 0.0059 mM and kcat_over_km 128.8135593220339 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column R103C: KM = 5.9 uM; kcat = 0.76 s-1; printed kcat/KM = 0.13 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature K55R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column K55R; printed row 'KM (uM)' = 7.4; printed row 'kcat (s^-1)' = 7.5; printed row 'kcat/KM (s^-1 uM^-1)' = 1.0. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.5 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.5 s^(-1). Km: printed Table 1 cell 7.4 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7.4 / 1000 = 0.0074 mM. kcat/Km: printed Table 1 cell 1.0 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.0 x 1000 = 1000.0 s^(-1)*mM^(-1). The exported values are kcat 7.5 s^(-1), Km 0.0074 mM and kcat_over_km 1013.5135135135134 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column K55R: KM = 7.4 uM; kcat = 7.5 s-1; printed kcat/KM = 1.0 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column K55R; printed row 'KM (uM)' = 7.4; printed row 'kcat (10^-3 s^-1)' = 18.2; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 2.5. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 18.2 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 18.2 x 10^-3 = 0.0182 s^(-1). Km: printed Table 1 cell 7.4 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7.4 / 1000 = 0.0074 mM. kcat/Km: printed Table 1 cell 2.5 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.5 x 10^-3 x 1000 = 2.5 s^(-1)*mM^(-1). The exported values are kcat 0.0182 s^(-1), Km 0.0074 mM and kcat_over_km 2.4594594594594597 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column K55R: KM = 7.4 uM; kcat = 18.2 x 10^-3 s-1; printed kcat/KM = 2.5 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column WT; printed row 'KM (uM)' = 3.3; printed row 'kcat (s^-1)' = 0.99; printed row 'kcat/KM (s^-1 uM^-1)' = 0.30. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.99 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.99 s^(-1). Km: printed Table 1 cell 3.3 in a row headed KM (uM); 1 uM is 1/1000 mM, so 3.3 / 1000 = 0.0033 mM. kcat/Km: printed Table 1 cell 0.30 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.30 x 1000 = 300.0 s^(-1)*mM^(-1). The exported values are kcat 0.99 s^(-1), Km 0.0033 mM and kcat_over_km 300.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column WT: KM = 3.3 uM; kcat = 0.99 s-1; printed kcat/KM = 0.30 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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


substrate_name: p-nitrophenyl phosphate

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

substrate: p-nitrophenyl phosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: Leu-p-nitroanilide

substrate: Leu-p-nitroanilide


enzyme_display_name: nitrile hydratase

organism: Rhodococcus erythropolis

substrate_name: methacrylonitrile (at pH 7.5)

smiles: CC(=C)C#N

proof_lines: Measured for the whole complex (PubMed:16636455, PubMed:20221653). kcat is 55000 min(-1) with methacrylonitrile as substrate (at pH 7.5) (PubMed:16636455). kcat is 96000 min(-1) with methacrylonitrile as substrate (at pH 7.5 and 20 degrees

enzyme: nitrile hydratase

substrate: methacrylonitrile (at pH 7.5)


enzyme_display_name: tyrosine 3-monooxygenase

organism: Bombyx mori

substrate_name: L-tyrosine

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

enzyme: tyrosine 3-monooxygenase

substrate: L-tyrosine