organism: Homo sapiens

substrate_name: ADP-ribose

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:W0NWJ0 by N110A substitution; UniProt and PMC checked 2026-06-06 and applied mutation signature N110A to reconstruct the assayed variant sequence.

substrate: ADP-ribose


source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:W0NWJ0 by F37A and L196A substitutions; UniProt and PMC checked 2026-06-06 and applied mutation signature F37A/L196A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

data_origin: experimental

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:W0NWJ0 by H111N substitution; UniProt and PMC checked 2026-06-06 and applied mutation signature H111N to reconstruct the assayed variant sequence.

mutation_type: substitution


enzyme_display_name: alpha,alpha-trehalase

organism: Apis mellifera

substrate_name: trehalose

source_db: brenda

kcat_over_km_display: Not reported

mutation_signature: Unknown

sequence_source: UniProtKB REST A8J4S9

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

assay_conditions_summary: pH 6.6; 308.15 K; buffer 50 mM sodium phosphate

proof_lines: recombinant enzyme, in 50 mM sodium phosphate buffer, pH 6.6, with 0.01% Triton X-100, at 35°C

enzyme: alpha,alpha-trehalase

substrate: trehalose

source: brenda


organism: Bombyx mori

substrate_name: alpha,alpha-trehalose

kcat_display: Not reported

sequence_source: UniProtKB REST P32358

assay_conditions_summary: pH 7

substrate: alpha,alpha-trehalose


sequence_source: UniProtKB REST Q3MV18


organism: Escherichia coli

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

sequence_source: UniProtKB REST P13482

assay_conditions_summary: pH 5.5; 310.15 K; buffer sodium maleate

proof_lines: at 37°C in sodium maleate buffer (75 mM, pH 5.5)

source_databases_merged: brenda skid


organism: Helicoverpa armigera

sequence_source: UniProtKB REST A0A0F6PB63

proof_lines: pH and temperature not specified in the publication


sequence_source: UniProtKB REST A0A0F6PAZ3


organism: Metacordyceps brittlebankisoides

substrate_name: H2O; alpha,alpha-Trehalose

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

sequence_source: UniProtKB REST Q6UDD8

substrate: H2O; alpha,alpha-Trehalose


substrate_name: alpha,alpha-Trehalose

substrate: alpha,alpha-Trehalose


organism: Spodoptera frugiperda

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


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q0ZIF5 and applied mutation signature R169A to reconstruct the assayed variant sequence.


organism: Tenebrio molitor


organism: Thermoplasma volcanium

proof_lines: pH 3.7, 30°C, recombinant truncated mutant K8A


proof_lines: pH 3.7, 30°C, recombinant truncated mutant Y9A


proof_lines: pH 3.7, 30°C, recombinant truncated mutant V7A/Y9A


proof_lines: pH 3.7, 30°C, recombinant truncated mutant V7A


proof_lines: pH 3.7, 30°C, recombinant truncated mutant Y9S


substrate_name: CDP-choline

sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature H111N to reconstruct the assayed variant sequence.

substrate: CDP-choline


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature F37Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature L196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature F37A/L196F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature R43A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature H111A to reconstruct the assayed variant sequence.


substrate_name: cyclic ADP-ribose

sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 FASTA/REST direct check; variant reconstructed from canonical sequence and applied mutation signature F37A/L196F/C253A to reconstruct the assayed variant sequence.

substrate: cyclic ADP-ribose


verification_status: verified

sequence_source: UniProtKB W0NWJ0 FASTA/REST direct check

column_label: PMID 25692488 Table 1. Kinetic parameters of human ADPRibase-Mn and mutants.; row Wild type / 2´,3´-cAMP (Table 1, third substrate line of the "Wild type" block); columns kcat (s-1), Km (µM) and kcat/Km (M-1s-1); printed cells kcat 60 ± 13 s-1, Km 2400 ± 300 µM, kcat/Km 25000 ± 6000 M-1s-1. The exported kcat/Km equals the printed kcat/Km cell after unit conversion (25000 M-1s-1 = 25 s^-1 mM^-1) and equals the quotient of this same row's two printed cells (60.0 s^-1 / 2.4 mM = 25.0); the two agree exactly, so no correction is claimed.

normalized_value_unit_evidence: metric: kcat; normalized value: 60.0 s^-1; metric: Km; normalized value: 2.4 mM; metric: kcat/Km; normalized value: 25.0 s^-1 mM^-1; assay condition: 37 C (310.15 K), pH 7.5, 5 mM MnCl2 standard conditions as printed in Materials and Methods ("Under the standard conditions, the assays were conducted at 37°C, pH 7.5, and in the presence of 5 mM MnCl2, unless otherwise stated."); recombinant human ADPRibase-Mn; kcat and Km from saturation analysis of initial-rate assays

raw_value_unit_evidence: Table row as printed: kcat 60 ± 13 s-1; Km 2400 ± 300 µM; kcat/Km 25000 ± 6000 M-1s-1.

status: verified


organism: Metarhizium anisopliae

substrate_name: alpha,alpha-Trehalose; H2O

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

sequence_source: UniProtKB REST Q6UDE0, checked 2026-06-06

substrate: alpha,alpha-Trehalose; H2O


sequence_source: UniProtKB REST Q9HDE9, checked 2026-06-06


sequence_source: UniProtKB REST Q0ZIF5, checked 2026-06-06


sequence_source: UniProtKB REST B5ATV4, checked 2026-06-06


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0ZIF5 canonical sequence with R222A/R287A reconstructed, checked 2026-06-06 and applied mutation signature R222A/R287A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q0ZIF5 canonical sequence with D322A reconstructed, checked 2026-06-06 and applied mutation signature D322A to reconstruct the assayed variant sequence.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature N110A to reconstruct the assayed variant sequence.

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature L196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature F210A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature C253A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature F37A/L196F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction and applied mutation signature F37A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB W0NWJ0 canonical sequence plus PMID 25692488 mutant reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature L196A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature F37A/L196F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature F37A/L196A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature F37Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature R43A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA checked 2026-06-06; variant reconstructed from selected mutation_signature and applied mutation signature F210A to reconstruct the assayed variant sequence.


enzyme_display_name: serine O-acetyltransferase

organism: Entamoeba histolytica

substrate_name: L-serine

sequence_source: GenBank AB023954.1 CDS translation / protein BAA82868.1; UniProt Q9U8X2 maps the same sequence to Entamoeba histolytica serine O-acetyltransferase EC 2.3.1.30.

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

assay_conditions_summary: pH 8

proof_lines: wild-type isozyme SAT1, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine

enzyme: serine O-acetyltransferase

substrate: L-serine


sequence_variant_note: Resolved canonical sequence from Reconstructed from GenBank AB023954.1 CDS translation / protein BAA82868.1 by applying H208S; UniProt Q9U8X2 supplies the canonical Entamoeba histolytica SAT1 sequence. and applied mutation signature H208S to reconstruct the assayed variant sequence.

proof_lines: isozyme SAT1 mutant H208S, pH 8.0, temperature not specified in the publication, in presence of 10 mM L-cysteine


organism: Arabidopsis thaliana

substrate_name: acetyl-CoA

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

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
chloroplastidic isozyme SAT-p
mitochondrial isozyme SAT-m
cytosolic isozyme SAT-c

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:W0NWJ0 and applied mutation signature N110A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:W0NWJ0 and applied mutation signature F37Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:W0NWJ0 and applied mutation signature F210A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_UniProtKB:W0NWJ0 and applied mutation signature F37A/L196F/C253A to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

substrate_name: ADP

substrate: ADP


enzyme_display_name: (R)-mandelonitrile lyase

organism: Chamberlinius hualienensis

substrate_name: benzaldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB accession A0A0H5BR52 REST/FASTA direct check, fetched 2026-06-06 and applied mutation signature Y40F with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

enzyme: (R)-mandelonitrile lyase

substrate: benzaldehyde


substrate_name: (R)-mandelonitrile

sequence_variant_note: Resolved canonical sequence from UniProtKB accession A0A0H5BR52 REST/FASTA direct check, fetched 2026-06-06 and applied mutation signature D56E with inferred residue-numbering offset +21 to reconstruct the assayed variant sequence.

substrate: (R)-mandelonitrile


organism: Davallia tyermanii

sequence_source: UniProtKB accession A0A1C9V3R0 REST/FASTA direct check, fetched 2026-06-06

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

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication, enzyme form DtHNL2


sequence_source: UniProtKB accession A0A1C9V3R6 REST/FASTA direct check, fetched 2026-06-06

proof_lines: pH 5.0, temperature not specified in the publication, enzyme form DtHNL4


sequence_source: UniProtKB accession A0A1C9V3R4 REST/FASTA direct check, fetched 2026-06-06

proof_lines: pH 5.0, temperature not specified in the publication, enzyme form DtHNL3


sequence_source: UniProtKB accession A0A1C9V3S9 REST/FASTA direct check, fetched 2026-06-06

proof_lines: pH 5.0, temperature not specified in the publication, enzyme form DtHNL1


organism: Eriobotrya japonica

substrate_name: Mandelonitrile

sequence_source: UniProtKB accession B7VF77 REST/FASTA direct check, fetched 2026-06-06

substrate: Mandelonitrile


organism: Granulicella tundricola

sequence_source: UniProtKB accession E8WYN5 REST/FASTA direct check, fetched 2026-06-06


substrate_name: ADPribose; H2O

sequence_source: UniProtKB:Q5M886 exact accession lookup

proof_lines: recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 0.1 mM MnCl2, at 37°C

proof_lines: recombinant enzyme, in 50 mM Tris-HCl (pH 7.5), 01 mM MnCl2, at 37°C

substrate: ADPribose; H2O


sequence_source: UniProtKB:Q9LFT6 exact accession lookup


sequence_source: UniProtKB:A0A0H5BR52 exact accession lookup


proof_lines:
pH 4.2, 22°C
Raw SKiD Env: Temp=22°C, pH=4.2


organism: Manihot esculenta


organism: Passiflora edulis

sequence_variant_note: Resolved canonical sequence from UniProt A0A1L7NZN4 canonical sequence with N105Q reconstructed on the mature PeHNL numbering used by PMID 27914120. and applied mutation signature N105Q with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt A0A1L7NZN4 canonical sequence with N105Q reconstructed from the selected BRENDA note and PMID 27914120 context. and applied mutation signature N105Q with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 4, hydroxynitrile lyase mutant N105Q expressed in Pichia pastoris


sequence_source: UniProt A0A1L7NZN4 canonical sequence.


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

mutation_type: deletion

assay_conditions_summary: pH 4

proof_lines: recombinant C-terminally truncated enzyme HNLDELTA112, at pH 4.0 and 25Â°C


proof_lines: recombinant C-terminally truncated enzyme HNLDELTA109, at pH 4.0 and 25Â°C


proof_lines: native enzyme from yellow cultivar, at pH 4.0 and 25Â°C

proof_lines: recombinant enzyme from yellow cultivar, at pH 4.0 and 25Â°C

proof_lines: recombinant enzyme from purple cultivar, at pH 4.0 and 25Â°C


proof_lines: recombinant C-terminally truncated enzyme HNLDELTA105, at pH 4.0 and 25Â°C


sequence_source: UniProt REST/FASTA direct lookup for A0A0H5BR52


sequence_source: UniProt REST/FASTA direct lookup for A0A0H5BR52 plus PMID 32679618 mature-sequence offset

sequence_variant_note: Mutation signature K117R matches the mutant residue at offset +11 and the reference residue at offset -11; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Mutation signature Y103F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: aromatic-amino-acid transaminase

organism: Bacillus subtilis

substrate_name: L-tyrosine

proof_lines:
pH 7.6, 37°C, isoenzyme B2
pH 7.5, 37°C
pH 7.6, 37°C, isoenzyme A

enzyme: aromatic-amino-acid transaminase

substrate: L-tyrosine


proof_lines: recombinant C-terminally truncated enzyme HNLDELTA117, at pH 4.0 and 25Â°C


proof_lines: recombinant C-terminally truncated enzyme HNLDELTA107, at pH 4.0 and 25Â°C


organism: Prunus mume

sequence_source: UniProtKB:B9X0I1 direct REST lookup on 2026-06-06

proof_lines:
pH 5.0, 25°C
Raw SKiD Env: Temp=25°C, pH=5


sequence_source: UniProtKB:B9X0I2 direct REST lookup on 2026-06-06


organism: Prunus serotina

sequence_source: UniProtKB:O82784 direct REST lookup on 2026-06-06


sequence_source: UniProtKB:O82435 direct REST lookup on 2026-06-06


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA, direct lookup 2026-06-06; variant reconstructed by applying F37A and L196F. and applied mutation signature F37A/L196F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA, direct lookup 2026-06-06; variant reconstructed by applying F37A. and applied mutation signature F37A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB W0NWJ0 canonical FASTA, direct lookup 2026-06-06.

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 W0NWJ0 canonical FASTA, direct lookup 2026-06-06; variant reconstructed by applying C253A. and applied mutation signature C253A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA, direct lookup 2026-06-06; variant reconstructed by applying H111N. and applied mutation signature H111N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA, direct lookup 2026-06-06; variant reconstructed by applying H111A. and applied mutation signature H111A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB W0NWJ0 canonical FASTA, direct lookup 2026-06-06; variant reconstructed by applying L196A. and applied mutation signature L196A to reconstruct the assayed variant sequence.


organism: Unknown

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


organism: Thermococcus litoralis

substrate_name: L-phenylalanine

proof_lines:
pH 7.6, 78°C, isoenzyme ArAT-I
pH 7.6, 78°C, isoenzyme ArAT-II

substrate: L-phenylalanine


enzyme_display_name: homocitrate synthase

organism: Schizosaccharomyces pombe

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed accession Q9Y823 FASTA, direct check on 2026-06-06

assay_conditions_summary: cofactor CoA

enzyme: homocitrate synthase

source: skid


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB reviewed accession Q4J989 FASTA, direct check on 2026-06-06

assay_conditions_summary: pH 7.5; 338.15 K; cofactor CoA


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

assay_conditions_summary: pH 7.6; 338.15 K; cofactor CoA


enzyme_display_name: riboflavin kinase

substrate_name: riboflavin

assay_conditions_summary: cofactor FMN

enzyme: riboflavin kinase

substrate: riboflavin


enzyme_display_name: choline kinase

organism: Caenorhabditis elegans

substrate_name: choline

assay_conditions_summary: pH 10; 310.15 K; cofactor ATP

proof_lines:
dimer
isozyme CKA-2, pH 10.0, 37°C
isozyme CKB-2, pH 10.0, 37°C

enzyme: choline kinase

substrate: choline


organism: Mus musculus

proof_lines:
isozyme CK-alpha
isozyme CK-beta
isozyme CK-alpha1/beta


substrate_name: N-Monomethylethanolamine

assay_conditions_summary: cofactor ATP

substrate: N-Monomethylethanolamine


substrate_name: acetyl-CoA; 2-oxoglutarate

sequence_source: UniProtKB REST:Q4J989 canonical sequence checked 2026-06-06

substrate: acetyl-CoA; 2-oxoglutarate


organism: Thermus thermophilus

sequence_source: UniProtKB REST:O87198 canonical sequence checked 2026-06-06

smiles: O=C(O)CCC(=O)C(=O)O

assay_conditions_summary: pH 7.5; 323.15 K; cofactor CoA


substrate_name: Acetyl-CoA

substrate: Acetyl-CoA


substrate_name: 2-Oxoglutarate; Acetyl-CoA; H2O

substrate: 2-Oxoglutarate; Acetyl-CoA; H2O


organism: Prunus dulcis

proof_lines:
pH 4.2, 25°C, isoenzyme HNL5
pH 4.2, 25°C, isoenzyme HNL2
pH 4.2, 25°C, isoenzyme HNL1


organism: Aspergillus fumigatus

sequence_source: UniProtKB REST direct lookup, accession C7C437, retrieved 2026-06-06

assay_conditions_summary: pH 7.5; 295.15 K; cofactor CoA


organism: Azotobacter vinelandii

substrate_name: Acetyl-CoA; 2-Oxoglutarate; H2O

sequence_source: UniProtKB REST direct lookup, accession P05342, retrieved 2026-06-06

substrate: Acetyl-CoA; 2-Oxoglutarate; H2O


organism: Saccharomyces cerevisiae

substrate_name: H2O; Acetyl-CoA; 2-Oxoglutarate

km_display: Not reported

ki_unit: mM

substrate: H2O; Acetyl-CoA; 2-Oxoglutarate


substrate_name: oxaloacetate

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

substrate: oxaloacetate


substrate_name: Oxaloacetate; Acetyl-CoA; H2O

substrate: Oxaloacetate; Acetyl-CoA; H2O


substrate_name: Unknown

sequence_source: UniProtKB REST direct lookup, accession Q12122, retrieved 2026-06-06

substrate: Unknown


substrate_name: acetyl-CoA

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup, accession P48570, with S385F substitution reconstructed on 2026-06-06 and applied mutation signature S385F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: alpha,alpha-trehalose

substrate: alpha,alpha-trehalose


enzyme_display_name: Homocitrate synthase, cytosolic isozyme

sequence_variant_note: Resolved canonical sequence from UniProtKB:P48570 canonical FASTA fetched 2026-06-06; reconstructed S385E after direct residue check S385=S. and applied mutation signature S385E to reconstruct the assayed variant sequence.

enzyme: Homocitrate synthase, cytosolic isozyme


sequence_source: UniProtKB:P48570 canonical FASTA fetched 2026-06-06.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48570 canonical FASTA fetched 2026-06-06; reconstructed S385L after direct residue check S385=S. and applied mutation signature S385L to reconstruct the assayed variant sequence.


enzyme_display_name: Homocitrate synthase, mitochondrial

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y823 canonical FASTA fetched 2026-06-06; reconstructed R288K after direct residue check R288=R. and applied mutation signature R288K to reconstruct the assayed variant sequence.

enzyme: Homocitrate synthase, mitochondrial


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y823 canonical FASTA fetched 2026-06-06; reconstructed D123N after direct residue check D123=D. and applied mutation signature D123N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q9Y823 canonical FASTA fetched 2026-06-06.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y823 canonical FASTA fetched 2026-06-06; reconstructed E222Q after direct residue check E222=E. and applied mutation signature E222Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y823 canonical FASTA fetched 2026-06-06; reconstructed Q364R after direct residue check Q364=Q. and applied mutation signature Q364R to reconstruct the assayed variant sequence.


organism: Bombyx mori

substrate_name: trehalose

assay_conditions_summary: pH 5.4; 310.15 K; buffer acetate

proof_lines: pH 5.4, 37°C, recombinant protein with N-terminal His-tag

proof_lines: soluble trehalase P II, inacetate buffer, pH 5.5, at 30°C

substrate: trehalose


organism: Arabidopsis thaliana

substrate_name: riboflavin (at pH 7.5)

source_db: uniprot

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

substrate: riboflavin (at pH 7.5)

source: uniprot


organism: Corynebacterium ammoniagenes

substrate_name: Mg-ATP (for riboflavin kinase activity)

substrate: Mg-ATP (for riboflavin kinase activity)


organism: Geobacillus thermodenitrificans (strain NG80-2)


substrate_name: choline (at 37 degrees Celsius and pH 10)

smiles: C[N+](C)(C)CCO

assay_conditions_summary: pH 10


assay_conditions_summary: pH 10; cofactor ATP

substrate: choline (at 37 degrees Celsius and pH 10)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ATP

substrate: ATP


organism: Apis mellifera

substrate_name: alpha,alpha-trehalose (in 0.1 M sodium phosphate pH 6.75, at 35 degrees Celsius)


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


organism: Rattus norvegicus

substrate_name: ADP-ribose

assay_conditions_summary: cofactor ADP

substrate: ADP-ribose


substrate_name: mandelonitrile

substrate: mandelonitrile


enzyme_display_name: homoserine O-acetyltransferase

organism: Bacillus cereus (strain ATCC 10987 / NRS 248)

enzyme: homoserine O-acetyltransferase


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate_name: L-homoserine (at 25 degrees Celsius and pH 7.5)

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: kcat is 92 sec(-1) with acetyl-CoA and L-homoserine as substrates (at 25 degrees Celsius and pH 7.5) (PubMed:10913262). kcat is 5 sec(-1) (PubMed:28581482).


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: acetyl-CoA (at pH 8)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: kcat is 9.34 sec(-1) with acetyl-CoA as substrate (at pH 8) (PubMed:16216079). kcat is 9.60 sec(-1) with L-homoserine as substrate (at pH 8) (PubMed:16216079). kcat is 16.1 sec(-1) with propionyl-CoA as substrate (at pH 8) (PubMed:16216079)

substrate: acetyl-CoA (at pH 8)


organism: Streptomyces lavendulae

substrate_name: L-serine (at 30 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

proof_lines: kcat is 95 min(-1) and 88 min(-1) for L-serine and L-homoserine, respectively (at 30 degrees Celsius and pH 8).


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

proof_lines: kcat is 9.49 sec(-1) with acetyl-CoA as substrate. kcat is 2.6 sec(-1) with propionyl-CoA as substrate. kcat is 0.19 sec(-1) with succinyl-CoA as substrate.


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


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

proof_lines: kcat is 92 min(-1) using 2-oxoglutarate as substrate (PubMed:12095615). kcat is 58 min(-1) using oxaloacetate as substrate (in the presence of KCl, necessary for activity) (PubMed:12095615). kcat is 41 min(-1) using 2-oxoglutarate as substr


organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)

substrate_name: riboflavin

proof_lines: kcat is 0.40 sec(-1) with riboflavin as substrate. kcat is 4.39 sec(-1) with FMN as substrate.

substrate: riboflavin


organism: Homo sapiens

substrate_name: choline

substrate: choline


proof_lines: kcat is 71 sec(-1) for trehalose (in the presence of BMH1, at pH 7.5 and 30 degrees Celsius). kcat is 6.2 sec(-1) for trehalose (in the presence of 5 mM calcium, at pH 7.5 and 30 degrees Celsius). kcat is 42 sec(-1) for trehalose (in the pr


organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

substrate_name: trehalose (at 50 degrees Celsius and pH 4.0)

assay_conditions_summary: pH 4

proof_lines: kcat is 77.0 sec(-1) at 50 degrees Celsius and pH 4.0. kcat is 102.5 sec(-1) at 60 degrees Celsius and pH 4.0.


substrate_name: trehalose (at 50 degrees Celsius and pH 3.7)

proof_lines: kcat is 1.60 sec(-1) at 50 degrees Celsius and pH 3.7. kcat is 3.43 sec(-1) at 70 degrees Celsius and pH 3.7.


organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)

substrate_name: L-homoserine

assay_conditions_summary: cofactor CoA

substrate: L-homoserine


substrate_name: acetyl-CoA


enzyme_display_name: adenine phosphoribosyltransferase

organism: Arabidopsis thaliana

substrate_name: adenine (at pH 7.4 and 37 degrees Celsius)

enzyme: adenine phosphoribosyltransferase


substrate: adenine (at pH 7.4 and 37 degrees Celsius)


substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


organism: Bos taurus

substrate_name: N-Acetylglucosamine; UDPglucose

substrate: N-Acetylglucosamine; UDPglucose


substrate_name: N-Acetylglucosamine; UDPgalactose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P08037 plus SABIO-RK R228K mutation annotation and applied mutation signature R228K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase(Enzyme) mutant R228K

substrate: N-Acetylglucosamine; UDPgalactose


substrate_name: chitotriose

substrate: chitotriose


substrate_name: UDP-alpha-D-galactose

proof_lines: recombinant wild type enzyme, at pH 7.0 and 37°C

substrate: UDP-alpha-D-galactose


substrate_name: Fetuin; UDPgalactose

substrate: Fetuin; UDPgalactose


organism: Allium cepa

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

substrate: acetyl-CoA


organism: Citrullus lanatus

substrate_name: Unknown

proof_lines:
versus L-serine
versus acetyl-CoA

substrate: Unknown


organism: Entamoeba histolytica

substrate_name: L-serine

proof_lines: 50 mM Tris-HCl, pH 8.0, 0.1 mM acetyl-CoA, 25°C

proof_lines: 50 mM Tris-HCl, pH 8.0, 1 mM L-serine, 25°C

proof_lines: competitive inhibition with L-serine but no inhibition with acetyl-CoA, 50 mM Tris-HCl, pH 8.0, 25°C

substrate: L-serine


organism: Escherichia coli

substrate_name: L-Threonine; Acetyl-CoA

substrate: L-Threonine; Acetyl-CoA


organism: Glycine max

proof_lines:
pH 8.0
versus acetyl-CoA
versus L-Ser


organism: Paracoccus denitrificans


organism: Phaseolus vulgaris


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Spinacia oleracea


organism: Staphylococcus aureus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

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


organism: Trypanosoma cruzi

sequence_source: UniProtKB Q9BKB1_TRYCR accession Q9BKB1; direct lookup showed EC 2.3.1.30 and reference PMID 11106665.

proof_lines:
versus acetyl-CoA
versus L-serine


organism: Bacillus cereus

sequence_source: UniProtKB reviewed entry Q72X44/METAA_BACC1; direct lookup showed EC 2.3.1.31, PDB 2GHR/2VDJ, and reference PMID 18216013.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: wild-type, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: wild-type, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72X44 FASTA plus PubMed 18216013 mutagenesis evidence and applied mutation signature E237A to reconstruct the assayed variant sequence.

proof_lines: E237A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: E237A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72X44 FASTA plus PubMed 18216013 mutagenesis evidence and applied mutation signature K47R to reconstruct the assayed variant sequence.

proof_lines: K47R, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: K47R, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72X44 FASTA plus PubMed 18216013 mutagenesis evidence and applied mutation signature R249M to reconstruct the assayed variant sequence.

proof_lines: R249M , 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: R249M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72X44 FASTA plus PubMed 18216013 mutagenesis evidence and applied mutation signature K47M to reconstruct the assayed variant sequence.

proof_lines: K47M, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: K47M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72X44 FASTA plus PubMed 18216013 mutagenesis evidence and applied mutation signature K163M to reconstruct the assayed variant sequence.

proof_lines: K163M, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: K163M, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q72X44 FASTA plus PubMed 18216013 mutagenesis evidence and applied mutation signature E237Q to reconstruct the assayed variant sequence.

proof_lines: E237Q, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: E237Q, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


substrate_name: UDP-galactose

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

substrate: UDP-galactose


organism: Homo sapiens

substrate_name: GlcNAc-B-S-pNP

substrate: GlcNAc-B-S-pNP


substrate_name: guanine37 in yeast tRNAAsp possessing an A36G37 sequence

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


substrate_name: guanine37 in tRNALeu

sequence_variant_note: Resolved canonical sequence from uniprot:P0A873 and applied mutation signature S88L to reconstruct the assayed variant sequence.

proof_lines:
recombinant mutant S88L, pH 8.0, 43°C
recombinant mutant S88L, pH 8.0, 30°C
recombinant mutant S88L, pH 8.0, 37°C

substrate: guanine37 in tRNALeu


proof_lines: recombinant wild-type enzyme, pH 8.0, 43°C

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

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


substrate_name: tRNA; S-Adenosyl-L-methionine

proof_lines:
recombinant enzyme, pH 7.3, 37°C
pH 8.0, 37°C
below 0.00123 pH 8.0, 37°C

substrate: tRNA; S-Adenosyl-L-methionine


organism: Methanocaldococcus jannaschii

substrate_name: S-Adenosyl-L-methionine; tRNA guanine

sequence_variant_note: Resolved canonical sequence from uniprot:Q58293 and applied mutation signature P267A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant P267A His-tag

substrate: S-Adenosyl-L-methionine; tRNA guanine


substrate_name: tRNA guanine; S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from uniprot:Q58293 and applied mutation signature P226A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant P226A His-tag

substrate: tRNA guanine; S-Adenosyl-L-methionine


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


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


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with source mutation signature N265H/P267A applied and applied mutation signature N265H/P267A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant N265H/P267A His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with source mutation signature N265A applied and applied mutation signature N265A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant N265A His-tag


organism: Pseudomonas aeruginosa

substrate_name: guanine37 in tRNALeu(CAG)

sequence_source: UniProtKB Q02RL6 canonical sequence

proof_lines: pH and temperature not specified in the publication

proof_lines: versus tRNA, pH 7.5, 37°C, recombinant enzyme

substrate: guanine37 in tRNALeu(CAG)


organism: Aquifex aeolicus

substrate_name: guanine37 in Haloferax volcanii tRNALeu(CAA)

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


substrate_name: S-Adenosyl-L-methionine; tRNA

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

substrate: S-Adenosyl-L-methionine; tRNA


organism: Haemophilus influenzae

substrate_name: guanine37 in tRNAGlnG36U

sequence_source: RCSB PDB 4YVG/4YVH/4YVI/4YVJ/4YVK SIFTS mapping to UniProt P43912; direct UniProt P43912 canonical sequence

proof_lines: pH 8.0, temperature not specified in the publication

substrate: guanine37 in tRNAGlnG36U


sequence_source: Direct UniProt EC 2.1.1.228 + Methanocaldococcus jannaschii lookup; reviewed accession Q58293

proof_lines: kcat in steady-state phase turnover, pH and temperature not specified in the publication

proof_lines: pH not specified in the publication, 55°C


organism: Streptococcus pneumoniae

substrate_name: S-adenosyl-L-homocysteine

substrate: S-adenosyl-L-homocysteine


substrate_name: acetyl-CoA

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

proof_lines: E250A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: E250A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


enzyme_display_name: sterol esterase

organism: Streptomyces sp.

substrate_name: cholesteryl acetate

sequence_source: UniProtKB Q2AAT6 REST/FASTA fetched 2026-06-06

enzyme: sterol esterase

substrate: cholesteryl acetate


substrate_name: cholesteryl oleate

substrate: cholesteryl oleate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with worker-applied mutation reconstruction and applied mutation signature N265H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant N265H His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with worker-applied mutation reconstruction and applied mutation signature G205A/G207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant G205A/G207A His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with worker-applied mutation reconstruction and applied mutation signature N265Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant N265Q His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with worker-applied mutation reconstruction and applied mutation signature N265Q/P267A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant N265Q/P267A His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with worker-applied mutation reconstruction and applied mutation signature D223A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant D223A His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB Q58293 canonical sequence with worker-applied mutation reconstruction and applied mutation signature N225A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tRNA (guanine37-N1)-methyltransferase(Enzyme) mutant N225A His-tag


substrate_name: p-Nitrophenyl palmitate

sequence_source: UniProtKB Q2AAT6 and NCBI Protein BAE80307.1 direct accession lookup

substrate: p-Nitrophenyl palmitate


substrate_name: Cholesteryl linoleate

substrate: Cholesteryl linoleate


substrate_name: cholesteryl stearate

substrate: cholesteryl stearate


substrate_name: H2O; Cholesteryl linoleate

substrate: H2O; Cholesteryl linoleate


substrate_name: Cholesteryl myristate

substrate: Cholesteryl myristate


substrate_name: p-Nitrophenyl laurate

substrate: p-Nitrophenyl laurate


substrate_name: p-Nitrophenyl myristate

substrate: p-Nitrophenyl myristate


substrate_name: cholesteryl palmitate

substrate: cholesteryl palmitate


enzyme_display_name: aromatic-L-amino-acid decarboxylase

substrate_name: L-Dopa

sequence_variant_note: Resolved canonical sequence from UniProtKB P20711 canonical sequence reconstructed as G102S on 2026-06-06 and applied mutation signature G102S to reconstruct the assayed variant sequence.

enzyme: aromatic-L-amino-acid decarboxylase

substrate: L-Dopa


sequence_variant_note: Resolved canonical sequence from UniProtKB P20711 canonical sequence reconstructed as F309L on 2026-06-06 and applied mutation signature F309L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatic-L-amino-acid decarboxylase(Enzyme) mutant F309L, C-terminal His-tag


sequence_source: UniProtKB P20711 canonical sequence reconstructed as G102S on 2026-06-06

proof_lines: SABIO-RK modifier species: aromatic-L-amino-acid decarboxylase(Enzyme) mutant G102S, C-terminal His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB P20711 canonical sequence reconstructed as A275T on 2026-06-06 and applied mutation signature A275T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P20711 canonical sequence reconstructed as S147R on 2026-06-06 and applied mutation signature S147R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatic-L-amino-acid decarboxylase(Enzyme) mutant S147R, C-terminal His-tag


organism: Levilactobacillus brevis

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


substrate_name: L-tyrosine

proof_lines: mutant H241N, pH not specified in the publication, temperature not specified in the publication

substrate: L-tyrosine


proof_lines: mutant H98M, pH not specified in the publication, temperature not specified in the publication


substrate_name: Unknown

sequence_source: UniProtKB direct REST lookup, accession P19835

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

substrate: Unknown


substrate_name: Cholesteryl oleate; H2O

sequence_source: UniProtKB direct REST lookup, accession P38571

substrate: Cholesteryl oleate; H2O


organism: Mus musculus

sequence_source: UniProtKB direct REST lookup, accession Q64285


organism: Streptomyces avermitilis

substrate_name: cholesteryl linoleate

sequence_source: UniProtKB direct REST lookup, accession Q82JC7

substrate: cholesteryl linoleate


organism: Bacillus atrophaeus

substrate_name: L-Tryptophan

sequence_source: UniProtKB direct REST lookup, accession I0DFJ0

substrate: L-Tryptophan


substrate_name: L-Phenylalanine

substrate: L-Phenylalanine


proof_lines:
30°C, pH 7
37°C, pH 7
45°C, pH 7


organism: Capsicum annuum

sequence_source: UniProtKB direct REST lookup, accession C0LIF1


organism: Catharanthus roseus

substrate_name: L-tryptophan

substrate: L-tryptophan


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P17770 and applied mutation signature Y348F to reconstruct the assayed variant sequence.


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

proof_lines: SABIO-RK modifier species: aromatic-L-amino-acid decarboxylase(Enzyme) mutant A275T, C-terminal His-tag


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P20711 and applied mutation signature F309L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot:P20711 and applied mutation signature S147R to reconstruct the assayed variant sequence.


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

proof_lines: decarboxylation reaction, pH and temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid


sequence_source: UniProtKB REST O88533

assay_conditions_summary: pH 7.2; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer, pH 7.2, 0.1 mM pargyline, 0.17 mM ascorbic acid, 0.1 mM EDTA, 1 mM beta-mercaptoethanol, 0.01 mMM pyridoxal 5-phosphate and 0.5 mM L-Dopa, at 30°C


organism: Pseudomonas putida

sequence_source: UniProtKB REST Q88JU5


proof_lines:
pH 8., 30°C
Raw SKiD Env: Temp=30°C, pH=8


organism: Rattus norvegicus

sequence_source: UniProtKB REST P14173


organism: Solanum lycopersicum

sequence_source: UniProtKB REST Q1KSC6


organism: Sus scrofa

sequence_source: UniProtKB REST P80041


substrate_name: L-Dopa; 5-Hydroxy-L-tryptophan

substrate: L-Dopa; 5-Hydroxy-L-tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y332F to reconstruct the assayed variant sequence.

proof_lines: Y332F DDC mutant, reaction in 50 mM Hepes, pH 7.5, at 25°C causes the production of ammonia and 3,4-dihydroxyphenylacetaldehyde along with the consumption of molecular oxygen in a 1:2 molar ratio


substrate_name: L-Dopa; 5-hydroxy-L-tryptophan

proof_lines: wild-type enzyme, the data of initial velocity for decarboxylation of L-dopa versus substrate concentration curiously exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.

proof_lines: wild-type enzyme, the data of initial velocity for decarboxylation of 5-hydroxy-L-tryptophan versus substrate concentration exhibit a substrate-inhibition pattern that requires a modified version of the Michaelis-Menten equation.

substrate: L-Dopa; 5-hydroxy-L-tryptophan


substrate_name: crotonyl-CoA

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

substrate: crotonyl-CoA


organism: Paenibacillus polymyxa

substrate_name: L-homoserine

substrate: L-homoserine


organism: Saccharomyces cerevisiae

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Schizosaccharomyces pombe

assay_conditions_summary: pH 8; 294.15 K; cofactor CoA


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


organism: Thermotoga maritima

substrate_name: succinyl-CoA

substrate: succinyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature S165A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row S165A, varying 2-OG column group; column Km 2-OG (mM) = 0.536; column kcat varying 2-OG (min^-1) = 160; column Kcat/Km (min^-1 mM^-1) = 298.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.536 mM; the printed Km column of this experiment is already in mM, so no unit conversion applies and the value is 0.536 mM. kcat: printed Table 2 cell 160 min^-1; dividing that per-minute cell by 60 gives 2.67 s^-1 at the 2-decimal precision in which this row's own 2-OG source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 298 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 298 / 60 = 4.966666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row S165A, varying 2-OG column group: Km 2-OG (mM) = 0.536; kcat varying 2-OG (min^-1) = 160; printed Kcat/Km (min^-1 mM^-1) = 298.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature T197A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row T197A, varying 2-OG column group; column Km 2-OG (mM) = 0.341; column kcat varying 2-OG (min^-1) = 11.9; column Kcat/Km (min^-1 mM^-1) = 34.9.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.341 mM; the printed Km column of this experiment is already in mM, so no unit conversion applies and the value is 0.341 mM. kcat: printed Table 2 cell 11.9 min^-1; dividing that per-minute cell by 60 gives 0.2 s^-1 at the 1-decimal precision in which this row's own 2-OG source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 34.9 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 34.9 / 60 = 0.5816666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row T197A, varying 2-OG column group: Km 2-OG (mM) = 0.341; kcat varying 2-OG (min^-1) = 11.9; printed Kcat/Km (min^-1 mM^-1) = 34.9.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature Q47A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row Q47A, varying 2-OG column group; column Km 2-OG (mM) = 4.94; column kcat varying 2-OG (min^-1) = 33.5; column Kcat/Km (min^-1 mM^-1) = 6.78.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.94 mM; the printed Km column of this experiment is already in mM, so no unit conversion applies and the value is 4.94 mM. kcat: printed Table 2 cell 33.5 min^-1; dividing that per-minute cell by 60 gives 0.56 s^-1 at the 2-decimal precision in which this row's own 2-OG source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 6.78 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 6.78 / 60 = 0.113 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row Q47A, varying 2-OG column group: Km 2-OG (mM) = 4.94; kcat varying 2-OG (min^-1) = 33.5; printed Kcat/Km (min^-1 mM^-1) = 6.78.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature E74Q to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row E74Q, varying AcCoA column group; column Km AcCoA (uM) = 30.7; column kcat varying AcCoA (min^-1) = 44.5; column kcat/Km (min^-1 uM^-1) = 1.45.

normalized_value_unit_evidence: Km: printed Table 2 cell 30.7 uM; 30.7 / 1000 = 0.0307 mM. kcat: printed Table 2 cell 44.5 min^-1; dividing that per-minute cell by 60 gives 0.74 s^-1 at the 2-decimal precision in which this row's own AcCoA source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 1.45 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 1.45 x 1000 / 60 = 24.166666666666668 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row E74Q, varying AcCoA column group: Km AcCoA (uM) = 30.7; kcat varying AcCoA (min^-1) = 44.5; printed kcat/Km (min^-1 uM^-1) = 1.45.


sequence_source: UniProtKB Q9Y823 reviewed entry plus RCSB/PDBe PDB 3IVS mapping to Q9Y823; variant sequence reconstructed locally from the checked canonical residue where applicable.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row WT, varying 2-OG column group; column Km 2-OG (mM) = 0.159; column kcat varying 2-OG (min^-1) = 308; column Kcat/Km (min^-1 mM^-1) = 1940.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.159 mM; the printed Km column of this experiment is already in mM, so no unit conversion applies and the value is 0.159 mM. kcat: printed Table 2 cell 308 min^-1; dividing that per-minute cell by 60 gives 5.13 s^-1 at the 2-decimal precision in which this row's own 2-OG source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 1940 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 1940 / 60 = 32.333333333333336 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row WT, varying 2-OG column group: Km 2-OG (mM) = 0.159; kcat varying 2-OG (min^-1) = 308; printed Kcat/Km (min^-1 mM^-1) = 1940.


organism: Thermus thermophilus

proof_lines: competitive inhibition mode, in 50 mM HEPES, pH 7.5, at 25°C


organism: Azotobacter vinelandii


organism: Candida albicans

proof_lines:
isoform Lys21p, at pH 7.5 and 22°C
isoform Lys22p, at pH 7.5 and 22°C


organism: Candida maltosa


organism: Penicillium chrysogenum


proof_lines: Kii, varied substrate acetyl-CoA, fixed substrate: 5 mM 2-oxoglutarate


organism: Bacillus cereus

proof_lines: S192A, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: S192A, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


proof_lines: E237D, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: E237D, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM acetyl-CoA, 25°C


proof_lines: E111G, 50 mM potassium phosphate buffer, pH 7.5, 2 mM L-homoserine, 25°C

proof_lines: E111G, 50 mM potassium phosphate buffer, pH 7.5, 0.5 mM succinyl-CoA, 25°C


organism: [Brevibacterium] flavum


assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: about, pH 8.0, 37°C, N-terminus His-tagged enzyme


organism: Cryptococcus neoformans

proof_lines: Ki value of competitive inhibition of acetyl-CoA

proof_lines: Ki value of noncompetitive inhibition of L-homoserine


organism: Catharanthus roseus

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


organism: Drosophila melanogaster

substrate_name: L-dopa

substrate: L-dopa


organism: Lophophora williamsii

substrate_name: L-tyrosine (at pH 7.5 and 30 degrees Celsius)


organism: Oryza sativa subsp. japonica

substrate_name: tryptophan

substrate: tryptophan


organism: Sus scrofa


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48570 canonical LYS20/YDL182W sequence with reviewed residue-position check; E155A reconstructed during this review. and applied mutation signature E155A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P48570 canonical LYS20/YDL182W sequence with reviewed residue-position check; Y320F reconstructed during this review. and applied mutation signature Y320F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature H103A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row H103A, varying 2-OG column group; column Km 2-OG (mM) = 3.56; column kcat varying 2-OG (min^-1) = 18.2; column Kcat/Km (min^-1 mM^-1) = 5.11.

normalized_value_unit_evidence: Km: printed Table 2 cell 3.56 mM; the printed Km column of this experiment is already in mM, so no unit conversion applies and the value is 3.56 mM. kcat: printed Table 2 cell 18.2 min^-1; dividing that per-minute cell by 60 gives 0.3 s^-1 at the 1-decimal precision in which this row's own 2-OG source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 5.11 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 5.11 / 60 = 0.08516666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row H103A, varying 2-OG column group: Km 2-OG (mM) = 3.56; kcat varying 2-OG (min^-1) = 18.2; printed Kcat/Km (min^-1 mM^-1) = 5.11.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature Y332F to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row Y332F, varying 2-OG column group; column Km 2-OG (mM) = 0.461; column kcat varying 2-OG (min^-1) = 20.7; column Kcat/Km (min^-1 mM^-1) = 44.9.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.461 mM; the printed Km column of this experiment is already in mM, so no unit conversion applies and the value is 0.461 mM. kcat: printed Table 2 cell 20.7 min^-1; dividing that per-minute cell by 60 gives 0.35 s^-1 at the 2-decimal precision in which this row's own 2-OG source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 44.9 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 44.9 / 60 = 0.7483333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row Y332F, varying 2-OG column group: Km 2-OG (mM) = 0.461; kcat varying 2-OG (min^-1) = 20.7; printed Kcat/Km (min^-1 mM^-1) = 44.9.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9Y823 canonical lys4/SPBC1105.02c sequence with reviewed residue-position check; R163K reconstructed during this review. and applied mutation signature R163K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9Y823 and applied mutation signature T197S to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic analysis of WT SpHCS and its active site mutants (J. Biol. Chem. 2009, 284(51):35769-35780); printed column heads Km AcCoA (uM) | kcat varying AcCoA (min^-1) | kcat/Km (min^-1 uM^-1) | Km 2-OG (mM) | kcat varying 2-OG (min^-1) | Kcat/Km (min^-1 mM^-1). Table 2, enzyme row T197S, varying AcCoA column group; column Km AcCoA (uM) = 6.00; column kcat varying AcCoA (min^-1) = 124; column kcat/Km (min^-1 uM^-1) = 20.6.

normalized_value_unit_evidence: Km: printed Table 2 cell 6.00 uM; 6.00 / 1000 = 0.006 mM. kcat: printed Table 2 cell 124 min^-1; dividing that per-minute cell by 60 gives 2.07 s^-1 at the 2-decimal precision in which this row's own AcCoA source record already renders the same cell, and computed_metric_note sets out the unrounded quotient in full. kcat/Km: printed Table 2 cell 20.6 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 20.6 x 1000 / 60 = 343.33333333333337 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, enzyme row T197S, varying AcCoA column group: Km AcCoA (uM) = 6.00; kcat varying AcCoA (min^-1) = 124; printed kcat/Km (min^-1 uM^-1) = 20.6.


sequence_source: UniProtKB:O87198; RCSB 2ZTJ/3A9I; PMID:19996101

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


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

proof_lines: H72L mutant, N-terminal His8 tag, larger than 2


organism: Wickerhamomyces anomalus

proof_lines: enzyme from S-(beta-aminoethyl)-L-cysteine resistant mutant strain


proof_lines:
competitive against 2-oxoglutarate
competitive against acetyl-CoA


organism: Bos taurus

substrate_name: UDP-galactose

sequence_source: UniProtKB:P08037; RCSB 1YRO; PMID:15736931

proof_lines: cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, wild-type enzyme

proof_lines: cosubstrate: UDP-galactose, without alpha-lactalbumin, wild-type enzyme

proof_lines: cosubstrate: UDP-glucose, without alpha-lactalbumin, wild-type enzyme

substrate: UDP-galactose


proof_lines: cosubstrate: N-acetylglucosamine, without alpha-lactalbumin, mutant enzyme R228K

proof_lines: cosubstrate: UDP-galactose, without alpha-lactalbumin, mutant enzyme R228K

proof_lines: cosubstrate: UDP-glucose, without alpha-lactalbumin, mutant enzyme R228K


substrate_name: N-acetylglucosamine

assay_conditions_summary: pH 7

substrate: N-acetylglucosamine


organism: Helicobacter pylori

substrate_name: UDP-Gal

substrate: UDP-Gal


organism: Homo sapiens

substrate_name: UDP-xylose

assay_conditions_summary: pH 7; 310.15 K; buffer 100 mM cacodylate

proof_lines: Km above 0.003 mM, purified maltose-binding protein-beta1,4-GalT7, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C

proof_lines: purified beta1,4-GalT7, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, at 37°C

substrate: UDP-xylose


substrate_name: UDPgalactose

proof_lines: reaction with glucose, wild-type enzyme and N-deglycosylated recombinant enzyme

substrate: UDPgalactose


organism: Mus musculus


organism: Rattus norvegicus

proof_lines:
enzyme from liver
enzyme from serum
enzyme from liver microsomal membrane


substrate_name: immunoglobulin G heavy chain

substrate: immunoglobulin G heavy chain


organism: Arabidopsis thaliana

substrate_name: adenine

substrate: adenine


organism: Artemia sp.


organism: Brassica juncea

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


organism: Escherichia coli

substrate_name: DNA adenine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0AEE9 REST record checked 2026-06-06 and applied mutation signature K139A to reconstruct the assayed variant sequence.

proof_lines: using the non-preferred sequence 5-GCATAAAAGATCGTCTAAATG-3, mutant enzyme K139A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, mutant enzyme K139A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

substrate: DNA adenine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P0AEE9 REST record checked 2026-06-06 and applied mutation signature N132A to reconstruct the assayed variant sequence.

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, mutant enzyme N132A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the non-preferred sequence 5-GCATAAAAGATCGTCTAAATG-3, mutant enzyme N132A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


organism: Thermus aquaticus

substrate_name: S-Adenosyl-L-methionine; DNA adenine

sequence_source: UniProtKB reviewed P14385 REST record checked 2026-06-06

substrate: S-Adenosyl-L-methionine; DNA adenine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P14385 REST record checked 2026-06-06 and applied mutation signature Y108A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: site-specific DNA-methyltransferase (adenine-specific)(Enzyme) mutant Y108A


substrate_name: DNA adenine; S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P14385 REST record checked 2026-06-06 and applied mutation signature F196W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: site-specific DNA-methyltransferase (adenine-specific)(Enzyme) mutant F196W

substrate: DNA adenine; S-Adenosyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P14385 REST record checked 2026-06-06 and applied mutation signature F196A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: site-specific DNA-methyltransferase (adenine-specific)(Enzyme) mutant F196A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P14385 REST record checked 2026-06-06 and applied mutation signature Y108W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: site-specific DNA-methyltransferase (adenine-specific)(Enzyme) mutant Y108W


organism: Cereibacter sphaeroides

sequence_source: UniProt:P14751; direct REST accession lookup on 2026-06-06


organism: Clostridioides difficile

substrate_name: adenine in DNA

sequence_source: UniProt:Q183J3; direct REST accession lookup on 2026-06-06

substrate: adenine in DNA


sequence_source: UniProt:P0AEE8; direct REST accession lookup on 2026-06-06

proof_lines: using the DNA sequence 5-GCATAAAAGATCGTCTAAATG-3, wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the DNA sequence 5-GCATACCCGATCAAGTAAATG-3, wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt:P0AEE9; direct REST accession lookup on 2026-06-06 and applied mutation signature N126A to reconstruct the assayed variant sequence.

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, mutant enzyme N126A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt:P0AEE9; direct REST accession lookup on 2026-06-06 and applied mutation signature R95A to reconstruct the assayed variant sequence.

proof_lines: using the non-preferred sequence 5-GCATAAAAGATCGTCTAAATG-3, mutant enzyme R95A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, mutant enzyme R95A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


sequence_source: UniProt:P0AEE9; direct REST accession lookup on 2026-06-06

proof_lines: using the non-preferred sequence 5-GCATAAAAGATCGTCTAAATG-3, wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, wild type enzyme, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt:P0AEE9; direct REST accession lookup on 2026-06-06 and applied mutation signature R116A to reconstruct the assayed variant sequence.

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, mutant enzyme R116A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the non-preferred sequence 5-GCATAAAAGATCGTCTAAATG-3, mutant enzyme R116A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt:P0AEE9; direct REST accession lookup on 2026-06-06 and applied mutation signature R137A to reconstruct the assayed variant sequence.

proof_lines: using the non-preferred sequence 5-GCATAAAAGATCGTCTAAATG-3, mutant enzyme R137A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C

proof_lines: using the preferred sequence 5-GCATACCGGATCAAGTAAATG-3, mutant enzyme R137A, in 20 mM potassium phosphate, pH 7.5, 200 mM NaCl, 0.2 mM EDTA, 0.2 mg/ml bovine serum albumin, 2 mM dithiothreitol, 10% (v/v) glycerol, at 22°C


organism: Plasmodium falciparum

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


organism: Saccharolobus solfataricus

substrate_name: Unknown

substrate: Unknown


organism: Saccharomyces cerevisiae

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


enzyme_display_name: glucosylceramidase

substrate_name: glucosylceramide

sequence_source: UniProtKB REST direct lookup for P04062 on 2026-06-06

proof_lines: velaglucerase alfa, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37°C

proof_lines: imiglucerase alfa, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37°C

proof_lines: imiglucerase, in 50 mM sodium citrate, pH 6.0 with 0.75 mg/ml bovine serum albumin, at 37°C

enzyme: glucosylceramidase

substrate: glucosylceramide


substrate_name: 3-beta-D-Glucosido lithocholic acid; H2O

sequence_source: UniProtKB REST direct lookup for Q9HCG7 on 2026-06-06

proof_lines: pH and temperature not specified in the publication


organism: Paenibacillus sp.

substrate_name: p-Nitrophenyl-beta-D-glucoside

sequence_source: UniProtKB REST direct lookup for Q8GAT9 on 2026-06-06

substrate: p-Nitrophenyl-beta-D-glucoside


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8GAT9 and applied mutation signature D223G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 310.15 K; buffer 25 mM sodium phosphate

column_label: Table 1: Kinetic parameters for substrate hydrolysis by Paenibacillus GCase and its active-site mutants (Biochem. J. 2004, 378(1):141-149). Printed column heads: Enzyme; Substrate; K m (mM); k cat (s-1); k cat /K m (M-1 . s-1); K m (wt)/K m; k cat (wt)/k cat; [k cat /K m (wt)]/(k cat /K m). Table 1, enzyme row D223G, substrate DNPG; column K m (mM) = 0.15; column k cat (s-1) = 0.012; column k cat /K m (M-1 . s-1) = 79. The three relative columns K m (wt)/K m, k cat (wt)/k cat and [k cat /K m (wt)]/(k cat /K m ) print 1.1, 3.9 x 10^4 and 3.7 x 10^4 on this line and are dimensionless comparisons against the wild type. The value printed after the plus/minus sign beside each Km and kcat cell is the printed uncertainty and is not an exported metric. captured primary segment: Table 1, enzyme row D223G, substrate DNPG | construct Paenibacillus GCase D223G | conditions pH 6.5, 25 mM sodium phosphate, 37 C | Km 0.15 mM | kcat 0.012 s^-1 | kcat/Km 79 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.15 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.15 mM; the exported value is 0.15 mM. kcat: printed Table 1 cell 0.012 s^-1; s^-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.012 s^(-1); the exported value is 0.012 s^(-1). kcat/Km: printed Table 1 cell 79 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 79 / 1000 = 0.079 s^(-1)*mM^(-1); the live catalog row stores no catalytic-efficiency value and this record proposes none.

raw_value_unit_evidence: Table 1, enzyme row D223G, substrate DNPG: K m = 0.15 mM; k cat = 0.012 s^-1; printed k cat /K m = 79 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8GAT9 and applied mutation signature E411A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters for substrate hydrolysis by Paenibacillus GCase and its active-site mutants (Biochem. J. 2004, 378(1):141-149). Printed column heads: Enzyme; Substrate; K m (mM); k cat (s-1); k cat /K m (M-1 . s-1); K m (wt)/K m; k cat (wt)/k cat; [k cat /K m (wt)]/(k cat /K m). Table 1, enzyme row E411A, substrate PNPG; column K m (mM) = 0.018; column k cat (s-1) = 0.099; column k cat /K m (M-1 . s-1) = 5.5 x 10^3. The three relative columns K m (wt)/K m, k cat (wt)/k cat and [k cat /K m (wt)]/(k cat /K m ) print 15, 5.6 x 10^3 and 380 on this line and are dimensionless comparisons against the wild type. The value printed after the plus/minus sign beside each Km and kcat cell is the printed uncertainty and is not an exported metric. captured primary segment: Table 1, enzyme row E411A, substrate PNPG | construct Paenibacillus GCase E411A | conditions pH 6.5, 25 mM sodium phosphate, 37 C | Km 0.018 mM | kcat 0.099 s^-1 | kcat/Km 5.5 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.018 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.018 mM; the exported value is 0.018 mM. kcat: printed Table 1 cell 0.099 s^-1; s^-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.099 s^(-1); the exported value is 0.099 s^(-1). kcat/Km: printed Table 1 cell 5.5 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.5 x 10^3 / 1000 = 5.5 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.099 / 0.018 = 5.500000000000001 s^-1 mM^-1, which is the exported catalytic-efficiency value, and that same quotient re-expressed in the printed unit reads 5.5 x 10^3 M^-1 s^-1 at the digits the catalytic-efficiency cell prints.

raw_value_unit_evidence: Table 1, enzyme row E411A, substrate PNPG: K m = 0.018 mM; k cat = 0.099 s^-1; printed k cat /K m = 5.5 x 10^3 M^-1 s^-1.


column_label: Table 1: Kinetic parameters for substrate hydrolysis by Paenibacillus GCase and its active-site mutants (Biochem. J. 2004, 378(1):141-149). Printed column heads: Enzyme; Substrate; K m (mM); k cat (s-1); k cat /K m (M-1 . s-1); K m (wt)/K m; k cat (wt)/k cat; [k cat /K m (wt)]/(k cat /K m). Table 1, enzyme row wt, substrate DNPG; column K m (mM) = 0.16; column k cat (s-1) = 470; column k cat /K m (M-1 . s-1) = 2.9 x 10^6. The three relative columns K m (wt)/K m, k cat (wt)/k cat and [k cat /K m (wt)]/(k cat /K m ) print an en dash on this wild-type line. The value printed after the plus/minus sign beside each Km and kcat cell is the printed uncertainty and is not an exported metric. captured primary segment: Table 1, enzyme row wt, substrate DNPG | construct Paenibacillus GCase wild type | conditions pH 6.5, 25 mM sodium phosphate, 37 C | Km 0.16 mM | kcat 470 s^-1 | kcat/Km 2.9 x 10^6 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.16 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.16 mM. kcat: printed Table 1 cell 470 s^-1; s^-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 470.0 s^(-1). kcat/Km: printed Table 1 cell 2.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^6 / 1000 = 2900.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row wt, substrate DNPG: K m = 0.16 mM; k cat = 470 s^-1; printed k cat /K m = 2.9 x 10^6 M^-1 s^-1.

row_label: Table 1, enzyme row wt, substrate DNPG


column_label: Table 1: Kinetic parameters for substrate hydrolysis by Paenibacillus GCase and its active-site mutants (Biochem. J. 2004, 378(1):141-149). Printed column heads: Enzyme; Substrate; K m (mM); k cat (s-1); k cat /K m (M-1 . s-1); K m (wt)/K m; k cat (wt)/k cat; [k cat /K m (wt)]/(k cat /K m). Table 1, enzyme row D223G, substrate PNPG; column K m (mM) = 0.33; column k cat (s-1) = 0.012; column k cat /K m (M-1 . s-1) = 36. The three relative columns K m (wt)/K m, k cat (wt)/k cat and [k cat /K m (wt)]/(k cat /K m ) print 0.8, 4.6 x 10^4 and 5.8 x 10^4 on this line and are dimensionless comparisons against the wild type. The value printed after the plus/minus sign beside each Km and kcat cell is the printed uncertainty and is not an exported metric. captured primary segment: Table 1, enzyme row D223G, substrate PNPG | construct Paenibacillus GCase D223G | conditions pH 6.5, 25 mM sodium phosphate, 37 C | Km 0.33 mM | kcat 0.012 s^-1 | kcat/Km 36 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 0.33 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.33 mM; the exported value is 0.33 mM. kcat: printed Table 1 cell 0.012 s^-1; s^-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.012 s^(-1); the exported value is 0.012 s^(-1). kcat/Km: printed Table 1 cell 36 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 36 / 1000 = 0.036 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.012 / 0.33 = 0.03636363636363636 s^-1 mM^-1, which is the exported catalytic-efficiency value, and that same quotient re-expressed in the printed unit reads 36 M^-1 s^-1 at the digits the catalytic-efficiency cell prints.

raw_value_unit_evidence: Table 1, enzyme row D223G, substrate PNPG: K m = 0.33 mM; k cat = 0.012 s^-1; printed k cat /K m = 36 M^-1 s^-1.


enzyme_display_name: Glucocerebrosidase

normalized_value_unit_evidence: Km: printed Table 1 cell 0.15 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.15 mM; the exported value is 0.15 mM. kcat: printed Table 1 cell 0.012 s^-1; s^-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.012 s^(-1); the exported value is 0.012 s^(-1). kcat/Km: printed Table 1 cell 79 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 79 / 1000 = 0.079 s^(-1)*mM^(-1).

row_label: Table 1, enzyme row D223G, substrate DNPG

table_label: Table 1: Kinetic parameters for substrate hydrolysis by Paenibacillus GCase and its active-site mutants (Biochem. J. 2004, 378(1):141-149). Printed column heads: Enzyme; Substrate; K m (mM); k cat (s-1); k cat /K m (M-1 . s-1); K m (wt)/K m; k cat (wt)/k cat; [k cat /K m (wt)]/(k cat /K m).

enzyme: Glucocerebrosidase


normalized_value_unit_evidence: Km: printed Table 1 cell 0.16 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.16 mM; the exported value is 0.16 mM. kcat: printed Table 1 cell 470 s^-1; s^-1 is already the canonical s^(-1), so no unit conversion applies and the paper value is 470.0 s^(-1); the exported value is 470.0 s^(-1). kcat/Km: printed Table 1 cell 2.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^6 / 1000 = 2900.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 470.0 / 0.16 = 2937.5 s^-1 mM^-1, which is the exported catalytic-efficiency value, and that same quotient re-expressed in the printed unit reads 2.9 x 10^6 M^-1 s^-1 at the digits the catalytic-efficiency cell prints.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GAT9 and applied mutation signature E411A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucosylceramidase(Enzyme) mutant E411A His6-tagged


enzyme_display_name: Glucosylceramidase / beta-glucosidase conflict

organism: Thermoanaerobacterium xylanolyticum

substrate_name: 4-nitrophenyl beta-D-glucoside

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6BL85 and applied mutation signature R544W to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides), protein row 'R544W', substrate column value '4NP β-D-glucoside'; column 'KM (mM)' = 0.26 ± 0.011; column 'kcat (s^-1)' = 48.2 ± 0.53; column 'kcat/KM (mM^-1 s^-1)' = 186; column 'temperature optimum' = 60 °C; column 'Tm' = 76.2 °C.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.26 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.26 mM. kcat: printed Table 2 cell 48.2 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 48.2 s^(-1). kcat/Km: printed Table 2 cell 186 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell normalizes to 186.0 s^(-1)*mM^(-1). The catalog identity for this measurement carries no catalytic-efficiency field, so the printed cell is kept as paper evidence.

raw_value_unit_evidence: Table 2, protein row 'R544W', substrate '4NP β-D-glucoside': KM = 0.26 mM; kcat = 48.2 s^-1; printed kcat/KM = 186 mM^-1 s^-1.

row_label: Table 2, protein row 'R544W' with substrate '4NP β-D-glucoside'

table_label: Table 2: Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides (ACS Chem. Biol. 2016, 11, 1891-1900)

substrate: 4-nitrophenyl beta-D-glucoside


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6BL85 and applied mutation signature D508H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides), protein row 'D508H', substrate column value '4NP β-D-glucoside'; column 'KM (mM)' = 110 ± 3; column 'kcat (s^-1)' = 3.47 ± 0.17; column 'kcat/KM (mM^-1 s^-1)' = 0.031; column 'temperature optimum' = 65 °C; column 'Tm' = 66.5 °C.

normalized_value_unit_evidence: Km: printed Table 2 cell 110 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 110.0 mM. kcat: printed Table 2 cell 3.47 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 3.47 s^(-1). kcat/Km: printed Table 2 cell 0.031 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell normalizes to 0.031 s^(-1)*mM^(-1). That printed catalytic-efficiency cell is the paper's own fitted value and is the value proposed for this metric.

raw_value_unit_evidence: Table 2, protein row 'D508H', substrate '4NP β-D-glucoside': KM = 110 mM; kcat = 3.47 s^-1; printed kcat/KM = 0.031 mM^-1 s^-1.

row_label: Table 2, protein row 'D508H' with substrate '4NP β-D-glucoside'

enzyme: Glucosylceramidase / beta-glucosidase conflict


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 uniprot_rest_accession:F6BL85 and applied mutation signature R786H to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters of TxGH116 and Its Mutants for Hydrolysis of 4NP-Glycosides and Oligosaccharides), protein row 'R786H', substrate column value '4NP β-D-glucoside'; column 'KM (mM)' = 15.7 ± 0.50; column 'kcat (s^-1)' = 193 ± 2.4; column 'kcat/KM (mM^-1 s^-1)' = 12.3; column 'temperature optimum' = 70 °C; column 'Tm' = 73.9 °C.

normalized_value_unit_evidence: Km: printed Table 2 cell 15.7 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 15.7 mM. kcat: printed Table 2 cell 193 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 193.0 s^(-1). kcat/Km: printed Table 2 cell 12.3 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed cell normalizes to 12.3 s^(-1)*mM^(-1). The exported kcat_over_km 12.29299363057325 s^(-1)*mM^(-1) is the exact quotient 193 / 15.7 of the same Table 2 cells, and the printed cell is that quotient carried to the precision the paper prints.

raw_value_unit_evidence: Table 2, protein row 'R786H', substrate '4NP β-D-glucoside': KM = 15.7 mM; kcat = 193 s^-1; printed kcat/KM = 12.3 mM^-1 s^-1.

row_label: Table 2, protein row 'R786H' with substrate '4NP β-D-glucoside'


organism: Hevea brasiliensis


proof_lines:
in (HPRT+)
in Propositus (HPRT-)


organism: Leishmania donovani

substrate_name: diphosphate

sequence_source: UniProtKB:Q27679 via RCSB 1QB7/1QB8/1QCC/1QCD SIFTS alignment

proof_lines: pH 7.4, temperature not specified in the publication

substrate: diphosphate


organism: Plasmodium chabaudi


enzyme_display_name: deoxyguanosine kinase

organism: Mus musculus

substrate_name: Deoxyguanosine; ATP

sequence_source: UniProtKB direct accession lookup: Q9QX60

assay_conditions_summary: cofactor ATP

enzyme: deoxyguanosine kinase

substrate: Deoxyguanosine; ATP


organism: Mycoplasma mycoides

substrate_name: Deoxyguanosine

sequence_source: UniProtKB direct accession lookup: Q93IG4

substrate: Deoxyguanosine


organism: Staphylococcus aureus

substrate_name: ATP; Deoxyguanosine

sequence_source: UniProtKB direct accession lookup: Q0H0G8

substrate: ATP; Deoxyguanosine


organism: Xenopus laevis

substrate_name: deoxyadenosine

sequence_source: UniProtKB direct accession lookup: Q6GPW6

proof_lines: at pH 8.0, temperature not specified in the publication

substrate: deoxyadenosine


organism: Arabidopsis thaliana

sequence_source: UniProtKB direct accession lookup: F4JLJ2


substrate_name: laminaribiose

sequence_source: UniProtKB direct accession lookup: F6BL85

proof_lines: wild type enzyme without N-terminal tag, at pH 5.5 and 60°C

proof_lines: wild type enzyme with N-terminal tag, at pH 5.5 and 60°C

substrate: laminaribiose


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup: F6BL85 and applied mutation signature D508N to reconstruct the assayed variant sequence.


organism: Unknown


organism: Bacillus subtilis

substrate_name: UTP; Deoxyguanosine

sequence_source: UniProtKB:P37530 direct REST lookup 2026-06-06

substrate: UTP; Deoxyguanosine


substrate_name: CTP

substrate: CTP


substrate_name: GTP

substrate: GTP


substrate_name: ATP

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: UTP

substrate: UTP


organism: Bos taurus

sequence_source: UniProtKB:Q2KIN2 direct REST lookup 2026-06-06


organism: Dictyostelium discoideum

substrate_name: ATP; Deoxyadenosine

sequence_source: UniProtKB:Q54UT2 direct REST lookup 2026-06-06

substrate: ATP; Deoxyadenosine


organism: Escherichia phage P1

substrate_name: ssDNA

substrate: ssDNA


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)

substrate_name: S-adenosyl-L-methionine

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

substrate: S-adenosyl-L-methionine


organism: Homo sapiens

substrate_name: U2 snRNA

substrate: U2 snRNA


organism: Thermus aquaticus

substrate_name: DNA

substrate: DNA


sequence_source: UniProtKB:Q54UT2 direct lookup


substrate_name: D-2'-Deoxycarbocyclic guanosine; ATP

sequence_source: UniProtKB:Q16854 direct lookup

substrate: D-2'-Deoxycarbocyclic guanosine; ATP


organism: Lactobacillus johnsonii

substrate_name: deoxyguanosine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q74HC2 direct lookup plus D84N reconstruction from selected mutation_signature and applied mutation signature D84N to reconstruct the assayed variant sequence.

substrate: deoxyguanosine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q74HC2 direct lookup plus D84A reconstruction from selected mutation_signature and applied mutation signature D84A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q74HC2 direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q74HC2 direct lookup plus D84E reconstruction from selected mutation_signature and applied mutation signature D84E to reconstruct the assayed variant sequence.


enzyme_display_name: S-formylglutathione hydrolase

organism: Escherichia coli

substrate_name: p-Nitrophenyl acetate

sequence_source: UniProtKB P33018 canonical sequence from direct REST/FASTA check

assay_conditions_summary: pH 8; 310.15 K; buffer Tris-HCl (20 mM

column_label: Table 1: Kinetic parameters of the E. coli FrmB and YeiG with several substrates (J. Biol. Chem. 2006, 281(20):14514-14522); printed column heads Substrate or YeiG form | Km (mM) | Vmax (units/mg) | kcat (s^-1) | kcat/Km (M^-1 s^-1); Table 1, YeiG block, row 'pNP-acetate (C2)'; column Km = 0.45; column Vmax = 0.50; column kcat = 0.26; column kcat/Km = 0.57 x 10^3.

normalized_value_unit_evidence: Km: printed cell 0.45 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.45 mM. kcat: printed cell 0.26 s^-1; s^-1 is already canonical, so no unit conversion applies and the value is 0.26 s^(-1). kcat/Km: printed cell 0.57 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.57 x 10^3 / 1000 = 0.57 s^(-1)*mM^(-1). The exported kcat_over_km 0.5777777777777778 s^(-1)*mM^(-1) is the quotient 0.26 / 0.45; the paper's own printed efficiency cell for this row is 0.57 s^(-1)*mM^(-1), which is the value carried on the paper side of this record.

raw_value_unit_evidence: Table 1, YeiG block, row 'pNP-acetate (C2)': Km = 0.45 mM; Vmax = 0.50 units/mg (footnote a: Units = umol/min); kcat = 0.26 s^-1; printed kcat/Km = 0.57 x 10^3 M^-1 s^-1.

enzyme: S-formylglutathione hydrolase

substrate: p-Nitrophenyl acetate


substrate_name: H2O; 1-Naphthylacetic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB P33018 canonical sequence; D199A reconstructed by replacing canonical residue 199 D with A and applied mutation signature D199A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D199A

substrate: H2O; 1-Naphthylacetic acid


substrate_name: p-Nitrophenyl acetate; H2O

sequence_source: UniProtKB P51025 canonical sequence from direct REST/FASTA check

substrate: p-Nitrophenyl acetate; H2O


substrate_name: 1-Naphthylacetic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB P33018 canonical sequence; C26A reconstructed by replacing canonical residue 26 C with A and applied mutation signature C26A to reconstruct the assayed variant sequence.

substrate: 1-Naphthylacetic acid


sequence_source: UniProtKB P33018 canonical sequence; C26A reconstructed by replacing canonical residue 26 C with A

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG C26A


substrate_name: p-Nitrophenyl propionate

column_label: Table 1: Kinetic parameters of the E. coli FrmB and YeiG with several substrates (J. Biol. Chem. 2006, 281(20):14514-14522); printed column heads Substrate or YeiG form | Km (mM) | Vmax (units/mg) | kcat (s^-1) | kcat/Km (M^-1 s^-1); Table 1, YeiG block, row 'pNP-propionate (C3)'; column Km = 0.48; column Vmax = 0.71; column kcat = 0.37; column kcat/Km = 0.76 x 10^3.

normalized_value_unit_evidence: Km: printed cell 0.48 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.48 mM. kcat: printed cell 0.37 s^-1; s^-1 is already canonical, so no unit conversion applies and the value is 0.37 s^(-1). kcat/Km: printed cell 0.76 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.76 x 10^3 / 1000 = 0.76 s^(-1)*mM^(-1). The exported kcat_over_km 0.7708333333333334 s^(-1)*mM^(-1) is the quotient 0.37 / 0.48; the paper's own printed efficiency cell for this row is 0.76 s^(-1)*mM^(-1), which is the value carried on the paper side of this record.

raw_value_unit_evidence: Table 1, YeiG block, row 'pNP-propionate (C3)': Km = 0.48 mM; Vmax = 0.71 units/mg (footnote a: Units = umol/min); kcat = 0.37 s^-1; printed kcat/Km = 0.76 x 10^3 M^-1 s^-1.

substrate: p-Nitrophenyl propionate


substrate_name: 1-Naphthylacetic acid; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB P33018 canonical sequence; D255A reconstructed by replacing canonical residue 255 D with A and applied mutation signature D255A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D255A

substrate: 1-Naphthylacetic acid; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature D255A to reconstruct the assayed variant sequence.


substrate_name: S-Lactoylglutathione

sequence_source: UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06

column_label: Table 1: Kinetic parameters of the E. coli FrmB and YeiG with several substrates (J. Biol. Chem. 2006, 281(20):14514-14522); printed column heads Substrate or YeiG form | Km (mM) | Vmax (units/mg) | kcat (s^-1) | kcat/Km (M^-1 s^-1); Table 1, YeiG block, row 'S-Lactoylglutathione'; column Km = 0.58; column Vmax = 1.97; column kcat = 1.02; column kcat/Km = 1.75 x 10^3.

normalized_value_unit_evidence: Km: printed cell 0.58 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.58 mM. kcat: printed cell 1.02 s^-1; s^-1 is already canonical, so no unit conversion applies and the value is 1.02 s^(-1). kcat/Km: printed cell 1.75 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.75 x 10^3 / 1000 = 1.75 s^(-1)*mM^(-1). The exported kcat_over_km 1.7586206896551726 s^(-1)*mM^(-1) is the quotient 1.02 / 0.58; the paper's own printed efficiency cell for this row is 1.75 s^(-1)*mM^(-1), which is the value carried on the paper side of this record.

raw_value_unit_evidence: Table 1, YeiG block, row 'S-Lactoylglutathione': Km = 0.58 mM; Vmax = 1.97 units/mg (footnote a: Units = umol/min); kcat = 1.02 s^-1; printed kcat/Km = 1.75 x 10^3 M^-1 s^-1.

substrate: S-Lactoylglutathione


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature D80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature D199A to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D80A


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 direct FASTA/JSON lookup on 2026-06-06 and applied mutation signature C54A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P51025 direct FASTA/JSON lookup on 2026-06-06

column_label: Table 1: Kinetic parameters of the E. coli FrmB and YeiG with several substrates (J. Biol. Chem. 2006, 281(20):14514-14522); printed column heads Substrate or YeiG form | Km (mM) | Vmax (units/mg) | kcat (s^-1) | kcat/Km (M^-1 s^-1); Table 1, FrmB block, row 'S-Lactoylglutathione'; column Km = 0.60; column Vmax = 0.09; column kcat = 0.05; column kcat/Km = 0.08 x 10^3.

normalized_value_unit_evidence: Km: printed cell 0.60 mM; mM is already the canonical unit, so no unit conversion applies and the value is 0.6 mM. kcat: printed cell 0.05 s^-1; s^-1 is already canonical, so no unit conversion applies and the value is 0.05 s^(-1). kcat/Km: printed cell 0.08 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.08 x 10^3 / 1000 = 0.08 s^(-1)*mM^(-1). The exported kcat_over_km 0.08333333333333334 s^(-1)*mM^(-1) is the full-precision quotient 0.05 / 0.60 of the same two printed cells, and that quotient reads 0.08 x 10^3 M^-1 s^-1 at the precision the table prints.

raw_value_unit_evidence: Table 1, FrmB block, row 'S-Lactoylglutathione': Km = 0.60 mM; Vmax = 0.09 units/mg (footnote a: Units = umol/min); kcat = 0.05 s^-1; printed kcat/Km = 0.08 x 10^3 M^-1 s^-1.


substrate_name: S-Formylglutathione

substrate: S-Formylglutathione


sequence_source: UniProtKB reviewed accession P33018


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33018 plus SABIO-RK source mutation note D218A and applied mutation signature D218A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: S-formylglutathione hydrolase(Enzyme) mutant YeiG D218A


organism: Saccharomyces cerevisiae

substrate_name: 4-nitrophenyl acetate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P40363 plus BRENDA source mutation note C60R/W197I and applied mutation signature C60R/W197I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C60R/W197I, in 0.067 M Na/K phosphate, at pH 7.4 and 22°C

substrate: 4-nitrophenyl acetate