organism: Zinnia elegans

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

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


enzyme_display_name: peroxidase

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

enzyme: peroxidase

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

source: uniprot


organism: Armoracia rusticana

source_db: oed

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

source: oed


smiles: OO


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

mutation_type: substitution


substrate_name: Guaiacol

substrate: Guaiacol


organism: Bacillus altitudinis

substrate_name: Sinapoylcholine

substrate: Sinapoylcholine


substrate_name: sinapate

substrate: sinapate


substrate_name: H2O2; Sinapate

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

substrate: H2O2; Sinapate


organism: Bos taurus

substrate_name: N-Acetyl-L-tryptophanamide

verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

substrate: N-Acetyl-L-tryptophanamide

status: unverified


organism: Cucumis sativus

substrate_name: H2O2; 4-Methoxy-alpha-naphthol

substrate: H2O2; 4-Methoxy-alpha-naphthol


organism: Euphorbia characias


organism: Cytisus multiflorus

source_db: brenda

source: brenda


organism: Elais guineensis

substrate_name: guaiacol

substrate: guaiacol


organism: Elizabethkingia meningoseptica


organism: Escherichia coli

substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Fragaria vesca

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

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


organism: Fragaria x ananassa


organism: Glycine max


organism: Homo sapiens

substrate_name: Br-

substrate: Br-


organism: Ipomoea carnea

substrate_name: o-Dianisidine

assay_conditions_summary: pH 8

proof_lines:
at pH 8.0
at pH 7.0
at pH 5.5

substrate: o-Dianisidine


organism: Lepidium sativum

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


organism: Lupinus albus

substrate_name: H2O2; Guaiacol

substrate: H2O2; Guaiacol


organism: Momordica charantia


enzyme_display_name: arginine kinase

organism: Locusta migratoria manilensis

substrate_name: L-Arg

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

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

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

enzyme: arginine kinase

substrate: L-Arg


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


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


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


organism: Manduca sexta

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

assay_conditions_summary: 310.15 K; cofactor ADP

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


organism: Molpadia arenicola

assay_conditions_summary: cofactor ATP


organism: Musca domestica


organism: Myzostoma cirriferum

substrate_name: ATP

km_display: Not reported

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


organism: Paracentrotus lividus

substrate_name: ADP

assay_conditions_summary: pH 6.7; 298.15 K; cofactor ADP

substrate: ADP


organism: Paramecium tetraurelia

substrate_name: L-arginine

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

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

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

substrate: L-arginine


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

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


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

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


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


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


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


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


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

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


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


organism: Penaeus chinensis

substrate_name: Unknown

ki_unit: mM

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

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

substrate: Unknown


organism: Periplaneta americana

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


organism: Sabella pavonina

substrate_name: D-Arg

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP

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

substrate: D-Arg


organism: Sabellastarte spectabilis

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

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


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

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

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

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


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

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

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


organism: Mycobacterium avium

assay_conditions_summary: pH 7; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer, pH 7.0


organism: Neurospora crassa


organism: Oryza sativa

assay_conditions_summary: pH 6


organism: Ovis aries

substrate_name: SCN-

substrate: SCN-


organism: Pelargonium graveolens


organism: Persea americana

substrate_name: pyrogallol

substrate: pyrogallol


organism: Plasmodium falciparum


organism: Pleurotus ostreatus

substrate_name: sinapinic acid

substrate: sinapinic acid


organism: Prunus persica

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

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

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


organism: Pyrococcus furiosus

substrate_name: rubredoxin

substrate: rubredoxin


organism: Raphanus sativus


organism: Raphanus sativus var. niger

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


proof_lines: isoform AK2 mutant G54A, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant G54A, using L-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C

proof_lines: isoform AK2 mutant G54A, using D-arginine as cosubstrate, in 100 mM Tris/HCl (pH 8.0), at 25°C


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

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

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


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

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

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

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


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

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

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


organism: Steinernema carpocapsae

assay_conditions_summary: pH 7.5; 299.15 K; cofactor ATP


organism: Sthenoteuthis oualaniensis

assay_conditions_summary: pH 7.2; 298.15 K; cofactor ATP


organism: Sulfurovum lithotrophicum

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

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


organism: Torpedo californica

substrate_name: ADP; L-Arginine phosphate

assay_conditions_summary: cofactor ADP

substrate: ADP; L-Arginine phosphate


organism: Tribolium castaneum


organism: Trypanosoma brucei

assay_conditions_summary: pH 8.6; 303.15 K; cofactor ATP

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

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


organism: Trypanosoma cruzi


enzyme_display_name: peptide deformylase

organism: Arabidopsis thaliana

substrate_name: N-formyl-Met-Leu-Glu

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

enzyme: peptide deformylase

substrate: N-formyl-Met-Leu-Glu


organism: Sclerocarya birrea


organism: Solanum betaceum


organism: Solanum melongena


organism: Sorghum bicolor

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


organism: Streptomyces lividans


organism: Triticum aestivum

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


organism: Vigna radiata

proof_lines: pH 5.5, temperature not specified in the publication


organism: Locusta migratoria manilensis


assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

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


organism: Bacillus subtilis

substrate_name: N-formyl-Met-Ala-Ser

proof_lines:
enzyme YkrB
enzyme Def
cobalt-substituted enzyme

substrate: N-formyl-Met-Ala-Ser


organism: Borreliella burgdorferi


organism: Chlamydia trachomatis


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


organism: Escherichia coli


substrate_name: N-formyl-phenylglycinol

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

substrate: N-formyl-phenylglycinol


substrate_name: N-formylmethionylleucyl-p-nitroanilide

proof_lines: recombinant mutant E133D Co2+-bound enzyme

substrate: N-formylmethionylleucyl-p-nitroanilide


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

mutation_signature: truncated zinc deformylase truncated zinc deformylase

mutation_type: truncation

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


mutation_signature: truncated cobalt deformylase truncated cobalt deformylase


mutation_signature: truncated Zn-PDF truncated Zn-PDF


mutation_signature: truncated Co-PDF truncated Co-PDF


organism: Haemophilus influenzae

substrate_name: formyl-Met-Ala-Ser

substrate: formyl-Met-Ala-Ser


organism: Homo sapiens

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

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


organism: Legionella pneumophila

proof_lines:
Ni2+ PdB
Zn2+ PdfC
Zn2+ PdfB


organism: Mycobacterium tuberculosis

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

proof_lines: 19.7 nM calculated value for the Mycobacterium tuberculosis enzyme

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


substrate_name: formyl-Met-Ala

substrate: formyl-Met-Ala


assay_conditions_summary: pH 7.4; buffer 20 mM phosphate

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


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


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


assay_conditions_summary: pH 7.4; buffer phosphate

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


organism: Solanum lycopersicum


organism: Staphylococcus aureus

proof_lines: pH 7.0, temperature not specified in the publication


organism: Streptococcus pneumoniae


organism: Trypanosoma cruzi

mutation_type: deletion

assay_conditions_summary: pH 7.5; 310.15 K; buffer KH2PO4

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


enzyme_display_name: beta-lactamase

organism: Aeromonas sobria

substrate_name: H2O; Imipenem

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

enzyme: beta-lactamase

substrate: H2O; Imipenem


organism: Enterobacter cloacae

substrate_name: H2O; Nitrocefin

proof_lines: pH and temperature not specified in the publication

substrate: H2O; Nitrocefin


organism: Klebsiella pneumoniae

substrate_name: H2O; Benzylpenicillin

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

substrate: H2O; Benzylpenicillin


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


organism: Stenotrophomonas maltophilia

substrate_name: Cefdinir; H2O

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

substrate: Cefdinir; H2O


enzyme_display_name: methionine adenosyltransferase

organism: Methanocaldococcus jannaschii

substrate_name: L-methionine

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

assay_conditions_summary: 328.15 K; cofactor ATP

enzyme: methionine adenosyltransferase

substrate: L-methionine


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


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


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


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


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


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


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


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


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


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


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


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


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


substrate_name: ATP

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP

substrate: ATP


organism: Mus musculus

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

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


enzyme_display_name: pyruvate kinase

substrate_name: Phosphoenolpyruvate; ADP

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

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

assay_conditions_summary: pH 8; 305.15 K; cofactor ATP

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

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

source_databases_merged: sabio_rk brenda skid

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


substrate_name: phosphoenolpyruvate

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

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ADP

substrate: phosphoenolpyruvate


source_db: skid

source_license: CC BY-NC-ND 4.0

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

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

source: skid


organism: Saccharomyces cerevisiae

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

assay_conditions_summary: cofactor ATP


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


assay_conditions_summary: pH 4.5; cofactor ATP


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


organism: Bacillus subtilis

substrate_name: ATP; H2O; L-Methionine

substrate: ATP; H2O; L-Methionine


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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


organism: Catharanthus roseus


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 9; 295.15 K; cofactor ATP

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


organism: Escherichia coli

substrate_name: L-Methionine; ATP; H2O

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

substrate: L-Methionine; ATP; H2O


substrate_name: tripolyphosphate

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

assay_conditions_summary: pH 8; cofactor ATP

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

substrate: tripolyphosphate


substrate_name: L-Methionine

substrate: L-Methionine


assay_conditions_summary: pH 8; 295.15 K; cofactor ATP


assay_conditions_summary: pH 8


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

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


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

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


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

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


organism: Mycolicibacterium smegmatis

substrate_name: L-methionine; ATP

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

assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP

substrate: L-methionine; ATP


organism: Plasmodium falciparum

substrate_name: ATP; L-methionine

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

assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP

substrate: ATP; L-methionine


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


organism: Pyrococcus furiosus

source_db: brenda;skid

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

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

assay_conditions_summary: pH 8; 353.15 K; cofactor ATP

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

source_databases_merged: brenda skid

source: brenda;skid


organism: Rattus norvegicus

substrate_name: ATP; methionine

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

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

substrate: ATP; methionine


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

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


substrate_name: methionine; ATP

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

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

substrate: methionine; ATP


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


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

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


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

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


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


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


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

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


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

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


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


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


organism: Homo sapiens

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


substrate_name: S-(-)-methioninol

verification_status: corrected

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

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

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

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

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

substrate: S-(-)-methioninol

status: corrected


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

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

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


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


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

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

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

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


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

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

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


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


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


organism: Saccharolobus solfataricus

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


substrate_name: L-ethionine

substrate: L-ethionine


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


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

assay_conditions_summary: pH 8; 308.15 K; cofactor ATP


organism: Streptomyces avermitilis


organism: Thermococcus kodakarensis

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


organism: Thermus thermophilus

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

assay_conditions_summary: pH 8; 343.15 K; cofactor ATP

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


enzyme_display_name: S-adenosylmethionine synthase isoform type-2

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

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

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

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


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

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

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

enzyme: S-adenosylmethionine synthase isoform type-2


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

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

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

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


enzyme_display_name: S-adenosylmethionine synthase

organism: Leishmania donovani

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

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

enzyme: S-adenosylmethionine synthase


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

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


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

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


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

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


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

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


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

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


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

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


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

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


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

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


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

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


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


organism: Methanocaldococcus jannaschii

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

assay_conditions_summary: pH 8; 331.15 K; cofactor ATP

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


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

assay_conditions_summary: 328.15 K; cofactor ATP


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

assay_conditions_summary: cofactor ADP


organism: Trichomonas vaginalis

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


organism: Trypanosoma brucei


organism: Ustilago maydis

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


organism: Zymomonas mobilis

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


organism: Pseudomonas aeruginosa

substrate_name: H2O; Penicillin G

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

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

substrate: H2O; Penicillin G


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

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


organism: Mus musculus

substrate_name: Unknown

proof_lines:
isoenzyme II
isoenzyme I

substrate: Unknown


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


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


organism: Unknown

substrate_name: L-methionine

substrate: L-methionine


organism: Catharanthus roseus


organism: Escherichia coli (strain K12)


organism: Mammalia


organism: Saccharomyces cerevisiae


organism: Streptomyces xinghaiensis

substrate_name: ATP

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

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

substrate: ATP


organism: Trypanosoma brucei brucei


organism: Acacia koa

substrate_name: L-methionine (at 50 degrees Celsius)

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

substrate: L-methionine (at 50 degrees Celsius)


organism: Bacteroides fragilis

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

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


organism: Bos taurus

assay_conditions_summary: cofactor ATP


organism: Cryptosporidium parvum

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


organism: Escherichia coli

assay_conditions_summary: pH 8.5; 318.15 K; cofactor ATP

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


assay_conditions_summary: pH 9; 303.15 K; cofactor ATP


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


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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


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


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


organism: Felis catus


organism: Homo sapiens


proof_lines: Q113A mutant, S-adenosylmethionine synthesis


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

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


organism: Lactiplantibacillus paraplantarum

assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP


organism: Lactiplantibacillus plantarum


organism: Lathyrus oleraceus


organism: Leishmania infantum

proof_lines: noncompetitive inhibition at 0.5-5 mM ATP concentrations


organism: Limosilactobacillus fermentum


organism: Limosilactobacillus reuteri


organism: Macaca mulatta


enzyme_display_name: carbonic anhydrase

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

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

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

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

enzyme: carbonic anhydrase


organism: Methanosarcina thermophila

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


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


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


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


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


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


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


organism: Methanothermobacter thermautotrophicus

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


enzyme_display_name: GDP-D-glucose phosphorylase

organism: Caenorhabditis elegans

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

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

enzyme: GDP-D-glucose phosphorylase

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


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

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

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


substrate_name: phosphate

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

substrate: phosphate


substrate_name: GDP-alpha-D-glucose

substrate: GDP-alpha-D-glucose


enzyme_display_name: beta-glucosidase

organism: Acetivibrio thermocellus

enzyme: beta-glucosidase


organism: Agroathelia rolfsii

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


organism: Agrobacterium tumefaciens

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


organism: Alternaria alternata

substrate_name: cellobiose

substrate: cellobiose


organism: Aspergillus fumigatus


organism: Aspergillus japonicus

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


organism: Fusarium proliferatum

substrate_name: ginsenoside Rg3

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

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

substrate: ginsenoside Rg3


organism: Saccharomyces cerevisiae

substrate_name: Phosphoenolpyruvate; ADP

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

substrate: Phosphoenolpyruvate; ADP


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


assay_conditions_summary: pH 4.5; cofactor ADP


organism: Amycolatopsis methanolica

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


organism: Arabidopsis thaliana


organism: Bos taurus

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


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


organism: Chlamydia trachomatis

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


organism: Corynebacterium glutamicum

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


organism: Escherichia coli

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


organism: Homo sapiens

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

assay_conditions_summary: pH 8; 305.15 K; cofactor ATP

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

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


organism: Rattus norvegicus

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


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


organism: Ricinus communis

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


enzyme_display_name: xylulokinase

organism: Escherichia coli (strain K12)

substrate_name: D-xylulose

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

enzyme: xylulokinase

substrate: D-xylulose


organism: Klebsiella aerogenes


organism: Saccharococcus caldoxylosilyticus

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


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


organism: Scheffersomyces stipitis


organism: Toxoplasma gondii

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

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


substrate_name: D-xylulose (at pH 8)

assay_conditions_summary: pH 8

substrate: D-xylulose (at pH 8)


organism: Aspergillus niger


substrate_name: ATP; D-Xylulose

substrate: ATP; D-Xylulose


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


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


substrate_name: D-arabitol

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

substrate: D-arabitol


organism: Halorhabdus utahensis


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


substrate_name: D-Xylulose

substrate: D-Xylulose


organism: Mucor circinelloides

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP


organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


substrate_name: (Polyphosphate)n

substrate: (Polyphosphate)n


enzyme_display_name: kojibiose phosphorylase

organism: Pyrococcus sp.

enzyme: kojibiose phosphorylase


organism: Citrus maxima

substrate_name: UDP-L-rhamnose; Prunin

sequence_source: UniProtKB REST exact accession lookup: Q8GVE3

substrate: UDP-L-rhamnose; Prunin


organism: Amycolatopsis orientalis

substrate_name: UDP-L-epi-vancosamine

sequence_source: UniProtKB REST exact accession lookup: Q9AFC7

substrate: UDP-L-epi-vancosamine


substrate_name: desvancosaminyl-vancomycin

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

substrate: desvancosaminyl-vancomycin


substrate_name: dTDP-beta-L-daunosamine

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

substrate: dTDP-beta-L-daunosamine


organism: Gardenia jasminoides

substrate_name: beta-D-glucosyl crocetin

sequence_source: UniProtKB REST exact accession lookup: F8WKW8

substrate: beta-D-glucosyl crocetin


substrate_name: bis(beta-D-glucosyl) crocetin

substrate: bis(beta-D-glucosyl) crocetin


organism: Panax ginseng

substrate_name: ginsenoside C-K

sequence_source: UniProtKB REST exact accession lookup: A0A0A6ZFR4

substrate: ginsenoside C-K


substrate_name: (20S)-ginsenoside Rh2

sequence_source: UniProtKB REST exact accession lookup: A0A0A6ZFY4

substrate: (20S)-ginsenoside Rh2


enzyme_display_name: taxadiene 5alpha-hydroxylase

organism: Taxus cuspidata

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: taxadiene 5alpha-hydroxylase


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

assay_conditions_summary: cofactor NADPH


organism: Homo sapiens


substrate_name: Piceid

substrate: Piceid


substrate_name: H+; NADPH; Testosterone; O2

assay_conditions_summary: cofactor NADP+

substrate: H+; NADPH; Testosterone; O2


substrate_name: Resveratroloside

substrate: Resveratroloside


enzyme_display_name: ent-sandaracopimaradiene 3-hydroxylase

organism: Oryza sativa

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

enzyme: ent-sandaracopimaradiene 3-hydroxylase

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


enzyme_display_name: phenylacetonitrile alpha-monooxygenase

organism: Chamberlinius hualienensis

substrate_name: 3-methyl phenylacetonitrile

enzyme: phenylacetonitrile alpha-monooxygenase

substrate: 3-methyl phenylacetonitrile


substrate_name: 2-methyl phenylacetonitrile

substrate: 2-methyl phenylacetonitrile


substrate_name: phenylacetonitrile

substrate: phenylacetonitrile


enzyme_display_name: pentalenic acid synthase

organism: Streptomyces avermitilis

substrate_name: Compactin

enzyme: pentalenic acid synthase

substrate: Compactin


substrate_name: diclofenac

substrate: diclofenac


enzyme_display_name: isopenicillin-N synthase

organism: Cephalosporium acremonium

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

enzyme: isopenicillin-N synthase


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


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


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


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


enzyme_display_name: (-)-pinoresinol reductase

organism: Arabidopsis thaliana

substrate_name: (-)-pinoresinol

enzyme: (-)-pinoresinol reductase

substrate: (-)-pinoresinol


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


organism: Camellia sinensis var. sinensis


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

organism: Thermococcus kodakarensis

substrate_name: NADH

assay_conditions_summary: pH 7.8; 348.15 K; cofactor NADH

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

substrate: NADH


organism: Thermococcus profundus

substrate_name: NADPH

assay_conditions_summary: pH 7.2; 348.15 K; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 7.2; 348.15 K; cofactor NADH


enzyme_display_name: caffeoyl-CoA O-methyltransferase

substrate_name: eriodictyol

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

enzyme: caffeoyl-CoA O-methyltransferase

substrate: eriodictyol


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


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium hassiacum

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

enzyme: MMP 1-O-methyltransferase


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


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


enzyme_display_name: pinosylvin synthase

organism: Pinus sylvestris

substrate_name: Malonyl-CoA; Cinnamoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: pinosylvin synthase

substrate: Malonyl-CoA; Cinnamoyl-CoA


enzyme_display_name: demethoxycurcumin synthase

organism: Curcuma longa

enzyme: demethoxycurcumin synthase


enzyme_display_name: glycine C-acetyltransferase

organism: Escherichia coli

substrate_name: Glycine; Acetyl-CoA

enzyme: glycine C-acetyltransferase

substrate: Glycine; Acetyl-CoA


organism: Thermus thermophilus


enzyme_display_name: trehalose 6-phosphate phosphorylase

organism: Badhamia polycephala

substrate_name: alpha,alpha-trehalose 6-phosphate

enzyme: trehalose 6-phosphate phosphorylase

substrate: alpha,alpha-trehalose 6-phosphate


organism: Lactococcus lactis

substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


organism: Lactococcus lactis subsp. lactis

substrate_name: Phosphate; Trehalose 6-phosphate

substrate: Phosphate; Trehalose 6-phosphate


substrate_name: Phosphate; Kojibiose

substrate: Phosphate; Kojibiose


enzyme_display_name: gallate dioxygenase

organism: Sphingobium sp. SYK-6

substrate_name: gallate

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

enzyme: gallate dioxygenase

substrate: gallate


enzyme_display_name: Gallate dioxygenase

organism: Sphingomonas paucimobilis

sequence_source: UniProtKB:Q5NTE5 direct exact accession lookup

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

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

enzyme: Gallate dioxygenase


organism: Synechocystis sp.

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

sequence_source: UniProtKB:P74334 direct exact accession lookup

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


organism: Streptomyces coeruleorubidus

sequence_source: UniProtKB:A0A3B6UEU3 direct exact accession lookup

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: Methylxanthine N1-demethylase NdmA

organism: Pseudomonas putida

substrate_name: theophylline

sequence_source: UniProtKB:H9N289 direct exact accession lookup

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

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

enzyme: Methylxanthine N1-demethylase NdmA

substrate: theophylline


substrate_name: Caffeine

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

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

substrate: Caffeine


substrate_name: paraxanthine

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

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

substrate: paraxanthine


enzyme_display_name: Methylxanthine N3-demethylase NdmB

sequence_source: UniProtKB:H9N290 direct exact accession lookup

enzyme: Methylxanthine N3-demethylase NdmB


substrate_name: Theobromine

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

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

substrate: Theobromine


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

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


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

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


enzyme_display_name: Tabersonine 16-hydroxylase 1

organism: Catharanthus roseus

substrate_name: H+; NADPH; O2; Tabersonine

sequence_source: UniProtKB:P98183 direct exact accession lookup

enzyme: Tabersonine 16-hydroxylase 1

substrate: H+; NADPH; O2; Tabersonine


substrate_name: tabersonine

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

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

substrate: tabersonine


organism: Arabidopsis thaliana

sequence_source: UniProtKB direct lookup Q9C5D7

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


organism: Goniophlebium amoenum

substrate_name: caffeoyl-CoA

sequence_source: UniProtKB direct lookup A0A4Y5R9F4

substrate: caffeoyl-CoA


substrate_name: quercetin

substrate: quercetin


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


organism: Linum usitatissimum

sequence_source: UniProtKB direct lookup Q4JHB1

assay_conditions_summary: 303.15 K; cofactor CoA


organism: Mesembryanthemum crystallinum

substrate_name: eriodictyol

sequence_source: UniProtKB direct lookup Q6YI95

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

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

substrate: eriodictyol


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


substrate_name: quercetagetin

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

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

substrate: quercetagetin


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

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


organism: Plagiochasma appendiculatum

sequence_source: UniProtKB direct lookup A0A0U2YR01


organism: Pyrus x bretschneideri

sequence_source: UniProtKB direct lookup A0A343J4W7

assay_conditions_summary: pH 4; 310.15 K; cofactor CoA


organism: Escherichia coli


substrate_name: D-mannitol[side 1]

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

substrate: D-mannitol[side 1]


organism: Methanocaldococcus jannaschii

substrate_name: GTP

substrate: GTP


substrate_name: Adenosyl cobinamide phosphate

substrate: Adenosyl cobinamide phosphate


enzyme_display_name: cardiolipin synthase (CMP-forming)

substrate_name: CDP-dioleoylglycerol

enzyme: cardiolipin synthase (CMP-forming)

substrate: CDP-dioleoylglycerol


organism: Saccharomyces cerevisiae


enzyme_display_name: thiosulfate--thiol sulfurtransferase

organism: Homo sapiens

substrate_name: thiosulfate

enzyme: thiosulfate--thiol sulfurtransferase

substrate: thiosulfate


proof_lines:
37°C, pH 7.4
cosubstrate glutathione, 37°C, pH 7.4


organism: Ommastrephes sloanei

substrate_name: 3'-Phosphoadenylyl sulfate; Chondroitin sulfate A


organism: Rhodococcus erythropolis

sequence_variant_note: Resolved canonical sequence from UniProtKB:P54997 and applied mutation signature Y63F/Q65H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54997 and applied mutation signature Y63F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P54997 and applied mutation signature Y63S to reconstruct the assayed variant sequence.


enzyme_display_name: S-inosyl-L-homocysteine hydrolase

substrate_name: Inosine

enzyme: S-inosyl-L-homocysteine hydrolase

substrate: Inosine


enzyme_display_name: C5a peptidase

organism: Streptococcus pyogenes

substrate_name: Peptide; H2O

enzyme: C5a peptidase

substrate: Peptide; H2O


substrate_name: C75-BODIPY-labeled recombinant human C5a peptide

sequence_variant_note: Resolved canonical sequence from direct_uniprot_rest:P15926 and applied mutation signature D783A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D783A, pH and temperature not specified in the publication


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

substrate: C75-BODIPY-labeled recombinant human C5a peptide


substrate_name: H2O; CXCL8

substrate: H2O; CXCL8


enzyme_display_name: complement subcomponent C1r

substrate_name: N-Acetyl-Gly-Lys methyl ester

enzyme: complement subcomponent C1r

substrate: N-Acetyl-Gly-Lys methyl ester


substrate_name: N-Acetyl-Gly-Lys methyl ester; H2O

proof_lines: pH 7.4, 37°C, substrate is a fragment consisting of complement control protein domains, CCP1 and CCP2, plus serine

substrate: N-Acetyl-Gly-Lys methyl ester; H2O


organism: Mus musculus

substrate_name: Fetuin glycopeptide I; H2O

substrate: Fetuin glycopeptide I; H2O


enzyme_display_name: arylformamidase

organism: Bacillus anthracis

substrate_name: N-formyl-L-kynurenine

proof_lines:
pH 7.4, 25°C, recombinant enzyme
Raw SKiD Env: Temp=25°C, pH=7.4

enzyme: arylformamidase

substrate: N-formyl-L-kynurenine


organism: Burkholderia cenocepacia


organism: Cupriavidus metallidurans

substrate_name: L-Formylkynurenine

substrate: L-Formylkynurenine


substrate_name: H2O; L-Formylkynurenine

substrate: H2O; L-Formylkynurenine


organism: Drosophila melanogaster

proof_lines:
pH 7.4, 22°C, recombinant enzyme
Raw SKiD Env: Temp=22°C, pH=7.4


enzyme_display_name: caffeoyl-CoA O-methyltransferase

organism: Vanilla planifolia

substrate_name: tricetin

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

enzyme: caffeoyl-CoA O-methyltransferase

substrate: tricetin


organism: Vitis vinifera

substrate_name: cyanidin 3-O-glucoside

sequence_source: UniProtKB:Q43237 canonical sequence from direct REST accession check on 2026-06-29

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

assay_conditions_summary: pH 8.5; 303.15 K; cofactor CoA

proof_lines: GST-tagged recombinant enzyme, at pH 8.5 and 30°C

proof_lines: thrombin-cleaved enzyme, at pH 8.5 and 30°C

substrate: cyanidin 3-O-glucoside


enzyme_display_name: methionine S-methyltransferase

organism: Wollastonia biflora

substrate_name: L-Methionine; S-Adenosyl-L-methionine

sequence_source: UniProtKB:Q9SWR3 canonical sequence from direct REST accession check on 2026-06-29

enzyme: methionine S-methyltransferase

substrate: L-Methionine; S-Adenosyl-L-methionine


organism: Medicago sativa

sequence_source: UniProtKB:P93324 canonical sequence from direct REST accession check on 2026-06-29


enzyme_display_name: indole-3-acetate O-methyltransferase

organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9FLN8 canonical sequence from direct REST accession check on 2026-06-29

enzyme: indole-3-acetate O-methyltransferase


organism: Oryza sativa Japonica Group

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB:Q0J998 canonical sequence from direct REST accession check on 2026-06-29

substrate: S-adenosyl-L-methionine


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium hassiacum

sequence_source: UniProtKB:K5B7F3 canonical sequence from direct REST accession check on 2026-06-29

enzyme: MMP 1-O-methyltransferase


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


organism: Panax ginseng

substrate_name: ginsenoside F2

sequence_source: UniProtKB:A0A0A6ZFY4 direct exact accession lookup, release 2026_02

proof_lines:
at pH 8.0 and 35°C
pH 7.5, 30°C

substrate: ginsenoside F2


organism: Homo sapiens

sequence_source: UniProtKB:O43825 direct exact accession lookup, release 2026_02


sequence_source: UniProtKB:Q9Y5Z6 direct exact accession lookup, release 2026_02


organism: Streptomyces hygroscopicus subsp. limoneus

substrate_name: GDP-valienol

sequence_source: UniProtKB:Q15JG1 direct exact accession lookup, release 2026_02

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

substrate: GDP-valienol


enzyme_display_name: alkylcobalamin dealkylase

substrate_name: Methylcobalamin; Glutathione

sequence_source: UniProtKB:Q9Y4U1 direct exact accession lookup, release 2026_02

enzyme: alkylcobalamin dealkylase

substrate: Methylcobalamin; Glutathione


enzyme_display_name: 3-aminobutanoyl-CoA transaminase

organism: Candidatus Cloacimonas acidaminovorans

sequence_source: UniProtKB:B0VH76 direct exact accession lookup, release 2026_02

assay_conditions_summary: pH 8.1; 301.15 K; cofactor CoA

enzyme: 3-aminobutanoyl-CoA transaminase


substrate_name: pyruvate

substrate: pyruvate


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


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


organism: Bacillus subtilis

sequence_source: UniProtKB:O31665 direct exact accession lookup, release 2026_02

smiles: CSCCC(=O)C(=O)[O-]


organism: Zea mays


enzyme_display_name: diaminobutyrate--pyruvate transaminase

organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I168 direct exact accession lookup, release 2026_02

enzyme: diaminobutyrate--pyruvate transaminase


substrate_name: Pyruvate; L-2,4-Diaminobutanoate

substrate: Pyruvate; L-2,4-Diaminobutanoate


organism: Staphylococcus aureus

substrate_name: 2',3'-Cyclic GMP

sequence_source: UniProtKB reviewed accession Q2FZ08; direct REST accession check on 2026-06-29

substrate: 2',3'-Cyclic GMP


substrate_name: H2O; Bis-4-nitrophenyl phosphate

substrate: H2O; Bis-4-nitrophenyl phosphate


substrate_name: Bis-4-nitrophenyl phosphate

substrate: Bis-4-nitrophenyl phosphate


substrate_name: 2',3'-Cyclic AMP

substrate: 2',3'-Cyclic AMP


sequence_source: UniProtKB reviewed accession Q7A6D4; direct REST accession check on 2026-06-29


sequence_source: UniProtKB reviewed accession O31521; direct REST accession check on 2026-06-29


sequence_source: UniProtKB reviewed accession O34559; direct REST accession check on 2026-06-29


organism: Bifidobacterium longum

sequence_source: UniProtKB reviewed accession E8MGH8; direct REST accession check on 2026-06-29


organism: Kribbella flavida

sequence_source: UniProtKB reviewed accession D2PPM7; direct REST accession check on 2026-06-29

proof_lines:
pH 8.0, 35°C
Raw SKiD Env: Temp=35°C, pH=8


enzyme_display_name: exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)

organism: Parabacteroides distasonis

sequence_source: UniProtKB reviewed accession A6LGF6; direct REST accession check on 2026-06-29


enzyme: exo beta-1,2-glucooligosaccharide sophorohydrolase (non-reducing end)


organism: Streptococcus pyogenes

substrate_name: Peptide

sequence_source: UniProtKB reviewed accession P15926; direct REST accession check on 2026-06-29

substrate: Peptide


assay_conditions_summary: cofactor ATP


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines:
pH 7.4
ATP in form of CaATP2-

substrate: ATP


enzyme_display_name: glycerate 2-kinase

organism: Escherichia coli

verification_status: verified

assay_conditions_summary: pH 7.5; 295.15 K; buffer pH 7; cofactor ATP

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GK (ATP); column kcat (s^-1) = 2.5; column Km (uM) = 61; column kcat/Km (M^-1 s^-1) = 4.1 x 10^4. captured primary segment: GK (ATP) | kcat 2.5 ± 0.4 s^-1 | Km 61 ± 2 uM | kcat/Km 4.1 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.5 s^(-1); the exported value is 2.5 s^(-1). Km: printed Table 1 cell 61 uM; 1 uM is 1/1000 mM, so 61 / 1000 = 0.061 mM; the exported value is 0.061 mM. kcat/Km: printed Table 1 cell 4.1 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.1 x 10^4 / 1000 = 41.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.5 / 0.061 = 40.98360655737705 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 1, row GK (ATP): kcat = 2.5 s^-1; Km = 61 uM; printed kcat/Km = 4.1 x 10^4 M^-1 s^-1.

row_label: Table 1, row GK (ATP)

enzyme: glycerate 2-kinase

status: verified


substrate_name: ATP; D-Glycerate

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GK (glycerate); column kcat (s^-1) = 2.5; column Km (uM) = 51; column kcat/Km (M^-1 s^-1) = 5.0 x 10^4. captured primary segment: GK (glycerate) | kcat 2.5 ± 0.1 s^-1 | Km 51 ± 1 uM | kcat/Km 5.0 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.5 s^(-1); the exported value is 2.5 s^(-1). Km: printed Table 1 cell 51 uM; 1 uM is 1/1000 mM, so 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 1 cell 5.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.0 x 10^4 / 1000 = 50.0 s^(-1)*mM^(-1); the live export row stores no kcat_over_km field for this identity, so the printed cell is carried in the typed kcat_over_km_provenance only.

raw_value_unit_evidence: Table 1, row GK (glycerate): kcat = 2.5 s^-1; Km = 51 uM; printed kcat/Km = 5.0 x 10^4 M^-1 s^-1.

row_label: Table 1, row GK (glycerate)

substrate: ATP; D-Glycerate


substrate_name: D-Glycerate

assay_conditions_summary: pH 7.5; 295.15 K; buffer pH 7; cofactor NADH

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.5 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 2.5 s^(-1); the exported value is 2.5 s^(-1). Km: printed Table 1 cell 51 uM; 1 uM is 1/1000 mM, so 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 1 cell 5.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.0 x 10^4 / 1000 = 50.0 s^(-1)*mM^(-1); the exported value is 49.01960784313726 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

table_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1)

substrate: D-Glycerate


organism: Escherichia coli K-12


substrate_name: (R)-glycerate

substrate: (R)-glycerate


organism: Picrophilus torridus


organism: Pyrococcus horikoshii

substrate_name: D-glycerate

substrate: D-glycerate


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: pH 6.5, 80°C, substrate-inhibition model


organism: Synechocystis sp.


organism: Thermoplasma acidophilum

assay_conditions_summary: pH 8; 328.15 K; cofactor ATP


organism: Thermoproteus tenax


organism: Thermotoga maritima


organism: Berberis koetineana

proof_lines:
isoenzyme NMT-III
isoenzyme NMT-II
isoenzyme NMT-I


organism: Medicago truncatula

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


enzyme_display_name: pinosylvin synthase

organism: Pinus densiflora

substrate_name: p-Coumaroyl-CoA

proof_lines:
isozyme PDSTS3
isozyme PDSTS2

enzyme: pinosylvin synthase

substrate: p-Coumaroyl-CoA


organism: Unknown

substrate_name: di-p-nitrophenyl phosphate

substrate: di-p-nitrophenyl phosphate


enzyme_display_name: cyanoalanine nitrilase

organism: Sorghum bicolor

proof_lines: isozyme complex NIT4A/B2, in 50 mM potassium phosphate (pH 8.0), 1 mM dithiothreitol, at 37°C

proof_lines: isozyme complex NIT4A/B1, in 50 mM potassium phosphate (pH 8.0), 1 mM dithiothreitol, at 37°C

enzyme: cyanoalanine nitrilase


enzyme_display_name: porphobilinogen synthase

organism: Homo sapiens

substrate_name: 5-aminolevulinic acid

sequence_source: UniProtKB reviewed accession P13716 direct lookup

assay_conditions_summary: pH 9

proof_lines: wild type, pH 9, predominantly hexamer and/or dimer

enzyme: porphobilinogen synthase

substrate: 5-aminolevulinic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P13716 canonical sequence with F12L reconstructed from selected mutation_signature and applied mutation signature F12L to reconstruct the assayed variant sequence.

proof_lines:
F12L, pH 9
F12L, pH 7


proof_lines:
Raw SKiD Env: Temp=-----, pH=9
Raw SKiD Env: Temp=-----, pH=7


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed accession Q59643 direct lookup

proof_lines:
37°C, pH 8.5
Raw SKiD Env: Temp=-----, pH=-----


organism: Methanocaldococcus jannaschii

substrate_name: L-homocysteine

sequence_source: UniProtKB reviewed Swiss-Prot exact accession Q58783; REST lookup 2026-06-29.

substrate: L-homocysteine


substrate_name: Inosine

substrate: Inosine


substrate_name: S-Inosyl-L-homocysteine

substrate: S-Inosyl-L-homocysteine


enzyme_display_name: retinoid isomerohydrolase

organism: Bos taurus

substrate_name: H2O; All-trans-Retinyl palmitate

sequence_source: UniProtKB reviewed Swiss-Prot exact accession Q28175; REST lookup 2026-06-29.

enzyme: retinoid isomerohydrolase

substrate: H2O; All-trans-Retinyl palmitate


organism: Danio rerio

substrate_name: an all-trans retinyl ester

proof_lines: pH and temperature not specified in the publication

substrate: an all-trans retinyl ester


organism: Acinetobacter baumannii

substrate_name: D-mannitol 1-phosphate

sequence_source: UniProtKB TrEMBL exact accession D0C7J2; REST lookup 2026-06-29.

substrate: D-mannitol 1-phosphate


enzyme_display_name: pseudouridine 5'-phosphatase

substrate_name: Pseudouridine 5'-phosphate; H2O

sequence_source: UniProtKB reviewed Swiss-Prot exact accession Q08623; REST lookup 2026-06-29.

enzyme: pseudouridine 5'-phosphatase

substrate: Pseudouridine 5'-phosphate; H2O


organism: Escherichia coli

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


sequence_source: UniProtKB reviewed Swiss-Prot exact accession P67095; REST lookup 2026-06-29.

assay_conditions_summary: pH 8.5; buffer Tris-HCl

proof_lines: in Tris-HCl buffer (pH 8.5) in the presence of 0.5 mM MnCl2

proof_lines: in Tris-HCl buffer (pH 8.5) in the presence of 5 mM MnCl2


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

proof_lines: pH 7.5, 37°C, mutant Y544A N-terminal domain of CpdB


proof_lines: pH 7.5, 37°C, mutant H117A N-terminal domain of CpdB


substrate_name: bis-4-nitrophenyl phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot exact accession P08331 with direct Y544A reconstruction; REST lookup 2026-06-29. and applied mutation signature Y544A to reconstruct the assayed variant sequence.

substrate: bis-4-nitrophenyl phosphate


substrate_name: CDP-choline

proof_lines:
pH 7.5, 37°C, N-terminal domain of CpdB
pH 7.5, 37°C
pH 7.5, 37°C, mature enzyme CpdB

substrate: CDP-choline


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Swiss-Prot exact accession P08331 with direct H117A reconstruction; REST lookup 2026-06-29. and applied mutation signature H117A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Swiss-Prot exact accession P08331; REST lookup 2026-06-29.

proof_lines: substrate bis-4-nitrophenyl phosphate, wild-type, pH 7.5, 37°C

proof_lines: substrate bis-4-nitrophenyl phosphate, isolated N-terminal domain,wild-type, pH 7.5, 37°C


sequence_source: UniProtKB reviewed Swiss-Prot exact accession P08331 only as canonical context; row-specific chimera/domain sequence not resolved.

proof_lines: chimera CpdB catalytic domain/UshA specificity domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: chimera UshA catalytic domain/CpdB specificity domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: isolated N-terminal domain, pH 7.5, 37°C


enzyme_display_name: tabersonine 16-hydroxylase

organism: Catharanthus roseus

substrate_name: tabersonine

enzyme: tabersonine 16-hydroxylase

substrate: tabersonine


enzyme_display_name: (-)-pinoresinol reductase

organism: Arabidopsis thaliana

substrate_name: (-)-pinoresinol

enzyme: (-)-pinoresinol reductase

substrate: (-)-pinoresinol


substrate_name: (+)-pinoresinol

substrate: (+)-pinoresinol


organism: Petunia hybrida

substrate_name: Unknown

substrate: Unknown


organism: Medicago sativa

substrate_name: isoliquiritigenin

substrate: isoliquiritigenin


substrate_name: indole-3-acetic acid (IAA)

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

substrate: indole-3-acetic acid (IAA)


organism: Pinus strobus

substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


organism: Pinus sylvestris


enzyme_display_name: glycine C-acetyltransferase

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

substrate_name: L-glycine (with acetyl-CoA at pH 6 and at 70 degrees Celsius)

assay_conditions_summary: pH 6; cofactor CoA

enzyme: glycine C-acetyltransferase


enzyme_display_name: kojibiose phosphorylase

organism: Thermoanaerobacter brockii

substrate_name: kojibiose

enzyme: kojibiose phosphorylase

substrate: kojibiose


organism: Citrus maxima

substrate_name: prunin

substrate: prunin


substrate_name: UDP-alpha-D-galactose

substrate: UDP-alpha-D-galactose


organism: Mus musculus


organism: Homo sapiens


organism: Escherichia coli (strain K12)

substrate_name: glycerate

substrate: glycerate


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: glycerate (at 50 degrees Celsius and at pH 7.3)

assay_conditions_summary: pH 7.3; cofactor ATP


organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

substrate_name: glycerate (at 45 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor ATP


organism: Streptomyces coeruleorubidus

proof_lines: kcat is 21.9 min(-1) with (3R)-3-[(carboxymethyl)amino]butanoate as substrate.


enzyme_display_name: methylxanthine N(1)-demethylase

organism: Pseudomonas putida

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

proof_lines: kcat is 190 min(-1) for caffeine (at pH 7.5 and 30 degrees Celsius).

enzyme: methylxanthine N(1)-demethylase


enzyme_display_name: methylxanthine N(3)-demethylase

substrate_name: 3-methylxanthine (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 46 min(-1) for theobromine (at pH 7.5 and 30 degrees Celsius).

enzyme: methylxanthine N(3)-demethylase


substrate_name: tabersonine in a T16H/16OMT coupled system

assay_conditions_summary: cofactor NADPH

proof_lines: concentrations of tabersonine greater than 30 uM are inhibitory.


enzyme_display_name: ent-sandaracopimaradiene 3-hydroxylase

organism: Oryza sativa subsp. japonica

substrate_name: ent-cassadiene

proof_lines: kcat is 1.4 sec(-1) with syn-pimaradiene as substrate.

enzyme: ent-sandaracopimaradiene 3-hydroxylase

substrate: ent-cassadiene


enzyme_display_name: phenylacetonitrile alpha-monooxygenase

organism: Prunus mume

substrate_name: phenylacetaldoxime (in the presence of NADPH at pH 7.6 and 30 degrees Celsius)

assay_conditions_summary: pH 7.6; cofactor NADPH

proof_lines: kcat is 46.3 min(-1) with phenylacetaldoxime as substrate (in the presence of NADPH at pH 7.6 and 30 degrees Celsius) (PubMed:25015725). kcat is 24.2 min(-1) with phenylacetonitrile as substrate (in the presence of NADPH at pH 7.6 and 30 de

enzyme: phenylacetonitrile alpha-monooxygenase


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

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

substrate_name: NADH

proof_lines: kcat is 68 sec(-1) for NADH oxidase activity. kcat is 50 sec(-1) for NADPH oxidase activity.

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

substrate: NADH


enzyme_display_name: kaempferol 4'-O-methyltransferase

organism: Solanum habrochaites

substrate_name: myricetin (in the presence of S-adenosylmethionine)

proof_lines: kcat is 7.40x10(-3) sec(-1) with myricetin as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat is 5.76x10(-3) sec(-1) with kaempferide as substrate (in the presence of S-adenosylmethionine) (PubMed:21343428). kcat

enzyme: kaempferol 4'-O-methyltransferase


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 / 3849)

enzyme: MMP 1-O-methyltransferase


enzyme_display_name: demethoxycurcumin synthase

organism: Curcuma longa

substrate_name: feruloyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 0.19 min(-1) with feruloyl-CoA. kcat is 0.36 min(-1) with p-coumaroyl-CoA.

enzyme: demethoxycurcumin synthase

substrate: feruloyl-CoA


substrate_name: kojibiose (at pH 7.5, 30 degrees Celsius)

proof_lines: kcat is 1.0 sec(-1) for phosphorolysis of kojibiose, and kcat is 0.8 sec(-1) for the reverse reaction.


organism: Amycolatopsis orientalis

substrate_name: devancoaminyl-vancomycin

substrate: devancoaminyl-vancomycin


enzyme_display_name: inosine/xanthosine triphosphatase

organism: Escherichia coli

substrate_name: xanthosine 5'-triphosphate

sequence_source: UniProtKB P39411 direct REST lookup on 2026-06-29; UniProtKB reviewed entry P39411 / NCPP_ECOLI, Inosine/xanthosine triphosphatase, EC 3.6.1.73, Escherichia coli strain K12; PDB cross-reference 1U5W

enzyme: inosine/xanthosine triphosphatase

substrate: xanthosine 5'-triphosphate


substrate_name: guanosine 5'-triphosphate

substrate: guanosine 5'-triphosphate


substrate_name: 2'-deoxyinosine 5'-triphosphate

substrate: 2'-deoxyinosine 5'-triphosphate


substrate_name: inosine 5'-triphosphate

substrate: inosine 5'-triphosphate


enzyme_display_name: D-ornithine/D-lysine decarboxylase

organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-Lysine

sequence_source: UniProtKB Q8ZNC4 direct REST lookup on 2026-06-29; UniProtKB reviewed entry Q8ZNC4 / DOKDC_SALTY, D-ornithine/D-lysine decarboxylase, EC 4.1.1.116, Salmonella typhimurium strain LT2

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme

enzyme: D-ornithine/D-lysine decarboxylase

substrate: D-Lysine


substrate_name: D-ornithine

substrate: D-ornithine


enzyme_display_name: carboxynorspermidine decarboxylase

organism: Vibrio vulnificus

substrate_name: Carboxynorspermidine

sequence_source: UniProtKB Q8D8D2 direct REST lookup on 2026-06-29; UniProtKB reviewed entry Q8D8D2 / NSPC_VIBVU, Carboxynorspermidine/carboxyspermidine decarboxylase, EC 4.1.1.96, Vibrio vulnificus strain CMCP6

enzyme: carboxynorspermidine decarboxylase

substrate: Carboxynorspermidine


substrate_name: carboxyspermidine

smiles: NCCCCNCCC(N)C(=O)O

substrate: carboxyspermidine


substrate_name: carboxynorspermidine

smiles: NCCCNCCC(N)C(=O)O

substrate: carboxynorspermidine


enzyme_display_name: 2-dehydro-3-deoxy-D-gluconate aldolase

organism: Picrophilus oshimae

sequence_source: UniProtKB Q6KZI8 checked directly; not accepted as the row sequence because organism does not match selected row

proof_lines: pH 6.2, 60°C, enzyme purified from Picrophilus torridus

enzyme: 2-dehydro-3-deoxy-D-gluconate aldolase


organism: Picrophilus torridus

sequence_source: UniProtKB Q6KZI8 direct REST lookup on 2026-06-29; UniProtKB reviewed entry Q6KZI8 / KDGA_PICTO, 2-dehydro-3-deoxy-D-gluconate/2-dehydro-3-deoxy-phosphogluconate aldolase, EC 4.1.2.14 and EC 4.1.2.51, Picrophilus torridus strain KAW 2/3; PDB cross-reference 4UXD


enzyme_display_name: porphobilinogen synthase

sequence_source: UniProtKB P0ACB2 direct REST lookup on 2026-06-29; UniProtKB reviewed entry P0ACB2 / HEM2_ECOLI, Delta-aminolevulinic acid dehydratase, EC 4.2.1.24, Escherichia coli strain K12

enzyme: porphobilinogen synthase


enzyme_display_name: arylformamidase

organism: Mus musculus

substrate_name: H2O; L-Formylkynurenine; H2O; L-Formylkynurenine; Formate; L-Kynurenine

sequence_source: UniProtKB:Q8K4H1 direct lookup

enzyme: arylformamidase


substrate_name: N-formyl-L-kynurenine

proof_lines:
pH 7.4, native wild-type enzyme
pH 7.4, recombinant wild-type enzyme

substrate: N-formyl-L-kynurenine


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB:Q9I234 direct lookup


organism: Saccharomyces cerevisiae

source_db: brenda; skid

sequence_source: UniProtKB:Q04066 direct lookup

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7.4

source: brenda; skid


organism: Streptomyces coelicolor

sequence_source: UniProtKB:Q9X8R1 direct lookup

proof_lines: pH 7.4, temperature not specified in the publication, recombinant His6-tagged enzyme


enzyme_display_name: N-substituted formamide deformylase

organism: Arthrobacter pascens

substrate_name: N-benzylformamide; N-butylformamide

sequence_source: UniProtKB:Q68AP4 direct lookup

enzyme: N-substituted formamide deformylase

substrate: N-benzylformamide; N-butylformamide


substrate_name: N-Benzylformamide; H2O; N-Benzylformamide; H2O; Formate; Benzylamine; N-Butylformamide; H2O; N-Butylformamide; Butylamine


enzyme_display_name: cyanoalanine nitrilase

organism: Lupinus angustifolius

substrate_name: H2O; 3-Cyano-L-alanine; H2O; 3-Cyano-L-alanine; L-Aspartate; NH3

sequence_source: UniProtKB:Q3LRV4 direct lookup

enzyme: cyanoalanine nitrilase


source_db: sabio_rk; brenda

sequence_source: UniProtKB:Q5QGZ8 direct lookup

substrate: H2O; 3-Cyano-L-alanine; H2O; 3-Cyano-L-alanine; L-Aspartate; NH3

source: sabio_rk; brenda


enzyme_display_name: ADP-sugar diphosphatase

organism: Arabidopsis thaliana

substrate_name: ADP-ribose; H2O; ADP-ribose; H2O; AMP; D-Ribose 5-phosphate; ADPglucose; H2O; ADPglucose; D-Glucose 1-phosphate

sequence_source: UniProtKB:Q9SZ63 direct lookup

assay_conditions_summary: cofactor ADP

enzyme: ADP-sugar diphosphatase


enzyme_display_name: UDP-2,3-diacylglucosamine diphosphatase

organism: Caulobacter vibrioides

sequence_source: UniProtKB:A0A0H3C8Q1 direct lookup

proof_lines: in 100 mM sodium acetate, 50 mM bis(2-hydroxyethyl)imino-tris(hydroxymethyl)hexane, and 50 mM Tris, 2 mM MgCl2, at 30°C, pH not specified in the publication

enzyme: UDP-2,3-diacylglucosamine diphosphatase


sequence_source: UniProtKB:P43341 direct lookup

proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8


organism: Haemophilus influenzae

sequence_source: UniProtKB:P44046 direct lookup


organism: Klebsiella pneumoniae

substrate_name: Unknown

sequence_source: UniProtKB:A6T5R0 direct lookup

substrate: Unknown


organism: Klebsiella pneumoniae subsp. pneumoniae

assay_conditions_summary: pH 8


organism: Escherichia coli (strain K12)

substrate_name: mannitol phosphorylation

substrate: mannitol phosphorylation


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

substrate_name: adenosylcobinamide phosphate

substrate: adenosylcobinamide phosphate


enzyme_display_name: cardiolipin synthase (CMP-forming)

substrate_name: phosphatidylglycerol (dioleoyl species)

enzyme: cardiolipin synthase (CMP-forming)

substrate: phosphatidylglycerol (dioleoyl species)


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: phosphatidylglycerol

substrate: phosphatidylglycerol


enzyme_display_name: thiosulfate--thiol sulfurtransferase

organism: Homo sapiens

substrate_name: glutathione

enzyme: thiosulfate--thiol sulfurtransferase

substrate: glutathione


organism: Nototodarus sloanii

substrate_name: PAPS

substrate: PAPS


enzyme_display_name: retinoid isomerohydrolase

organism: Bos taurus

substrate_name: all-trans-retinyl palmitate

enzyme: retinoid isomerohydrolase

substrate: all-trans-retinyl palmitate


organism: Danio rerio

substrate_name: 11-cis retinol

substrate: 11-cis retinol


organism: Gallus gallus


enzyme_display_name: pseudouridine 5'-phosphatase

enzyme: pseudouridine 5'-phosphatase


organism: Bacillus subtilis (strain 168)

substrate_name: unsaturated rhamnogalacturonan disaccharide (at pH 6 and 30 degrees Celsius)

assay_conditions_summary: pH 6


enzyme_display_name: adenylylsulfatase

substrate_name: P(1)-P(3)-bis(5'-adenosyl) triphosphate

enzyme: adenylylsulfatase

substrate: P(1)-P(3)-bis(5'-adenosyl) triphosphate


organism: Vibrio alginolyticus

substrate_name: carboxynorspermidine (at 37 degrees Celsius and pH 8.25)


organism: Vibrio vulnificus (strain CMCP6)

substrate_name: carboxynorspermidine


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: KDG (at 60 degrees Celsius and pH 6.2)

substrate: KDG (at 60 degrees Celsius and pH 6.2)


substrate_name: 5-aminolevulinic acid

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

substrate: 5-aminolevulinic acid


substrate_name: 5-aminolevulinate at pH 7

assay_conditions_summary: pH 7

substrate: 5-aminolevulinate at pH 7


organism: Gardenia jasminoides

substrate_name: beta-D-glucosyl crocetin

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

proof_lines: kcat is 0.036 sec(-1) for beta-D-glucosyl crocetin. kcat is 0.071 sec(-1) for bis(beta-D-glucosyl) crocetin.

substrate: beta-D-glucosyl crocetin


organism: Panax ginseng

substrate_name: protopanaxadiol (at pH 7 and 35 degrees Celsius)

proof_lines: kcat is 55.6 usec(-1) with protopanaxadiol as substrate (at pH 7 and 35 degrees Celsius). kcat is 134.7 usec(-1) with compound K as substrate (at pH 7 and 35 degrees Celsius).


substrate_name: ginsenoside Rh2 (at pH 8 and 40 degrees Celsius)

proof_lines: kcat is 8.6 sec(-1) with ginsenoside Rh2 as substrate (at pH 7 and 35 degrees Celsius). kcat is 0.41 sec(-1) with ginsenoside F2 as substrate (at pH 7 and 35 degrees Celsius) (PubMed:25320211). kcat is 1111 sec(-1) with ginsenoside Rh2 as s


organism: Streptomyces hygroscopicus subsp. limoneus

substrate_name: GDP-valienol

proof_lines: kcat is 7 min(-1) with GDP-valienol as substrate. kcat is 7 min(-1) with validamine 7-phosphate as substrate.

substrate: GDP-valienol


enzyme_display_name: alkylcobalamin dealkylase

proof_lines: kcat is 11.7 h(-1) for the dealkylation of methylcobalamin (MeCbl) (PubMed:19801555). kcat is 0.006 h(-1) for the dealkylation of 5'-deoxyadenosylcobalamin (AdoCbl) (PubMed:19801555).

enzyme: alkylcobalamin dealkylase


enzyme_display_name: 3-aminobutanoyl-CoA transaminase

organism: Cloacimonas acidaminovorans (strain Evry)

proof_lines: kcat is 1.80 sec(-1) for 3-aminobutyryl-CoA. kcat is 1.80 sec(-1) for alpha-ketoglutarate. kcat is 0.4 sec(-1) for pyruvate.

enzyme: 3-aminobutanoyl-CoA transaminase


substrate_name: KMTB

substrate: KMTB


substrate_name: PtdIns (in the absence of phosphatidylserine)

assay_conditions_summary: cofactor ATP

proof_lines: In the absence of the carrier phosphatidylserine, enzymatic kinetics toward PtdIns4P are non-linear.


enzyme_display_name: glycerate 2-kinase

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

substrate_name: ATP

proof_lines: kcat is 14.4 sec(-1) for phosphorylation of D-glycerate.

enzyme: glycerate 2-kinase

substrate: ATP


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

substrate_name: adenosylcobinamide

proof_lines: kcat is 15.1 min(-1) for adenosylcobinamide kinase activity. kcat is 5.6 min(-1) for guanylyltransferase activity.

substrate: adenosylcobinamide


organism: Rhodococcus qingshengii

substrate_name: HBPS

substrate: HBPS


enzyme_display_name: S-inosyl-L-homocysteine hydrolase

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

substrate_name: inosine (at pH 7.0 and 70 degrees Celsius)

proof_lines: kcat is 0.83 sec(-1) for the synthesis of SIH from inosine and L-homocysteine. kcat is 0.42 sec(-1) for the hydrolysis of SIH (at pH 7.0 and 70 degrees Celsius).

enzyme: S-inosyl-L-homocysteine hydrolase


substrate_name: unsaturated rhamnogalacturonan disaccharide (at pH 4 and 30 degrees Celsius)


organism: Mus musculus

substrate_name: fetuin glycopeptide I

substrate: fetuin glycopeptide I


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: asialofetuin

substrate: asialofetuin


substrate_name: N-formyl-L-kynurenine

substrate: N-formyl-L-kynurenine


organism: Arthrobacter pascens

substrate_name: N-benzylformamide

substrate: N-benzylformamide


organism: Arabidopsis thaliana

substrate_name: Ala(CN) (for the nitrilase activity)

substrate: Ala(CN) (for the nitrilase activity)


organism: Lupinus angustifolius

substrate_name: Ala(CN)

substrate: Ala(CN)


substrate_name: ADP-D-ribose

substrate: ADP-D-ribose


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)


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


substrate_name: adenosine 5'-phosphoramidate (at pH 6.8)


enzyme_display_name: isopenicillin-N synthase

organism: Hapsidospora chrysogena

substrate_name: Unknown

enzyme: isopenicillin-N synthase

substrate: Unknown


enzyme_display_name: (-)-pinoresinol reductase

organism: Thuja plicata

substrate_name: (-)-pinoresinol

proof_lines: wild type isoform PLR2, at pH 8.0 and 30°C

enzyme: (-)-pinoresinol reductase

substrate: (-)-pinoresinol


proof_lines: mutant G267V of isoform PLR2, at pH 8.0 and 30°C


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

organism: Giardia duodenalis

substrate_name: NADH

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

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

substrate: NADH


enzyme_display_name: caffeoyl-CoA O-methyltransferase

organism: Ammi majus

substrate_name: quercetin

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH 7.5, 37°C, in presence of 0.1 mM Co2+

proof_lines: pH 7.5, 37°C, in presence of 0.15 mM Mg2+

enzyme: caffeoyl-CoA O-methyltransferase

substrate: quercetin


organism: Azadirachta indica

substrate_name: caffeic acid

substrate: caffeic acid


organism: Camellia sinensis

assay_conditions_summary: pH 6.8; 308.15 K; cofactor CoA


organism: Citrus reticulata

substrate_name: tricetin

substrate: tricetin


organism: Citrus sinensis

substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: caffeoyl-CoA


organism: Medicago sativa


organism: Nicotiana tabacum

sequence_variant_note: Resolved canonical sequence from UniProtKB O24144 FASTA; PMID 11459845 and NCBI protein 30580325 link to O24144 and applied mutation signature Q61S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O24144 FASTA; PMID 11459845 and NCBI protein 30580325 link to O24144


organism: Oryza sativa

assay_conditions_summary: pH 7.5; 310.15 K; buffer Tris-HCl; cofactor CoA

proof_lines: OMT-17, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C


organism: Triticum aestivum

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA


enzyme_display_name: kaempferol 4'-O-methyltransferase

organism: Dianthus caryophyllus

substrate_name: S-Adenosyl-L-methionine; Kaempferol

enzyme: kaempferol 4'-O-methyltransferase

substrate: S-Adenosyl-L-methionine; Kaempferol


enzyme_display_name: indole-3-acetate O-methyltransferase

organism: Illicium anisatum

enzyme: indole-3-acetate O-methyltransferase


organism: Populus trichocarpa

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: MMP 1-O-methyltransferase

organism: Mycolicibacterium smegmatis

enzyme: MMP 1-O-methyltransferase


enzyme_display_name: pinosylvin synthase

organism: Pinus sylvestris

substrate_name: phenylpropionyl-CoA

enzyme: pinosylvin synthase

substrate: phenylpropionyl-CoA


enzyme_display_name: gallate dioxygenase

organism: Pseudomonas putida

substrate_name: gallate

enzyme: gallate dioxygenase

substrate: gallate


organism: Sphingobium sp. SYK-6

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


enzyme_display_name: tabersonine 16-hydroxylase

organism: Catharanthus roseus

substrate_name: NADPH

enzyme: tabersonine 16-hydroxylase

substrate: NADPH


enzyme_display_name: taxadiene 5alpha-hydroxylase

organism: Taxus cuspidata

enzyme: taxadiene 5alpha-hydroxylase


organism: Taxus media

assay_conditions_summary: cofactor NADP+


organism: Homo sapiens

substrate_name: taurochenodeoxycholate

substrate: taurochenodeoxycholate


enzyme_display_name: ent-sandaracopimaradiene 3-hydroxylase

substrate_name: ent-cassadiene

proof_lines: pH and temperature not specified in the publication

enzyme: ent-sandaracopimaradiene 3-hydroxylase

substrate: ent-cassadiene


organism: Actinomyces sp.


organism: Amycolatopsis lactamdurans


organism: Flavobacterium sp.


enzyme_display_name: demethoxycurcumin synthase

organism: Curcuma longa

proof_lines: pH 8.0, 37°C, with cinnamoyl-diketide-N-acetylcysteaminyl-CoA

enzyme: demethoxycurcumin synthase


enzyme_display_name: glycine C-acetyltransferase

organism: Bos taurus

substrate_name: acetyl-CoA

enzyme: glycine C-acetyltransferase

substrate: acetyl-CoA


organism: Escherichia coli

substrate_name: propionyl-CoA

substrate: propionyl-CoA


organism: Thermus thermophilus


enzyme_display_name: trehalose 6-phosphate phosphorylase

organism: Lactococcus lactis ssp. lactis

substrate_name: glucose 6-phosphate

enzyme: trehalose 6-phosphate phosphorylase

substrate: glucose 6-phosphate


enzyme_display_name: kojibiose phosphorylase

substrate_name: D-glucose

enzyme: kojibiose phosphorylase

substrate: D-glucose


organism: Lactobacillus acidophilus

proof_lines: pH 6.2, 45°C, recombinant loop 3 mutant 2 of maltose phosphorylase

proof_lines: pH 6.2, 45°C, recombinant loop 3 mutant 3 of maltose phosphorylase

proof_lines: pH 6.2, 45°C, recombinant loop 3 mutant 1 of maltose phosphorylase


organism: Thermoanaerobacter brockii

substrate_name: kojibiose

substrate: kojibiose


substrate_name: phosphate

substrate: phosphate


substrate_name: beta-D-glucose 1-phosphate

substrate: beta-D-glucose 1-phosphate


organism: Citrus maxima

substrate_name: UDP-L-rhamnose

proof_lines: pH 7.5, 37°C, cosubstrate hesperetin 7-O-glucoside

proof_lines: pH 7.5, 37°C, cosubstrate naringenin 7-O-glucoside

substrate: UDP-L-rhamnose


organism: Dipsacus asperoides

substrate_name: UDP-beta-L-rhamnose

substrate: UDP-beta-L-rhamnose


organism: Panax major

substrate_name: protopanaxadiol

substrate: protopanaxadiol


organism: Salinispora tropica

substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


organism: Gallus gallus


organism: Mus musculus


organism: Oryctolagus cuniculus


organism: Rattus norvegicus


enzyme_display_name: alkylcobalamin dealkylase

organism: Homo sapiens

substrate_name: nitrocobalamin

enzyme: alkylcobalamin dealkylase

substrate: nitrocobalamin


organism: Solanum lycopersicum


enzyme_display_name: diaminobutyrate--pyruvate transaminase

organism: Halomonas elongata

substrate_name: L-glutamate

enzyme: diaminobutyrate--pyruvate transaminase

substrate: L-glutamate


organism: Halorhodospira halochloris


organism: Pseudomonas aeruginosa

substrate_name: pyruvate

proof_lines: pH 7.5, 25°C, with 2-oxoglutarate, recombinant enzyme

proof_lines: pH 7.5, 25°C, with pyruvate, recombinant enzyme

substrate: pyruvate


substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, reaction with phosphatidylinositol, without phosphatidylserine

proof_lines: pH 7.5, 30°C, reaction with phosphatidylinositol, in presence of phosphatidylserine

proof_lines: pH 7.5, 30°C, in presence of phosphatidylserine

substrate: ATP


enzyme_display_name: glycerate 2-kinase

organism: Escherichia coli

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP

enzyme: glycerate 2-kinase


organism: Hyphomicrobium methylovorum

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: cosubstrate D-glycerate, at pH 7.0, 30°C


organism: Picrophilus oshimae