sequence_variant_note: Resolved canonical sequence from UniProtKB:C6F3U5 direct lookup plus selected-row mutation E134A and applied mutation signature E134A to reconstruct the assayed variant sequence.


enzyme_display_name: phenacrylate decarboxylase

organism: Enterobacter sp.

substrate_name: ferulate

source_db: brenda

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_source: UniProtKB:C6F3U5 direct UniProtKB lookup

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

enzyme: phenacrylate decarboxylase

substrate: ferulate

source: brenda


source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB:C6F3U5 direct lookup plus selected-row mutation W25A and applied mutation signature W25A to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

source: oed


sequence_source: UniProtKB:C6F3U5 direct lookup plus selected-row mutation E134A


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Saccharomyces cerevisiae

substrate_name: trans-cinnamate

sequence_source: UniProtKB:Q03034 direct UniProtKB lookup

substrate: trans-cinnamate


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

source_databases_merged: brenda skid


enzyme_display_name: cyclin-dependent kinase

organism: Homo sapiens

substrate_name: ATP

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

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines:
in 20 mM MOPS (pH 7.5), at 30°C
pH 7.5, 37°C

enzyme: cyclin-dependent kinase

substrate: ATP


substrate_name: ADAQHATPPKKKRKVEDPKDF

proof_lines:
pH 7.4, Cdk1-as1/cyclin 2B
pH 7.4, Cdk1-as1/cyclin 5B

substrate: ADAQHATPPKKKRKVEDPKDF


enzyme_display_name: cerebroside-sulfatase

organism: Acipenser gueldenstaedtii

substrate_name: p-nitrocatechol sulfate

kcat_display: Not reported

proof_lines: in milt plasma with 160 mM sodium chloride

enzyme: cerebroside-sulfatase

substrate: p-nitrocatechol sulfate


organism: Bos taurus

substrate_name: cerebroside 3-sulfate

proof_lines:
depends on taurocholate concentrations
in presence of 2 mM taurocholate
at pH 5.6

substrate: cerebroside 3-sulfate


organism: Helix pomatia


substrate_name: 4-nitrocatechol sulfate

substrate: 4-nitrocatechol sulfate


organism: Marthasterias glacialis


organism: Oryctolagus cuniculus

substrate_name: nitrocatechol sulfate

substrate: nitrocatechol sulfate


organism: Sus scrofa

proof_lines:
seminal plasma
sperm cell extract


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

sequence_source: UniProtKB direct accession lookup

substrate: Unknown


substrate_name: H2O; 4-Nitrocatechol sulfate

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

substrate: H2O; 4-Nitrocatechol sulfate


organism: Mus musculus

substrate_name: 4-Nitrocatechol sulfate; H2O

substrate: 4-Nitrocatechol sulfate; H2O


enzyme_display_name: glutathione gamma-glutamate hydrolase

organism: Bacillus licheniformis

substrate_name: L-glutamic acid-(4-nitroanilide)

verification_status: unverified

enzyme: glutathione gamma-glutamate hydrolase

substrate: L-glutamic acid-(4-nitroanilide)

status: unverified


enzyme_display_name: 1,2-beta-oligoglucan phosphorylase

organism: Lachnoclostridium phytofermentans

substrate_name: alpha-D-glucose 1-phosphate

sequence_source: UniProt FASTA direct lookup on 2026-06-23; header=>tr|A9KJS6|A9KJS6_LACP7 Uncharacterized protein OS=Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) OX=357809 GN=Cphy_0694 PE=1 SV=1

enzyme: 1,2-beta-oligoglucan phosphorylase

substrate: alpha-D-glucose 1-phosphate


organism: Listeria innocua

sequence_source: identity_reuse_cache accession:Q92AT0 canonical sequence from source_record


substrate_name: sophorose

substrate: sophorose


enzyme_display_name: deoxyribose-phosphate aldolase

organism: Aeropyrum pernix

substrate_name: 2-deoxy-D-ribose 5-phosphate

sequence_source: identity_reuse_cache accession:Q9Y948 canonical sequence from source_record

proof_lines:
50°C, pH 6.5
Raw SKiD Env: Temp=50°C, pH=6.5

enzyme: deoxyribose-phosphate aldolase

substrate: 2-deoxy-D-ribose 5-phosphate


organism: Candidatus Aciduliprofundum boonei

sequence_source: identity_reuse_cache accession:B5IEU6 canonical sequence from source_record


organism: Escherichia coli

sequence_source: identity_reuse_cache accession:P0A6L0 canonical sequence from source_record


substrate_name: 2-Deoxy-D-ribose 5-phosphate

sequence_variant_note: Resolved canonical sequence from identity_reuse_cache accession:P0A6L0 canonical sequence from source_record and applied mutation signature S239E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxyribose-phosphate aldolase(Enzyme) mutant S239E

substrate: 2-Deoxy-D-ribose 5-phosphate


sequence_variant_note: Resolved canonical sequence from identity_reuse_cache accession:P0A6L0 canonical sequence from source_record and applied mutation signature S238D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from identity_reuse_cache accession:P0A6L0 canonical sequence from source_record and applied mutation signature R207E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxyribose-phosphate aldolase(Enzyme) mutant R207E


sequence_variant_note: Resolved canonical sequence from identity_reuse_cache accession:P0A6L0 canonical sequence from source_record and applied mutation signature K172E to reconstruct the assayed variant sequence.


proof_lines: SABIO-RK modifier species: deoxyribose-phosphate aldolase(Enzyme) mutant K172E


sequence_source: UniProtKB REST P0A6L0

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P0A6L0 and applied mutation signature S238D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxyribose-phosphate aldolase(Enzyme) mutant S238D


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P0A6L0 and applied mutation signature S239E to reconstruct the assayed variant sequence.


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

proof_lines: pH 7.5, 25°C, enzyme directly immobilized through ionic exchange interactions on oxidized multiwalled carbon nanotubes

source_databases_merged: sabio_rk brenda skid


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P0A6L0 and applied mutation signature R207E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P0A6L0 and applied mutation signature G205E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: deoxyribose-phosphate aldolase(Enzyme) mutant G205E


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P0A6L0 and applied mutation signature S239P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P0A6L0 and applied mutation signature S238I/S239I to reconstruct the assayed variant sequence.


organism: Haemophilus influenzae

sequence_source: UniProtKB REST P44430

proof_lines: pH 7.5, temperature not specified in the publication


organism: Halalkalibacterium halodurans

sequence_source: UniProtKB REST Q9KD67

sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q9KD67 and applied mutation signature F160Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST Q9KD67 and applied mutation signature M173I to reconstruct the assayed variant sequence.


organism: Bacillus cereus


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


proof_lines:
pH 7.5, 25°C, wild-type
wild type enzyme


substrate_name: Chloroacetaldehyde

substrate: Chloroacetaldehyde


organism: Lactiplantibacillus plantarum

substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Lactobacillus plantarum

substrate_name: Glyceraldehyde 3-phosphate; Propanal

substrate: Glyceraldehyde 3-phosphate; Propanal


organism: Pectobacterium atrosepticum


organism: Pyrobaculum aerophilum

proof_lines: recombinant enzyme at 25°C in triethanolamine-HCl (pH 7.5)

proof_lines: native enzyme at 25°C in 0.1 M sodium acetate (pH 6.0)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature M173V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature F160W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature I170V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature F160H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct lookup for Q9KD67 on 2026-06-23

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


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature M173L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature F160M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature F160K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup for Q9KD67 on 2026-06-23 and applied mutation signature F160Y/M173I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F160Y/M173I, at pH 8.5 and 30°C


organism: Haloarcula japonica

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

proof_lines: pH and temperature not specified in the publication


organism: Homo sapiens

sequence_source: UniProtKB REST direct lookup for Q9Y315 on 2026-06-23


organism: Hyperthermus butylicus

sequence_source: UniProtKB REST direct lookup for A2BLE9 on 2026-06-23

assay_conditions_summary: pH 5.5; 298.15 K; buffer 100 mM sodium acetate

proof_lines: in 100 mM sodium acetate buffer (pH 5.5) at 25°C


sequence_source: UniProtKB REST direct lookup for Q88Z64 on 2026-06-23


organism: Meiothermus ruber

sequence_source: UniProtKB REST direct lookup for D3PKW1 on 2026-06-23


organism: Paenibacillus sp.

sequence_source: UniProtKB REST direct lookup for C7E719 on 2026-06-23

assay_conditions_summary: pH 8.8; 323.15 K; buffer 100 mM Tris-HCl

proof_lines: in 100 mM Tris-HCl buffer (pH 8.8), at 50°C


organism: Pseudomonas syringae pv. syringae

sequence_source: UniProtKB REST direct lookup for Q4ZMV1 on 2026-06-23


organism: Aciduliprofundum boonei (strain DSM 19572 / T469)

source_db: uniprot

source: uniprot


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)


organism: Escherichia coli (strain K12)


organism: Pseudomonas syringae pv. syringae (strain B728a)


organism: Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2)


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


organism: Pyrobaculum calidifontis

sequence_source: UniProtKB A3MU95 FASTA/flat-file direct accession lookup


organism: Rhodococcus erythropolis

verification_status: corrected

protein_accession_database: NCBI Protein

sequence_source: NCBI Protein AFJ39578.1 translated from GenBank JN665070.1 CDS; PMID 22222309 source construct

status: corrected


organism: Thermococcus kodakarensis

sequence_source: UniProtKB Q877I0 FASTA/flat-file direct accession lookup


organism: Yersinia sp. EA015

sequence_source: UniProtKB C0LSK9 FASTA/flat-file direct accession lookup

assay_conditions_summary: pH 8.8; buffer 100 mM Tris-HCl; cofactor NADH

proof_lines: in 100 mM Tris-HCl buffer, pH 8.8, 0.3 mM NADH, 10 U alcohol dehydrogenase, 1 mM 2-deoxy-D-ribose-5-phosphate


organism: Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)

proof_lines: kcat is 97 sec(-1) for (beta-(1->2)-D-glucans) x 2 units in the synthetic reaction. kcat is 110 sec(-1) for (beta-(1->2)-D-glucans) x 3 units in the synthetic reaction. kcat is 90 sec(-1) for (beta-(1->2)-D-glucans) x 4 units in the synthet


organism: Rhodococcus erythropolis (strain PR4 / NBRC 100887)

proof_lines: kcat is 18 sec(-1) with 2-deoxy-D-ribose 5-phosphate as substrate. kcat is 1.23 sec(-1) with 2-deoxy-D-ribose as substrate.


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

substrate_name: 2-deoxy-D-ribose 5-phosphate (at 95 degrees Celsius)

proof_lines: kcat is 116 sec(-1) (at 95 degrees Celsius).


organism: Rattus norvegicus


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Streptococcus suis


organism: Thermotoga maritima

proof_lines: native enzyme at 25°C in 0.1 M imidazole-HCl (pH 6.5)


organism: Thermus thermophilus


enzyme_display_name: glycine amidinotransferase

substrate_name: arginine (alpha-transamidinase form)

proof_lines: Two forms of the enzyme (denoted alpha and beta) with slightly different kinetic properties are present in cellular extracts. The molecular basis of the differences is unclear.

enzyme: glycine amidinotransferase

substrate: arginine (alpha-transamidinase form)


organism: Homo sapiens

substrate_name: L-arginine

substrate: L-arginine


organism: Escherichia coli (strain K12)

substrate_name: glutathione transfer to glycylglycine (gly-gly)


substrate_name: glutathione

substrate: glutathione


substrate_name: glycylglycine

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

substrate: glycylglycine


substrate_name: leukotriene C(4)

substrate: leukotriene C(4)


organism: Bos taurus

substrate_name: diclofenac-S-acyl-glutathione

substrate: diclofenac-S-acyl-glutathione


organism: Lachnoclostridium phytofermentans

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: A9KJS6

proof_lines:
pH 7, 40°C
phosphorolysis, pH 7, 40°C
synthesis, pH 7, 40°C


organism: Listeria innocua

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: Q92AT0

proof_lines: pH 7.5, 30°C, cosubstrate alpha-D-glucopyranose 1-phosphate

proof_lines: pH 7.5, 30°C, cosubstrate phosphate, release of alpha-D-glucopyranose 1-phosphate


organism: Arabidopsis thaliana

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: Q9M0A5; sequence not assigned because accession/EC evidence is unresolved


sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: Q9M0A7; sequence not assigned because accession/EC evidence is unresolved


organism: Bacillus licheniformis

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23 supplied canonical context for A9YTT0; row-specific variant sequence not resolved

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

mutation_type: deletion

proof_lines:
mutant DELTAY385-I396, pH 8.0, 25°C
mutant DELTAY385-K394, pH 8.0, 25°C
mutant DELTAY385-P391, pH 8.0, 25°C


sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: A9YTT0


organism: Helicobacter pylori

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23 supplied canonical context for O25743; row-specific variant sequence not resolved


sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: O25743


substrate_name: L-glutamine

substrate: L-glutamine


substrate_name: oxidized glutathione

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: P19440

substrate: oxidized glutathione


substrate_name: leukotriene C4

sequence_source: UniProtKB REST direct accession lookup on 2026-06-23: P36269

substrate: leukotriene C4


organism: Thermochaetoides thermophila (strain DSM 1495 / CBS 144.50 / DAOM 24625 / IMI 039719)

substrate_name: H3K27me0 peptide substrate

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

substrate: H3K27me0 peptide substrate


enzyme_display_name: glutamate formimidoyltransferase

substrate_name: Unknown

enzyme: glutamate formimidoyltransferase

substrate: Unknown


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

substrate_name: 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)

proof_lines: kcat is 1.16 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).


organism: Streptococcus pyogenes serotype M1

substrate_name: 5-CHO-THF-Glu3 (at pH 7.3 and 30 degrees Celsius)

proof_lines: kcat is 0.13 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).


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

proof_lines: kcat is 0.27 sec(-1) for formyltransferase with 5-CHO-THF or 5-CHO-THF-Glu3 as substrates (at pH 7.3 and 30 degrees Celsius).

substrate: 5-CHO-THF (at pH 7.3 and 30 degrees Celsius)


organism: Candidatus Korobacter versatilis


organism: Picrophilus oshimae


organism: Streptococcus pyogenes


organism: Sus scrofa

substrate_name: tetrahydrofolate; (6R,S)-tetrahydrofolate; N-formimino-L-glutamate; (6S)-tetrahydropteroylpentaglutamate; tetrahydropteroic acid

proof_lines: recombinant His-tagged formiminotransferase domain

proof_lines: recombinant His-tagged bifunctional formiminotransferase cyclodeaminase


proof_lines: wild-type bifunctional formiminotransferase cyclodeaminase


organism: Thermoplasma acidophilum

sequence_source: UniProtKB Q9HI69 reviewed EC 2.1.2.5 entry supported by PMID 20952389


organism: Paramecium bursaria Chlorella virus 1

substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB O41094 direct FASTA lookup plus validated Y109G substitution reconstruction and applied mutation signature Y109G to reconstruct the assayed variant sequence.

substrate: S-adenosyl-L-methionine


sequence_source: UniProtKB O41094 direct FASTA lookup plus validated Y109G substitution reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB O41094 direct FASTA lookup plus validated L116A substitution reconstruction and applied mutation signature L116A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O41094 direct FASTA lookup plus validated L116A substitution reconstruction


sequence_source: UniProtKB O41094 direct FASTA lookup


sequence_source: UniProtKB P53603 direct FASTA lookup


substrate_name: histone H3(K27)

sequence_variant_note: Resolved canonical sequence from UniProtKB O41094 and RCSB 2G46/PubMed 16603186; Y50F reconstructed from canonical O41094 residue 50. and applied mutation signature Y50F to reconstruct the assayed variant sequence.

substrate: histone H3(K27)


sequence_variant_note: Resolved canonical sequence from UniProtKB O41094 and RCSB 2G46/PubMed 16603186; F52Y reconstructed from canonical O41094 residue 52. and applied mutation signature F52Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB O41094 and RCSB 2G46/PubMed 16603186.


organism: Glycine max

substrate_name: glycine

substrate: glycine


organism: Homo sapiens

sequence_source: UniProtKB reviewed Swiss-Prot P50440 (GATM_HUMAN), EC 2.1.4.1 evidence includes PubMed 3800397.


organism: Rattus norvegicus

substrate_name: arginine

sequence_source: UniProtKB reviewed Swiss-Prot P50442 (GATM_RAT), EC 2.1.4.1 evidence includes PubMed 6766137.

proof_lines:
beta-transamidinase
alpha-transamidinase
alpha-and beta-transamidinase

substrate: arginine


sequence_source: UniProtKB reviewed Swiss-Prot P50441 (GATM_PIG), EC 2.1.4.1 annotated by similarity to reviewed GATM.


sequence_source: UniProtKB:O41094 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:O41094 direct REST lookup and applied mutation signature Y109G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:O41094 direct REST lookup and applied mutation signature L116A to reconstruct the assayed variant sequence.


organism: Cylindrospermopsis raciborskii

sequence_source: UniProtKB:B0LI36 direct REST lookup

proof_lines:
per active site, pH 8.5, 30°C
pH 8.5, 30°C


substrate_name: L-Arginine; Glycine

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

sequence_source: UniProtKB:P50440 direct REST lookup

substrate: L-Arginine; Glycine


substrate_name: Glycine; L-Arginine

proof_lines: SABIO-RK modifier species: glycine amidinotransferase(Enzyme) mutant C410A N-terminal His6-tagged

substrate: Glycine; L-Arginine


sequence_source: UniProtKB:Q6ITZ7 direct REST lookup (primary accession P50442)


enzyme_display_name: 6-aminohexanoate-oligomer exohydrolase

organism: Paenarthrobacter ureafaciens

substrate_name: 6-aminohexanoate dimer

sequence_source: UniProtKB:P07061 direct REST lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07061 direct REST lookup and applied mutation signature R187S to reconstruct the assayed variant sequence.

smiles: NCCCCCC(O)=NCCCCCC(=O)O

enzyme: 6-aminohexanoate-oligomer exohydrolase

substrate: 6-aminohexanoate dimer


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07061 direct REST lookup and applied mutation signature R187A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07061 direct REST lookup and applied mutation signature R187G to reconstruct the assayed variant sequence.


enzyme_display_name: ferric-chelate reductase (NADPH)

organism: Escherichia coli (strain K12)

substrate_name: ferric ions (anaerobically at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: ferric-chelate reductase (NADPH)

substrate: ferric ions (anaerobically at pH 7.5)


enzyme_display_name: nicotinate riboside kinase

substrate_name: nicotinamide riboside (with ATP as cosubstrate)

assay_conditions_summary: cofactor ATP

enzyme: nicotinate riboside kinase


substrate: nicotinamide riboside (with ATP as cosubstrate)


organism: Brassica napus

substrate_name: Fe(III)-citrate

proof_lines: at optimal iron nutrition, pH and temperature not specified in the publication

proof_lines: at iron deficiency, pH and temperature not specified in the publication

proof_lines: at suboptimal iron nutrition, pH and temperature not specified in the publication

substrate: Fe(III)-citrate


organism: Escherichia coli

substrate_name: Fe(III)-EDTA

sequence_source: UniProtKB Q46871 (YQJH_ECOLI), reviewed; PubMed 21097627 supports yqjH ferric reductase activity.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

substrate: Fe(III)-EDTA


substrate_name: Fe(III)-enterobactin

sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB Q46871 (YQJH_ECOLI) using the selected R130A mutation note; PubMed 22098718 names YqjH ferric reductase activity. and applied mutation signature R130A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R130A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C

proof_lines: mutant enzyme R130A in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C

substrate: Fe(III)-enterobactin


substrate_name: Fe(III)-vibriobactin

sequence_source: UniProtKB Q46871 (YQJH_ECOLI), reviewed; PubMed 22098718 names YqjH ferric reductase activity.

proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C

substrate: Fe(III)-vibriobactin


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB Q46871 (YQJH_ECOLI) using the selected K55A mutation note; PubMed 22098718 names YqjH ferric reductase activity. and applied mutation signature K55A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K55A, in 50 mM Tris-HCl (pH 8.0) and 100 mM NaCl at 25°C


organism: Synechocystis sp.

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM sodium phosphate; cofactor FAD

proof_lines: in the presence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C

proof_lines: in the absence of FAD, in 50 mM sodium phosphate buffer (pH 7.0) containing 0.2 mM NADPH at 25°C


organism: Arthrobacter sp.


organism: Flavobacterium sp.

substrate_name: 6-aminohexanoate trimer

substrate: 6-aminohexanoate trimer


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

proof_lines:
single mutation D181E
mutation D181E


proof_lines:
single mutation D181N
mutation D181N


proof_lines: for EII without mutation, substitution of Asp181 to Asn or Glu affects substrate binding


organism: Pseudomonas sp.

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


substrate_name: NADPH; Fe3+

sequence_source: UniProtKB:Q46871 direct REST lookup on 2026-06-23

assay_conditions_summary: cofactor NADPH

substrate: NADPH; Fe3+


substrate_name: beta-D-ribosylnicotinamide

substrate: beta-D-ribosylnicotinamide


substrate_name: tiazofurin

substrate: tiazofurin


substrate_name: uridine

substrate: uridine


substrate_name: cytidine

substrate: cytidine


substrate_name: beta-D-ribosylnicotinate

substrate: beta-D-ribosylnicotinate


proof_lines: pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187G, hydrolysis in 90% t-butyl alcohol


proof_lines: pH 7.3, 30°C, recombinant enzyme Hyb-24DNY, hydrolysis in 90% t-butyl alcohol


proof_lines: pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187A, hydrolysis in 90% t-butyl alcohol


proof_lines: pH 7.3, 30°C, recombinant Hyb-24DNY mutant R187S, hydrolysis in 90% t-butyl alcohol


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

assay_conditions_summary: cofactor CoA


enzyme_display_name: putrescine carbamoyltransferase

organism: Enterococcus faecalis

substrate_name: Carbamoyl phosphate; Putrescine

sequence_source: UniProtKB:Q837U7 direct REST lookup on 2026-06-23

proof_lines: pH and temperature not specified in the publication

enzyme: putrescine carbamoyltransferase

substrate: Carbamoyl phosphate; Putrescine


substrate_name: putrescine

substrate: putrescine


substrate_name: ketopantoate

substrate: ketopantoate


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: alpha-ketoisovalerate (at 37 degrees Celsius and pH 7.5)


organism: Enterococcus faecalis (strain ATCC 700802 / V583)

substrate_name: carbamoyl phosphate

substrate: carbamoyl phosphate


substrate_name: Carbamoyl phosphate

assay_conditions_summary: pH 7

proof_lines:
at pH 7.0
arsenolytic cleavage
recombinant enzyme

substrate: Carbamoyl phosphate


enzyme_display_name: formate C-acetyltransferase

substrate_name: pyruvate (at pH 8.1 and 30 degrees Celsius)

assay_conditions_summary: pH 8.1; cofactor CoA

proof_lines: kcat is 1100 sec(-1) with pyruvate and CoA as substrates. kcat is 380 sec(-1) with formate and acetyl-CoA as substrates.

enzyme: formate C-acetyltransferase


sequence_source: UniProtKB REST Q9NWW6 canonical sequence checked 2026-06-23.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: with ATP, pH and temperature not specified in the publication


sequence_source: UniProtKB REST Q9NPI5 canonical sequence checked 2026-06-23.


organism: Unknown

substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


enzyme_display_name: mRNA guanylyltransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: GTP

enzyme: mRNA guanylyltransferase

substrate: GTP


substrate_name: Tetrahydropteroylpentaglutamate

proof_lines: forward and reverse reaction, methylenetetrahydrofolate: formaldehyde + tetrahydrofolate

substrate: Tetrahydropteroylpentaglutamate


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: peptide TSAVLQSGFRK-NH(2)


organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)

substrate_name: ATP (unmodified pRNA)

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

proof_lines: kcat is 0.013 min(-1) for unmodified pRNA (PubMed:39011881). kcat is 2.311 min(-1) for pRNA with N6,N6,2'-O trimethyladenosine on A1, 2'-O ribose methylations on A2 and C3, N3-2'-O-dimethyluridine on U4 (PubMed:39011881). kcat is 1.843 min(

substrate: ATP (unmodified pRNA)


organism: Vaccinia virus (strain Western Reserve)

substrate_name: GpppA

proof_lines: A-570 and A-763 mutants have 3-fold and 10-fold higher Km values for GpppA.

substrate: GpppA


organism: Corynebacterium glutamicum

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

proof_lines: pH 6.8, 37°C, recombinant mutant K25A/E189S


sequence_source: UniProtKB Q9X712 direct REST lookup, reviewed Swiss-Prot, 2026-06-23

proof_lines: pH 6.8, 37°C, recombinant wild-type enzyme


sequence_source: UniProtKB P31057 direct REST lookup, reviewed Swiss-Prot, 2026-06-23


organism: Clostridium butyricum

substrate_name: acetyl-CoA

proof_lines:
pyruvate-formate exchange
pyruvate

substrate: acetyl-CoA


substrate_name: Pyruvate; Coenzyme A

substrate: Pyruvate; Coenzyme A


substrate_name: pyruvate

substrate: pyruvate


proof_lines: pH 7.6, 30°C, recombinant wild-type enzyme


substrate_name: formate

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA

proof_lines:
backward direction
forward direction
pH 7.4, 30°C

substrate: formate


organism: Lactococcus lactis subsp. cremoris


organism: Lactococcus lactis subsp. lactis


organism: Streptococcus mutans


organism: Escherichia coli

substrate_name: CoA

sequence_source: UniProtKB:P09373 REST direct lookup 2026-06-23

assay_conditions_summary: pH 8.5; 294.15 K; cofactor CoA

proof_lines:
at pH 8.5 and 21°C
at pH 8.1 and 20°C

substrate: CoA


sequence_source: UniProtKB:O32797 REST direct lookup 2026-06-23


organism: Streptococcus bovis

substrate_name: Coenzyme A; Pyruvate

sequence_source: UniProtKB:O66391 REST direct lookup 2026-06-23

substrate: Coenzyme A; Pyruvate


sequence_source: UniProtKB:Q59934 REST direct lookup 2026-06-23


organism: Homo sapiens


organism: Orthopoxvirus vaccinia

proof_lines: pH 8.0, 37°C, guanylyltransferase activity, D1R domain, residues 1-545


proof_lines: pH 8.0, 37°C, guanylyltransferase activity, holoenzyme capping enzyme


organism: Saccharomyces cerevisiae


organism: Triticum aestivum


enzyme_display_name: Genome polyprotein / RNA-directed RNA polymerase-Methyltransferase NS5 context

organism: Dengue virus

substrate_name: Unknown

sequence_source: UniProtKB reviewed accession P29990; direct FASTA check on 2026-06-23

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

substrate: Unknown


enzyme_display_name: mRNA-capping enzyme subunit alpha

substrate_name: GTP; (5')ppPur-mRNA

sequence_source: UniProtKB reviewed accession Q01159; direct FASTA check on 2026-06-23

enzyme: mRNA-capping enzyme subunit alpha

substrate: GTP; (5')ppPur-mRNA


organism: Yellow fever virus

sequence_source: UniProtKB reviewed accession P03314; direct FASTA check on 2026-06-23

enzyme: Genome polyprotein / RNA-directed RNA polymerase-Methyltransferase NS5 context


enzyme_display_name: homoserine kinase

organism: Escherichia coli (strain K12)

substrate_name: L-homoserine

proof_lines: The catalytic efficiency is 500-fold higher with L-homoserine than with D-homoserine as substrate.

enzyme: homoserine kinase

substrate: L-homoserine


enzyme_display_name: folate gamma-glutamyl hydrolase

organism: Bos taurus

substrate_name: Pteroyltriglutamate

enzyme: folate gamma-glutamyl hydrolase

substrate: Pteroyltriglutamate


organism: Gallus gallus


organism: Geobacillus thermodenitrificans

proof_lines:
pH 7.8, 52°C
Vmax: 0.36 micromol/min/mg


substrate_name: methotrexate diglutamate

substrate: methotrexate diglutamate


organism: Methanocaldococcus jannaschii

substrate_name: ATP

sequence_source: UniProtKB REST current accession lookup: Q58504

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


organism: Arabidopsis thaliana

substrate_name: pteroylpentaglutamate

sequence_source: UniProtKB REST current accession lookup: O65355

proof_lines:
37°C, pH 6.0, AtGGH2
37°C, pH 6.0, AtGGH1

substrate: pteroylpentaglutamate


organism: Danio rerio

substrate_name: 5-formyltetrahydrofolate triglutamate

sequence_source: UniProtKB REST current accession lookup: Q6NY42

proof_lines:
Vmax: 87.6 nmol/min/microg
Raw SKiD Env: Temp=-----, pH=-----

substrate: 5-formyltetrahydrofolate triglutamate


organism: Solanum lycopersicum

substrate_name: folic acid pentaglutamate

sequence_source: UniProtKB REST current accession lookup: B2Z9Y3

substrate: folic acid pentaglutamate


substrate_name: p-aminobenzoylpentaglutamate

sequence_source: UniProtKB REST current accession lookup: B2Z9Y5

substrate: p-aminobenzoylpentaglutamate


substrate_name: Pteroylheptaglutamate

substrate: Pteroylheptaglutamate


organism: Lathyrus oleraceus


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed Q62867 (GGH_RAT), direct EC 3.4.19.9 + Rattus norvegicus lookup


organism: Sus scrofa

assay_conditions_summary: pH 4


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


organism: Homo sapiens

substrate_name: of tetrahydrofolate-Glu2

substrate: of tetrahydrofolate-Glu2


substrate_name: phosphatidylinositol-5- phosphate

substrate: phosphatidylinositol-5- phosphate


organism: Rhodospirillum rubrum

assay_conditions_summary: pH 8; 301.15 K; cofactor ATP


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Schizosaccharomyces pombe

proof_lines: in 50 mM HEPES, pH 7.5, 40 mM KCl, 10 mM MgCl2, at 37°C


organism: Triticum aestivum


organism: [Brevibacterium] flavum


organism: Escherichia coli

sequence_source: UniProtKB P00547 (KHSE_ECOLI), supported by PMID 4364023 title naming Escherichia coli K-12 homoserine kinase.

assay_conditions_summary: pH 7.8; 300.15 K; cofactor ATP


proof_lines:
mutant R234L
mutant enzyme R234L


substrate_name: D-homoserine

sequence_source: UniProtKB P00547 (KHSE_ECOLI), directly returned by UniProt search for PMID 8973190.

substrate: D-homoserine


substrate_name: L-homoserine propyl ester

proof_lines:
mutant H202L
mutant enzyme H202L

substrate: L-homoserine propyl ester


organism: Hordeum vulgare


assay_conditions_summary: pH 8.5; cofactor ATP


substrate_name: L-Homoserine; ATP

substrate: L-Homoserine; ATP


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature H139L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: homoserine kinase(Enzyme) mutant H139L


proof_lines: SABIO-RK modifier species: homoserine kinase(Enzyme) mutant R234C


proof_lines: SABIO-RK modifier species: homoserine kinase(Enzyme) mutant H202L


substrate_name: ATP; L-Homoserine

proof_lines: SABIO-RK modifier species: homoserine kinase(Enzyme) mutant R234L

substrate: ATP; L-Homoserine


proof_lines: SABIO-RK modifier species: homoserine kinase(Enzyme) mutant R234H


proof_lines: SABIO-RK modifier species: homoserine kinase(Enzyme) mutant H205Q


enzyme_display_name: rubredoxin--NAD(P)(+) reductase

organism: Pyrococcus furiosus

substrate_name: NADH

sequence_source: UniProtKB reviewed FASTA Q8U1K9 / NROR_PYRFU

assay_conditions_summary: pH 8; 353.15 K; cofactor NADH

enzyme: rubredoxin--NAD(P)(+) reductase

substrate: NADH


substrate_name: Oxidized benzyl viologen

substrate: Oxidized benzyl viologen


substrate_name: NADPH

assay_conditions_summary: pH 8; 353.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: arsenite methyltransferase

substrate_name: arsenite

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature D150N to reconstruct the assayed variant sequence.

enzyme: arsenite methyltransferase

substrate: arsenite


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature T104A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature V161A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature G82A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature R83A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature L77A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature S81A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature G134A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature Y135A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed FASTA Q9HBK9 / AS3MT_HUMAN and applied mutation signature V157A to reconstruct the assayed variant sequence.


organism: Cricetinae


substrate_name: S-adenosyl-L-methionine

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

proof_lines:
37°C, pH 8.0, Trp173 allozyme
37°C, pH 8.0, Thr287 allozyme

substrate: S-adenosyl-L-methionine


proof_lines: mutant enzyme C375S, in PBS (25 mM, pH 7.0), at 37°C


proof_lines: mutant enzyme C360S, in PBS (25 mM, pH 7.0), at 37°C


proof_lines: mutant enzyme C271S, in PBS (25 mM, pH 7.0), at 37°C


proof_lines: mutant enzyme C334S, in PBS (25 mM, pH 7.0), at 37°C


substrate_name: methylarsonate

assay_conditions_summary: pH 7.4; 298.15 K; buffer 100 mM Tris-HCl

proof_lines: mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C

proof_lines: mutant enzyme M287T, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C

proof_lines: mutant enzyme M287T, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 37°C

substrate: methylarsonate


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

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C

proof_lines: wild type enzyme, in the presence of 1 mM glutathione, in 100 mM Tris-HCl buffer (pH 7.4), at 25°C


organism: Oryctolagus cuniculus


substrate_name: Unknown

substrate: Unknown


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

substrate_name: rubredoxin (at 80 degrees Celsius, in the presence of NADPH)

proof_lines: kcat is 15000 sec(-1) with rubredoxin as substrate. kcat is 750 sec(-1) with benzyl viologen as substrate. kcat is 19 sec(-1) with 5,5'-dithiobis[2-nitrobenzoic acid] as substrate. kcat is 9 sec(-1) with H(2)O(2) as substrate. kcat is 341 s


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HBK9 canonical sequence, reconstructed with mutation R57A and applied mutation signature R57A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9HBK9 canonical sequence, reconstructed with mutation Y58A and applied mutation signature Y58A to reconstruct the assayed variant sequence.


proof_lines:
isoform PI5P4Kbeta, at pH 7.5 and 37°C
isoform PI5P4Kalpha, at pH 7.5 and 37°C


sequence_source: UniProtKB direct REST/FASTA check for reviewed accession P78356 (PI42B_HUMAN), Homo sapiens, EC 2.7.1.149.

assay_conditions_summary: pH 7.4; 295.15 K; cofactor ATP

proof_lines:
isoform PI5P4Kbeta, at pH 7.4 and 22°C
isoform PI5P4Kbeta, at pH 7.4 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB direct REST/FASTA check for reviewed accession P78356 plus explicit A381E reconstruction after confirming residue 381 is alanine. and applied mutation signature A381E to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor ATP

proof_lines: SABIO-RK modifier species: 1-phosphatidylinositol-5-phosphate 4-kinase(Enzyme) mutant II beta A381E


sequence_source: UniProtKB direct REST/FASTA check for reviewed accession P48426 (PI42A_HUMAN), Homo sapiens, EC 2.7.1.149.

proof_lines:
isoform PI5P4Kalpha, at pH 7.4 and 22°C
isoform PI5P4Kalpha, at pH 7.4 and 30°C


substrate_name: ATP

sequence_source: UniProtKB direct REST/FASTA check for reviewed accession Q8TBX8 (PI42C_HUMAN), Homo sapiens, EC 2.7.1.149.

proof_lines:
isoform PI5P4Kgamma, at pH 7.4 and 22°C
isoform PI5P4Kgamma, at pH 7.4 and 30°C

substrate: ATP


enzyme_display_name: formylglycine-generating enzyme

organism: Thermomonospora curvata

sequence_variant_note: Resolved canonical sequence from UniProtKB D1A7C3 reviewed canonical sequence; variants reconstructed from selected BRENDA mutation note when applicable. and applied mutation signature C187A/C231A/C284S/C298A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0

proof_lines: mutant C187A/C231A/C284S/C298A, at pH 8.0 and 25°C

proof_lines: mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0

enzyme: formylglycine-generating enzyme


sequence_source: UniProtKB D1A7C3 reviewed canonical sequence; variants reconstructed from selected BRENDA mutation note when applicable.

proof_lines: wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.002 mM CuSO4, pH 8.0

proof_lines: wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, pH 8.0


sequence_variant_note: Resolved canonical sequence from UniProtKB D1A7C3 reviewed canonical sequence; variants reconstructed from selected BRENDA mutation note when applicable. and applied mutation signature C187A/C284S/C298A to reconstruct the assayed variant sequence.

proof_lines: mutant C187A/C284S/C298A, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB D1A7C3 reviewed canonical sequence; variants reconstructed from selected BRENDA mutation note when applicable. and applied mutation signature Y273F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB D1A7C3 reviewed canonical sequence; variants reconstructed from selected BRENDA mutation note when applicable. and applied mutation signature C187A/C231A/Y273F/C284S/C298A to reconstruct the assayed variant sequence.

proof_lines: mutant C187A/C231A/Y273F/C284S/C298A, at pH 8.0 and 25°C


proof_lines: mutant enzyme S290K, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0


proof_lines: mutant enzyme C187A/C231A/C284S/C298A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0


proof_lines: wild-type enzyme, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0


proof_lines: mutant enzyme S266A, 25°C, 5 mM DTT, 50 mM EDTA, 50 mM NaCl, and 50 mM Tris·HCl, 0.005 mM CuSO4, pH 8.0


substrate_name: Abz-ATTPLCGPSRASILSGR

substrate: Abz-ATTPLCGPSRASILSGR


organism: Unknown

assay_conditions_summary: cofactor NADPH


substrate_name: oxidized rubredoxin

sequence_source: UniProtKB reviewed accession Q8U1K9 FASTA/JSON, accessed 2026-06-23

assay_conditions_summary: pH 8; 296.15 K; cofactor NADPH

proof_lines: pH 8, 80°C, cosubstrate: benzyl viologen

substrate: oxidized rubredoxin


organism: Entamoeba histolytica

substrate_name: oxidized Clostridium pasteurianum rubredoxin

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

proof_lines: with NADH as cosubstrate, at pH 7.0 and 30°C

proof_lines: with NADPH as cosubstrate, at pH 7.0 and 30°C


sequence_source: UniProtKB reviewed entry Q8U1K9 / NROR_PYRFU, linked to PubMed 10464233

proof_lines: pH 8.0, 80°C, cosubstrate: benzyl viologen


substrate_name: [sulfatase]-L-cysteine

proof_lines: kcat is 6.06 min(-1) with [sulfatase]-L-cysteine as substrate.

substrate: [sulfatase]-L-cysteine


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

proof_lines: kcat is 17.3 min(-1) with [sulfatase]-L-cysteine as substrate.


organism: Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 / NCIMB 10081 / Henssen B9)

substrate_name: [sulfatase]-L-cysteine (in presence of Cu(+))

proof_lines: kcat is 1.6 min(-1) in presence of Cu(+).


enzyme_display_name: phloretin hydrolase

organism: Eubacterium ramulus

substrate_name: phloretin

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

assay_conditions_summary: pH 7

enzyme: phloretin hydrolase

substrate: phloretin


organism: Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CCUG 20993 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543 / L948)

proof_lines: kcat is 0.85 sec(-1) with phloretin as substrate. kcat is 49.6 sec(-1) with MAPG as substrate.


enzyme_display_name: tartronate-semialdehyde synthase

substrate_name: Glyoxylate

sequence_source: UniProtKB:P0AEP7 canonical sequence

enzyme: tartronate-semialdehyde synthase

substrate: Glyoxylate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature I393V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tartronate-semialdehyde synthase(Enzyme) mutant I393V


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature I479V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tartronate-semialdehyde synthase(Enzyme) mutant I479V


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature I393A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tartronate-semialdehyde synthase(Enzyme) mutant I393A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature V51D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tartronate-semialdehyde synthase(Enzyme) mutant V51D


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature L478A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tartronate-semialdehyde synthase(Enzyme) mutant L478A


organism: Escherichia coli K-12

substrate_name: glyoxylate

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

substrate: glyoxylate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature V51S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature E52Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AEP7 canonical sequence reconstructed with selected mutation signature and applied mutation signature V51E to reconstruct the assayed variant sequence.


organism: Gloeomonas sp.

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


sequence_variant_note: Resolved canonical sequence from UniProt REST P0AEP7 plus residue-checked PMID 22970650 family context. and applied mutation signature I479V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I479V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P0AEP7 plus residue-checked PMID 22970650 family context. and applied mutation signature I393A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I393A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C


sequence_source: UniProt REST P0AEP7 plus residue-checked PMID 22970650 family context.

proof_lines: wild type enzyme, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P0AEP7 plus residue-checked PMID 22970650 family context. and applied mutation signature I393V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I393V, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P0AEP7 plus residue-checked PMID 22970650 family context. and applied mutation signature V51D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme V51D, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P0AEP7 plus residue-checked PMID 22970650 family context. and applied mutation signature L478A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L478A, in 50 mM KH2PO4 (pH 7.7), 0.06 M KCl, 0.1 mM thiamin diphosphate, 5 mM MgCl2, at 37°C


organism: Mus musculus


organism: Bos taurus

substrate_name: RPE65; RPE65; Retinol

sequence_source: UniProt REST direct lookup, accession Q9BGL2

substrate: RPE65; RPE65; Retinol


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

proof_lines: SABIO-RK modifier species: phosphatidylcholine---retinol O-acyltransferase(Enzyme) mutant E14L


proof_lines: SABIO-RK modifier species: phosphatidylcholine---retinol O-acyltransferase(Enzyme) mutant del1-30


sequence_source: UniProt REST direct lookup, accession Q9JI60

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


organism: Escherichia coli (strain K12)

substrate_name: malonyl-[ACP] (in the presence of dodecanoyl-[ACP])

assay_conditions_summary: cofactor CoA


organism: Escherichia coli

substrate_name: malonyl-CoA

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

assay_conditions_summary: pH 6.5; 298.15 K; cofactor CoA

proof_lines: R206G mutant protein, donor lauroyl-CoA, 0.1 mM lauroyl-CoA, pH 6.5, 25°C

substrate: malonyl-CoA


substrate_name: lauroyl-CoA

proof_lines: wild type protein, acceptor malonyl-CoA, 0.5 mM malonyl-CoA, pH 6.5, 25°C

proof_lines: wild type protein, donor lauroyl-CoA, 0.075 mM lauroyl-CoA, pH 6.5, 25°C

proof_lines: wild type protein, donor lauroyl-ACP, 0.01 mM lauroyl-ACP, pH 6.5, 25°C

substrate: lauroyl-CoA


organism: Helicobacter pylori

substrate_name: hexanoyl-[acyl-carrier protein]

proof_lines: pH and temperature not specified in the publication

substrate: hexanoyl-[acyl-carrier protein]


organism: Spinacia oleracea

substrate_name: palmitoyl-[acyl-carrier protein]

substrate: palmitoyl-[acyl-carrier protein]


substrate_name: Acetyl-[acyl-carrier protein]; Malonyl-[acyl-carrier protein]

sequence_source: UniProtKB reviewed accession P0AAI5; direct REST check on 2026-06-23


sequence_source: UniProtKB reviewed accession Q715L4; direct REST check on 2026-06-23

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

proof_lines:
pH 7.0, 37°C
recombinant enzyme, pH 7.0, 37°C


organism: Mycobacterium abscessus

substrate_name: H2O; Phloretin

proof_lines: SABIO-RK modifier species: phloretin hydrolase(Enzyme) mutant H269A N-terminally His6-tagged

substrate: H2O; Phloretin


proof_lines: SABIO-RK modifier species: phloretin hydrolase(Enzyme) mutant Y232A N-terminally His6-tagged


proof_lines: SABIO-RK modifier species: phloretin hydrolase(Enzyme) mutant H133A N-terminally His6-tagged


sequence_source: UniProtKB reviewed accession B1MK49; direct REST check on 2026-06-23


proof_lines: SABIO-RK modifier species: phloretin hydrolase(Enzyme) mutant H217A N-terminally His6-tagged


organism: Aspergillus niger


organism: Flavonifractor plautii


organism: Mycobacteroides abscessus


sequence_source: UniProtKB:B1MK49; EC and function evidence cite PMID 30784195

proof_lines: wild type enzyme, with phloretin as substrate, at pH 6.5 and 25°C

proof_lines: wild type enzyme, with monoacetylphloroglucinol as substrate, at pH 6.5 and 25°C


organism: Pantoea agglomerans


organism: Platyrrhini

substrate_name: phlorizin

substrate: phlorizin


organism: Rattus norvegicus


organism: Homo sapiens

substrate_name: all-trans-retinol

proof_lines: pH not specified in the publication, 20°C

substrate: all-trans-retinol


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

substrate_name: methyl alpha-glucoside

substrate: methyl alpha-glucoside


organism: Staphylococcus carnosus (strain TM300)

substrate_name: glucose

substrate: glucose


proof_lines: with dipalmitoylphosphatidylcholine, chemically dimerized enzyme

proof_lines: pH 7.5, 37°C, retinal pigment epithelium microsomes


organism: Gallus gallus

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA


proof_lines: with dipalmitoylphosphatidylcholine, C208A mutant


proof_lines: with dipalmitoylphosphatidylcholine, C168S mutant


proof_lines: with dipalmitoylphosphatidylcholine, C182A mutant


proof_lines: with dipalmitoylphosphatidylcholine, C161S mutant


proof_lines: with dipalmitoylphosphatidylcholine, H60Q mutant


proof_lines: with dipalmitoylphosphatidylcholine, H72Q mutant


proof_lines: with dipalmitoylphosphatidylcholine, H46Q mutant


proof_lines: pH and temperature not specified in the publication

proof_lines: with dipalmitoylphosphatidylcholine, cloned enzyme, expressed in HEK-293T cells


substrate_name: retinol-(cellular-retinol-binding protein) type II

proof_lines: intestinal LRAT, reaction with phosphatidylcholine

proof_lines: liver LRAT, reaction with phosphatidylcholine


enzyme_display_name: ethanolamine kinase

substrate_name: choline

enzyme: ethanolamine kinase

substrate: choline


organism: Caenorhabditis elegans

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


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: ethanolamine

substrate: ethanolamine


enzyme_display_name: hydroxybutyrate-dimer hydrolase

organism: Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337)

substrate_name: linear 3HB-dimer

enzyme: hydroxybutyrate-dimer hydrolase

substrate: linear 3HB-dimer


organism: Ralstonia pickettii


organism: Enterococcus faecalis

substrate_name: Protein N-phosphohistidine; Glucose

substrate: Protein N-phosphohistidine; Glucose


organism: Escherichia coli

substrate_name: D-glucose[side 1]

substrate: D-glucose[side 1]


organism: Lactococcus lactis subsp. lactis

substrate_name: D-Glucose; Protein N-phosphohistidine

proof_lines: SABIO-RK modifier species: protein-Npi-phosphohistidine---D-glucose phosphotransferase(Enzyme) mutant Lac- Gal d

substrate: D-Glucose; Protein N-phosphohistidine


substrate_name: Protein N-phosphohistidine; D-Glucose

substrate: Protein N-phosphohistidine; D-Glucose


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-mannose[side 1]

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

substrate: D-mannose[side 1]


organism: Salmonella typhimurium


organism: Staphylococcus carnosus

proof_lines: membrane-bound isoform EIICBAGlc1, at pH 7.5 and 37°C

proof_lines: membrane-bound isoform EIICBAGlc2, at pH 7.5 and 37°C

proof_lines: solubilized isoform EIICBAGlc1, at pH 7.5 and 37°C


organism: Achromobacter sp.

substrate_name: ATP

substrate: ATP


organism: Flavobacterium rhenanum


organism: Glycine max


organism: Homo sapiens


organism: Rattus norvegicus

substrate_name: ATP; Ethanolamine

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines: in presence of equivalent amounts of ATP and Mg2+, pH 8.5

substrate: ATP; Ethanolamine


organism: Saccharomyces cerevisiae


organism: Spinacia oleracea


organism: Bacillus subtilis

sequence_source: UniProtKB:P20166 direct JSON lookup from source accession P20166


organism: Streptococcus pyogenes

sequence_source: UniProtKB:Q99XX0 direct JSON lookup from source accession Q48WG5


sequence_source: UniProtKB:Q99XX0 direct JSON lookup from source accession Q48WG5; canonical sequence retained as context only

proof_lines: SABIO-RK modifier species: protein-Npi-phosphohistidine---D-glucose phosphotransferase(Enzyme) mutant deltamalE

proof_lines: SABIO-RK modifier species: protein-Npi-phosphohistidine---D-glucose phosphotransferase(Enzyme) mutant compdeltamalE

proof_lines: SABIO-RK modifier species: protein-Npi-phosphohistidine---D-glucose phosphotransferase(Enzyme) mutant deltamalT


proof_lines: SABIO-RK modifier species: protein-Npi-phosphohistidine---D-glucose phosphotransferase(Enzyme) mutant deltaM5005_spy1692

proof_lines: SABIO-RK modifier species: protein-Npi-phosphohistidine---D-glucose phosphotransferase(Enzyme) mutant compdeltaM5005_spy1692


substrate_name: Ethanolamine; ATP

sequence_source: UniProtKB:Q9Y259 direct JSON lookup from source accession Q9Y259

substrate: Ethanolamine; ATP


sequence_source: UniProtKB:P35790 direct JSON lookup from source accession P35790


organism: Plasmodium falciparum

sequence_source: UniProtKB:Q8IIB7 direct JSON lookup from source accession Q8IIB7


organism: Plasmodium falciparum 3D7


sequence_source: UniProtKB:O54783 direct JSON lookup from source accession O54783


organism: Trypanosoma brucei

sequence_source: UniProtKB:Q57W59 direct JSON lookup from source accession Q57W59

assay_conditions_summary: pH 7.8; cofactor ATP


sequence_source: UniProtKB:Q386V0 direct JSON lookup from source accession Q386V0


enzyme_display_name: NADH oxidase (H2O-forming)

organism: Lactiplantibacillus pentosus

substrate_name: BNAH

assay_conditions_summary: pH 7; 310.15 K; cofactor NADH

enzyme: NADH oxidase (H2O-forming)

substrate: BNAH


substrate_name: MNAH

substrate: MNAH


organism: Streptococcus mutans

substrate_name: NADH

sequence_source: UniProtKB direct accession lookup Q54453 (Q54453_STRMG); retrieved 2026-06-23.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: glycerate 3-kinase

organism: Arabidopsis thaliana

substrate_name: D-glycerate

sequence_source: UniProtKB direct accession lookup Q944I4 (GLYK_ARATH); retrieved 2026-06-23.

enzyme: glycerate 3-kinase

substrate: D-glycerate


substrate_name: ATP; D-Glycerate

sequence_source: UniProtKB direct accession lookup Q8IVS8 (GLCTK_HUMAN); retrieved 2026-06-23.

substrate: ATP; D-Glycerate


sequence_source: UniProtKB direct accession lookup Q0VGK3 (GLCTK_RAT); retrieved 2026-06-23.


organism: Acidovorax sp. SA1


organism: Acidovorax sp. sa1


organism: Burkholderia pickettii

sequence_source: UniProtKB direct accession lookup Q9X6X9 (HBOH2_RALPI); retrieved 2026-06-23.


organism: Cupriavidus necator

sequence_source: UniProtKB direct accession lookup Q0K9H3 (HBOH_CUPNH); retrieved 2026-06-23.


enzyme_display_name: allophanate hydrolase

organism: Candida albicans

sequence_source: UniProtKB direct accession lookup A0A1D8PDC6 (A0A1D8PDC6_CANAL); retrieved 2026-06-23.

proof_lines: pH 7.3, temperature not specified in the publication, urea amidolyase

enzyme: allophanate hydrolase


organism: Enterobacter cloacae

substrate_name: allophanate

substrate: allophanate


organism: Granulibacter bethesdensis

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q0BRB0 canonical sequence by applying Y299A/R307M; retrieved 2026-06-23. and applied mutation signature Y299A/R307M to reconstruct the assayed variant sequence.


sequence_source: UniProtKB direct accession lookup Q0BRB0 (Q0BRB0_GRABC); retrieved 2026-06-23.

proof_lines: pH 7.4, 25°C, recombinant wild-type enzyme


enzyme_display_name: aromatase

organism: Homo sapiens

substrate_name: NADPH; O2; Testosterone; H+

sequence_source: UniProtKB P11511 direct lookup; variant not reconstructed

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant D509A

enzyme: aromatase

substrate: NADPH; O2; Testosterone; H+


substrate_name: NADPH; H+; Testosterone; O2

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK S312C source note and applied mutation signature S312C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant S312C

substrate: NADPH; H+; Testosterone; O2


substrate_name: Testosterone; NADPH; H+; O2

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK D309N source note and applied mutation signature D309N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant D309N

substrate: Testosterone; NADPH; H+; O2


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK H128Q source note and applied mutation signature H128Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant H128Q


substrate_name: O2; Testosterone; H+; NADPH

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK H128A source note and applied mutation signature H128A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant H128A

substrate: O2; Testosterone; H+; NADPH


substrate_name: H+; Testosterone; NADPH; O2

sequence_source: UniProtKB P11511 canonical sequence direct lookup

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

substrate: H+; Testosterone; NADPH; O2


substrate_name: H+; O2; NADPH; Testosterone

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK C299A source note and applied mutation signature C299A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant C299A

substrate: H+; O2; NADPH; Testosterone


substrate_name: O2; H+; Androst-4-ene-3,17-dione; NADPH

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK R264C source note and applied mutation signature R264C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant R264C His-tagged

substrate: O2; H+; Androst-4-ene-3,17-dione; NADPH


substrate_name: O2; H+; NADPH; Androst-4-ene-3,17-dione

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P11511 canonical sequence plus SABIO-RK R264H source note and applied mutation signature R264H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aromatase(Enzyme) mutant R264H His-tagged

substrate: O2; H+; NADPH; Androst-4-ene-3,17-dione


organism: Anaerocolumna aminovalerica

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: H+; O2; NADH

sequence_source: UniProtKB P39662 canonical sequence direct lookup

assay_conditions_summary: cofactor NADH

substrate: H+; O2; NADH


proof_lines: kcat is 0.060 sec(-1) with androst-4-ene-3,17-dione as substrate (PubMed:20385561). kcat is 0.13 sec(-1) with 19-oxo-androst-4-ene-3,17-dione (PubMed:20385561). kcat is 0.42 sec(-1) with androst-4-ene-3,17-dione as substrate (PubMed:2038556


organism: Pseudomonas sp. (strain ADP)

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 16.4 sec(-1) for allophanate. kcat is 0.1 sec(-1) for malonamate.


organism: Bacillus subtilis

assay_conditions_summary: pH 9; 308.15 K; cofactor NADH


organism: Lacticaseibacillus rhamnosus

assay_conditions_summary: pH 5.6; 338.15 K; cofactor NADH


organism: Streptococcus pyogenes

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 7; 328.15 K; cofactor NADH


organism: Brassica rapa subsp. oleifera

assay_conditions_summary: cofactor ATP


organism: Escherichia coli


organism: Nostoc sp. PCC 7120 = FACHB-418


organism: Oryza sativa


organism: Pisum sativum

substrate_name: D-Glycerate; ATP

substrate: D-Glycerate; ATP


organism: Secale cereale


organism: Spinacia oleracea

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


organism: Zea mays

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

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


organism: Acidovorax sp.


organism: Alcaligenes faecalis


organism: Cupriavidus necator


organism: Paracoccus denitrificans


organism: Lactococcus lactis subsp. cremoris (strain MG1363)

substrate_name: beta-NADH (in the presence of oxygen)

substrate: beta-NADH (in the presence of oxygen)


organism: Streptococcus pneumoniae

substrate_name: NADH (at pH 7.4 and 30 degrees Celsius)

assay_conditions_summary: pH 7.4; cofactor NADH

substrate: NADH (at pH 7.4 and 30 degrees Celsius)


organism: Escherichia coli (strain K12)

substrate_name: glycerate

substrate: glycerate


organism: Homo sapiens


organism: Granulibacter bethesdensis

sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature R307M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature Y299A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature Y299A/R307A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature R307A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature Y299F/R307M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_reconstructed_variant and applied mutation signature Y299F to reconstruct the assayed variant sequence.


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


substrate_name: urea-1-carboxylate; allophanate

proof_lines: pH 7.3, temperature not specified in the publication, allophanate hydrolase

substrate: urea-1-carboxylate; allophanate


organism: Pseudomonas sp. strain ADP

substrate_name: malonamic acid; allophanate

assay_conditions_summary: pH 9.5; cofactor ADP

proof_lines:
pH 9.5, recombinant enzyme
Raw SKiD Env: Temp=-----, pH=9.5

substrate: malonamic acid; allophanate


organism: Saccharomyces cerevisiae

proof_lines: pH 7.3, temperature not specified in the publication, urea amidolyase


organism: Paucimonas lemoignei


organism: Pseudomonas sp.


organism: Ralstonia pickettii


organism: Zoogloea ramigera


organism: Chlamydomonas reinhardtii


organism: Oleomonas sagaranensis


organism: Pseudomonas syringae pv. tomato

proof_lines: pH 7.3, temperature not specified in the publication, allophanate hydrolase with urea carboxylase in a 1:1 molar ratio


enzyme_display_name: phosphate propanoyltransferase

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

substrate_name: propanoyl-phosphate

proof_lines: The above values were measured with a recombinant PduL fused to eight C-terminal histidine residues (PduL-His8). The Vmax values may be underestimated due to the instability of PduL-His8.

enzyme: phosphate propanoyltransferase

substrate: propanoyl-phosphate


organism: Listeria monocytogenes serotype 1/2a (strain 10403S)

substrate_name: 2-methylbutanoyl-CoA (at 30 degrees Celsius)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 27.5 min(-1) (at 30 degrees Celsius) and 2.8 min(-1) (at 10 degrees Celsius) with 2-methylbutanoyl-CoA as substrate. kcat is 19.0 min(-1) (at 30 degrees Celsius) and 6.1 min(-1) (at 10 degrees Celsius) with 2-methylpropanoyl-CoA as


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: 2-methylpropanoyl-CoA (in the presence of malonyl-FabC)

proof_lines: kcat is 17.17 min(-1) with 2-methylpropanoyl-CoA as substrate (in the presence of malonyl-FabC) (PubMed:22136753). kcat is 1.72 min(-1) with acetyl-CoA as substrate (in the presence of malonyl-FabC) (PubMed:22136753). kcat is 0.66 min(-1) w


organism: Streptomyces lividans

substrate_name: propanoyl-CoA

proof_lines: kcat is 74 min(-1) with propanoyl-CoA as substrate. kcat is 113 min(-1) with butanoyl-CoA as substrate. kcat is 58 min(-1) with acetyl-CoA as substrate.

substrate: propanoyl-CoA


substrate_name: acetyl-CoA

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

substrate: acetyl-CoA


organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)


organism: Streptomyces glaucescens

substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


enzyme_display_name: kanamycin kinase

organism: Pseudomonas aeruginosa

substrate_name: kanamycin

enzyme: kanamycin kinase

substrate: kanamycin


organism: unknown prokaryotic organism

substrate_name: Kanamycin; ATP

substrate: Kanamycin; ATP


organism: Escherichia coli

substrate_name: ATP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, isoenzyme APH3-IIIa
pH 6.5, 37°C, isoenzyme APH3-IIIa

substrate: ATP


enzyme_display_name: glycerol kinase

organism: Thermococcus kodakarensis

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

enzyme: glycerol kinase


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature K271E to reconstruct the assayed variant sequence.


organism: Trypanosoma brucei

substrate_name: Glycerol; ATP

substrate: Glycerol; ATP


organism: Trypanosoma brucei brucei

substrate_name: ADP

assay_conditions_summary: pH 6.8; buffer 0.1 M MOPS; cofactor ADP

proof_lines: in 0.1 M MOPS buffer (pH 6.8) containing 1 mM EDTA, 5 mM MgSO4, temperature not specified in the publication

substrate: ADP


organism: Trypanosoma congolense

substrate_name: sn-glycerol 3-phosphate

substrate: sn-glycerol 3-phosphate


organism: Trypanosoma vivax


organism: Enterococcus faecalis

substrate_name: Amikacin

verification_status: verified

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris pH 7; cofactor NADH

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'amikacin'; column 'K_m (uM)' = 245 ± 27; column 'k_cat (s^-1)' = 2.46 ± 0.11; column 'K_i (mM)' = nd; column 'k_cat/K_m (M^-1 s^-1)' = 1.00 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.46 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.46 s^(-1). Km: printed Table 3 cell 245 uM; 245 / 1000 = 0.245, so the paper value is 0.245 mM. kcat/Km: printed Table 3 cell 1.00 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.00 x 10^4 / 1000 = 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row amikacin: Km = 245 ± 27 uM; kcat = 2.46 ± 0.11 s^-1; printed kcat/Km = 1.00 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row amikacin

substrate: Amikacin

status: verified


assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM Tris pH 7; cofactor ATP

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'ATP'; column 'K_m (uM)' = 27.7 ± 3.7; column 'k_cat (s^-1)' = 1.76 ± 0.08; column 'K_i (mM)' = nd; column 'k_cat/K_m (M^-1 s^-1)' = 6.37 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.76 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.76 s^(-1). Km: printed Table 3 cell 27.7 uM; 27.7 / 1000 = 0.0277, so the paper value is 0.0277 mM. kcat/Km: printed Table 3 cell 6.37 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.37 x 10^4 / 1000 = 63.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row ATP: Km = 27.7 ± 3.7 uM; kcat = 1.76 ± 0.08 s^-1; printed kcat/Km = 6.37 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row ATP


substrate_name: ATP; Kanamycin A

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, recombinant enzyme, versus ATP

proof_lines: pH 7.5, 25°C, recombinant enzyme, versus kanamycin

substrate: ATP; Kanamycin A


substrate_name: Butirosin

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'butirosin'; column 'K_m (uM)' = 34.3 ± 3.1; column 'k_cat (s^-1)' = 2.02 ± 0.07; column 'K_i (mM)' = 2.17 ± 0.41; column 'k_cat/K_m (M^-1 s^-1)' = 5.87 x 10^4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.02 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.02 s^(-1). Km: printed Table 3 cell 34.3 uM; 34.3 / 1000 = 0.0343, so the paper value is 0.0343 mM. kcat/Km: printed Table 3 cell 5.87 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5.87 x 10^4 / 1000 = 58.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row butirosin: Km = 34.3 ± 3.1 uM; kcat = 2.02 ± 0.07 s^-1; printed kcat/Km = 5.87 x 10^4 M^-1 s^-1.

row_label: Table 3, substrate row butirosin

substrate: Butirosin


substrate_name: paromomycin

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'paromomycin'; column 'K_m (uM)' = 19.5 ± 3.5; column 'k_cat (s^-1)' = 3.62 ± 0.25; column 'K_i (mM)' = 0.53 ± 0.11; column 'k_cat/K_m (M^-1 s^-1)' = 1.86 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.62 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.62 s^(-1). Km: printed Table 3 cell 19.5 uM; 19.5 / 1000 = 0.0195, so the paper value is 0.0195 mM. kcat/Km: printed Table 3 cell 1.86 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.86 x 10^5 / 1000 = 186.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row paromomycin: Km = 19.5 ± 3.5 uM; kcat = 3.62 ± 0.25 s^-1; printed kcat/Km = 1.86 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row paromomycin

substrate: paromomycin


substrate_name: Kanamycin B

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'kanamycin B'; column 'K_m (uM)' = 19.4 ± 2.2; column 'k_cat (s^-1)' = 3.51 ± 0.19; column 'K_i (mM)' = nd; column 'k_cat/K_m (M^-1 s^-1)' = 1.81 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.51 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.51 s^(-1). Km: printed Table 3 cell 19.4 uM; 19.4 / 1000 = 0.0194, so the paper value is 0.0194 mM. kcat/Km: printed Table 3 cell 1.81 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.81 x 10^5 / 1000 = 181.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row kanamycin B: Km = 19.4 ± 2.2 uM; kcat = 3.51 ± 0.19 s^-1; printed kcat/Km = 1.81 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row kanamycin B

substrate: Kanamycin B


substrate_name: Lividomycin A

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'lividomycin A'; column 'K_m (uM)' = 31.6 ± 5.1; column 'k_cat (s^-1)' = 3.97 ± 0.25; column 'K_i (mM)' = 1.53 ± 0.42; column 'k_cat/K_m (M^-1 s^-1)' = 1.26 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.97 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 3.97 s^(-1). Km: printed Table 3 cell 31.6 uM; 31.6 / 1000 = 0.0316, so the paper value is 0.0316 mM. kcat/Km: printed Table 3 cell 1.26 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.26 x 10^5 / 1000 = 126.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row lividomycin A: Km = 31.6 ± 5.1 uM; kcat = 3.97 ± 0.25 s^-1; printed kcat/Km = 1.26 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row lividomycin A

substrate: Lividomycin A


substrate_name: Ribostamycin sulfate

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'ribostamycin'; column 'K_m (uM)' = 9.30 ± 1.8; column 'k_cat (s^-1)' = 1.89 ± 0.10; column 'K_i (mM)' = 1.73 ± 0.66; column 'k_cat/K_m (M^-1 s^-1)' = 2.03 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.89 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 1.89 s^(-1). Km: printed Table 3 cell 9.30 uM; 9.30 / 1000 = 0.0093, so the paper value is 0.0093 mM. kcat/Km: printed Table 3 cell 2.03 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.03 x 10^5 / 1000 = 203.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row ribostamycin: Km = 9.30 ± 1.8 uM; kcat = 1.89 ± 0.10 s^-1; printed kcat/Km = 2.03 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row ribostamycin

substrate: Ribostamycin sulfate


substrate_name: Neomycin B

column_label: Table 3: Kinetic Parameters of Purified Overexpressed APH(3')-IIIa (Biochemistry 1994, 33(22):6936-6944), substrate row 'neomycin B'; column 'K_m (uM)' = 7.72 ± 0.9; column 'k_cat (s^-1)' = 2.08 ± 0.07; column 'K_i (mM)' = 2.65 ± 0.59; column 'k_cat/K_m (M^-1 s^-1)' = 2.69 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.08 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 2.08 s^(-1). Km: printed Table 3 cell 7.72 uM; 7.72 / 1000 = 0.00772, so the paper value is 0.00772 mM. kcat/Km: printed Table 3 cell 2.69 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.69 x 10^5 / 1000 = 269.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row neomycin B: Km = 7.72 ± 0.9 uM; kcat = 2.08 ± 0.07 s^-1; printed kcat/Km = 2.69 x 10^5 M^-1 s^-1.

row_label: Table 3, substrate row neomycin B

substrate: Neomycin B


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

substrate_name: ATP (at pH 7.5 and 80 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 940 sec(-1) for glycerol (at pH 7.5 and 80 degrees Celsius).

substrate: ATP (at pH 7.5 and 80 degrees Celsius)


enzyme_display_name: glutamate N-acetyltransferase

organism: Sinorhizobium meliloti

sequence_source: UniProtKB reviewed accession Q92MJ1; REST check https://rest.uniprot.org/uniprotkb/Q92MJ1.json

enzyme: glutamate N-acetyltransferase


organism: Streptomyces clavuligerus

substrate_name: L-Glutamate; N2-Acetyl-L-ornithine

sequence_source: UniProtKB reviewed accession Q9LCS7; REST check https://rest.uniprot.org/uniprotkb/Q9LCS7.json

substrate: L-Glutamate; N2-Acetyl-L-ornithine


organism: Thermotoga neapolitana

sequence_source: UniProtKB reviewed accession Q9Z4S1; REST check https://rest.uniprot.org/uniprotkb/Q9Z4S1.json


organism: Moorella thermoacetica

substrate_name: propanoyl-CoA

assay_conditions_summary: pH 7.6; 328.15 K; cofactor CoA

substrate: propanoyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: acetyl phosphate

smiles: CC(=O)OP(=O)(O)O

substrate: acetyl phosphate


organism: Listeria monocytogenes serotype 1/2a

sequence_source: UniProtKB REST direct check 2026-06-23; accession C0LNR0; reviewed Swiss-Prot entry FABH_LISM4

assay_conditions_summary: pH 7; 283.15 K; cofactor CoA

proof_lines:
pH 7, 10°C
pH 7, 30°C


substrate_name: isobutanoyl-CoA

substrate: isobutanoyl-CoA


substrate_name: isovaleryl-CoA

substrate: isovaleryl-CoA


sequence_source: UniProtKB REST direct check 2026-06-23; accession Q54206; reviewed Swiss-Prot entry FABH_STRGA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7.2; 303.15 K; cofactor CoA

proof_lines: cosubstrate malonyl-[RedQ], pH 7.2, 30°C

proof_lines: cosubstrate isobutanoyl-CoA, pH 7.2, 30°C

proof_lines: cosubstrate malonyl-[FabC], pH 7.2, 30°C


organism: Chlamydomonas reinhardtii

substrate_name: L-glutamate

substrate: L-glutamate


organism: Chlorella vulgaris

substrate_name: alpha-N-acetyl-L-ornithine

substrate: alpha-N-acetyl-L-ornithine


organism: Citrullus lanatus

assay_conditions_summary: pH 7


organism: Geobacillus stearothermophilus


organism: Lathyrus oleraceus


organism: Methanocaldococcus jannaschii


organism: Saccharomyces cerevisiae


organism: Candida mycoderma

substrate_name: glycerol

assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP

substrate: glycerol


organism: Candida vini

substrate_name: Glycerol; ATP

assay_conditions_summary: cofactor ATP

substrate: Glycerol; ATP


organism: Cellulomonas sp.

assay_conditions_summary: pH 8.5; 303.15 K; cofactor ATP

proof_lines:
pH 8.5, 30°C
ATP at 10.5 mM Mg2+, pH 8.5, 30°C
ATP at 21 mM Mg2+, pH 8.5, 30°C


organism: Cucumis sativus

substrate_name: UTP

substrate: UTP


organism: Elizabethkingia meningoseptica

substrate_name: ATP

substrate: ATP


organism: Epidermophyton floccosum


organism: Escherichia coli

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

proof_lines: E478C mutant protein, allosteric regulation


proof_lines: E478C/T428V/R429N mutant protein, allosteric regulation


assay_conditions_summary: pH 7; 298.15 K; cofactor ATP


substrate_name: N(2)-acetyl-L-ornithine (at pH 7.0)

substrate: N(2)-acetyl-L-ornithine (at pH 7.0)


substrate_name: acetyl-CoA (AGSase activity)

substrate: acetyl-CoA (AGSase activity)


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

substrate_name: N-acetyl-L-ornithine

substrate: N-acetyl-L-ornithine


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: glutamate

substrate: glutamate


organism: Streptomyces clavuligerus

substrate_name: L-N-acetylornithine (at 37 degrees Celsius and pH 8.0)

assay_conditions_summary: pH 8


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

assay_conditions_summary: cofactor CoA


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)


organism: Homo sapiens


organism: Enterococcus casseliflavus

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP


organism: Thermococcus kodakarensis

sequence_variant_note: Resolved canonical sequence from UniProtKB:O93623 canonical sequence with row-specific K271E substitution; residue 271 checked directly from UniProt REST on 2026-06-23. and applied mutation signature K271E to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant enzyme mutant K271E


sequence_source: UniProtKB:O93623 canonical FASTA; RCSB SIFTS structure entries align to O93623 for Thermococcus kodakarensis glycerol kinase.


enzyme_display_name: 15-cis-phytoene synthase

organism: Capsicum annuum

substrate_name: geranylgeranyl diphosphate

enzyme: 15-cis-phytoene synthase

substrate: geranylgeranyl diphosphate


organism: Pantoea ananas

substrate_name: GGPP (at pH 8 and 37 degrees Celsius)

substrate: GGPP (at pH 8 and 37 degrees Celsius)


organism: Citrullus lanatus

substrate_name: L-Glutamate; N2-Acetyl-L-ornithine

sequence_source: UniProtKB:Q3C251 direct lookup

substrate: L-Glutamate; N2-Acetyl-L-ornithine


organism: Geobacillus stearothermophilus

sequence_source: UniProtKB:Q07908 direct lookup


organism: Methanocaldococcus jannaschii

substrate_name: N2-Acetyl-L-ornithine; L-Glutamate

sequence_source: UniProtKB:Q57645 direct lookup

substrate: N2-Acetyl-L-ornithine; L-Glutamate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WPZ3 direct lookup

proof_lines: pH and temperature not specified in the publication, versus 1 mM of N2-acetyl-L-ornithine


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:Q04728 direct lookup


sequence_source: UniProtKB:Q9M8L4 direct lookup


organism: Bombyx mori

sequence_source: UniProtKB:B0I1G6 direct lookup

assay_conditions_summary: 278.15 K; cofactor ATP

proof_lines: enzyme source: crude extract from diapause eggs exposed to 5°C for 200 days, Bombyx mori has 3 glycerol kinase genes


organism: Cellulomonas sp.


proof_lines: mutant enzyme T386I/F388Y, at pH 7.5 and 37°C


proof_lines: mutant enzyme A344V/T386I/F388Y, at pH 7.5 and 37°C


smiles: OCC(O)CO


organism: Cucumis sativus

substrate_name: ATP; Glycerol

sequence_source: UniProtKB:A0A0A0KA32 direct lookup

substrate: ATP; Glycerol


organism: Enterococcus faecalis

sequence_source: UniProtKB:O34154 direct lookup


organism: Plasmodium falciparum

sequence_source: UniProtKB:Q8IDI4 direct lookup


organism: Capsicum sp.

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


organism: Solanum lycopersicum

proof_lines: pH 8.0, 28°C, chloroplast enzyme and chromoplast enzyme


organism: Escherichia coli

substrate_name: dihydroxyacetone

proof_lines:
pH 7.0, 25°C
25°C, plus D-glyceraldehyde
ATP in form of MgATP2-

substrate: dihydroxyacetone


organism: Gallus gallus

proof_lines:
and also 0.22 mM, 30°C
and also 0.025 mM, 30°C


organism: Haemophilus influenzae

proof_lines:
and also 2.5 mM, pH 7.0, 25°C
and also 0.045 mM, pH 7.0, 25°C


organism: Mus musculus

proof_lines:
and also 1.5 mM, 30°C
and also 0.04 mM, 30°C


organism: Pediococcus pentosaceus


organism: Rattus norvegicus

proof_lines:
and also 1.26 mM, 30°C
pH 7.35, 37°C
and also 0.02 mM, 30°C


organism: Thermococcus kodakarensis

assay_conditions_summary: pH 8; 353.15 K; cofactor ATP


organism: Thermus thermophilus


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP


organism: Trypanosoma brucei gambiense

substrate_name: ADP

assay_conditions_summary: pH 6.8; 310.15 K; cofactor ADP

substrate: ADP


enzyme_display_name: lysozyme

proof_lines: human serum albumin-bound enzyme, pH 5.2, 37°C

enzyme: lysozyme


organism: Homo sapiens


organism: Liolophura japonica


organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

substrate_name: Unknown

substrate: Unknown


organism: Ruditapes philippinarum

substrate_name: p-nitrophenyl beta 1,4-linked pentamer of N-acetyl-D-glucosamine ((GlcNAc)5-PNP) at pH 5 and 40 degrees Celsius

assay_conditions_summary: pH 5


enzyme_display_name: deoxynogalonate monooxygenase

organism: Streptomyces nogalater

substrate_name: dithranol

proof_lines: kcat is 1.5 sec(-1) for monooxygenase activity with dithranol as substrate.

enzyme: deoxynogalonate monooxygenase

substrate: dithranol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature N63A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'Asn63Ala'; column 'Vmax (umol min^-1 mg^-1)' = 0.07; column 'relative Vmax (%)' = 1.1; column 'kcat (s^-1)' = 0.02; column 'KM (uM)' = 68; column 'kcat/KM (M^-1 s^-1)' = 2.3 x 10^2. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.02 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.02 s^(-1). Km: printed Table 3 cell 68 in a column headed KM (uM); 1 uM is 0.001 mM, so 68 / 1000 = 0.068 mM. kcat/Km: printed Table 3 cell 2.3 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 229.99999999999997 / 1000 = 0.22999999999999998 s^-1 mM^-1. The catalog values for this identity are kcat 0.02 s^(-1), Km 0.068 mM; this identity stores no kcat_over_km field.

raw_value_unit_evidence: Table 3, printed enzyme line 'Asn63Ala': kcat = 0.02 s^-1; KM = 68 uM; printed kcat/KM = 2.3 x 10^2 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'Asn63Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature H49A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'His49Ala'; column 'Vmax (umol min^-1 mg^-1)' = 1.3; column 'relative Vmax (%)' = 20.6; column 'kcat (s^-1)' = 0.3; column 'KM (uM)' = 150; column 'kcat/KM (M^-1 s^-1)' = 2.0 x 10^3. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.3 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.3 s^(-1). Km: printed Table 3 cell 150 in a column headed KM (uM); 1 uM is 0.001 mM, so 150 / 1000 = 0.15 mM. kcat/Km: printed Table 3 cell 2.0 x 10^3 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000.0 / 1000 = 2.0 s^-1 mM^-1. The catalog values for this identity are kcat 0.3 s^(-1), Km 0.15 mM; this identity stores no kcat_over_km field.

raw_value_unit_evidence: Table 3, printed enzyme line 'His49Ala': kcat = 0.3 s^-1; KM = 150 uM; printed kcat/KM = 2.0 x 10^3 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'His49Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O54259 and applied mutation signature N18A to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'Asn18Ala'; column 'Vmax (umol min^-1 mg^-1)' = 0.1; column 'relative Vmax (%)' = 1.6; column 'kcat (s^-1)' = 0.03; column 'KM (uM)' = 120; column 'kcat/KM (M^-1 s^-1)' = 2.2 x 10^2. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.03 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.03 s^(-1). Km: printed Table 3 cell 120 in a column headed KM (uM); 1 uM is 0.001 mM, so 120 / 1000 = 0.12 mM. kcat/Km: printed Table 3 cell 2.2 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 220.00000000000003 / 1000 = 0.22000000000000003 s^-1 mM^-1. The catalog values for this identity are kcat 0.03 s^(-1), Km 0.12 mM and kcat_over_km 0.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed enzyme line 'Asn18Ala': kcat = 0.03 s^-1; KM = 120 uM; printed kcat/KM = 2.2 x 10^2 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'Asn18Ala'


sequence_variant_note: Resolved canonical sequence from UniProt O54259 FASTA direct lookup plus validated R90E substitution on the canonical sequence. and applied mutation signature R90E to reconstruct the assayed variant sequence.


normalized_value_unit_evidence: kcat: printed Table 3 cell 0.03 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.03 s^(-1). Km: printed Table 3 cell 120 in a column headed KM (uM); 1 uM is 0.001 mM, so 120 / 1000 = 0.12 mM. kcat/Km: printed Table 3 cell 2.2 x 10^2 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 220.00000000000003 / 1000 = 0.22000000000000003 s^-1 mM^-1. The catalog values for this identity are kcat 0.03 s^(-1), Km 0.12 mM; this identity stores no kcat_over_km field.

table_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1).


normalized_value_unit_evidence: kcat: printed Table 3 cell 0.3 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.3 s^(-1). Km: printed Table 3 cell 150 in a column headed KM (uM); 1 uM is 0.001 mM, so 150 / 1000 = 0.15 mM. kcat/Km: printed Table 3 cell 2.0 x 10^3 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000.0 / 1000 = 2.0 s^-1 mM^-1. The catalog values for this identity are kcat 0.3 s^(-1), Km 0.15 mM and kcat_over_km 2.0 s^(-1)*mM^(-1).


sequence_source: UniProt O54259 FASTA direct lookup.

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

column_label: Table 3: Kinetic Parameters of Wild-Type and Mutant SnoaB (Biochemistry 2010, 49(5):934-944). Printed column heads: SnoaB variants; Vmax (umol min^-1 mg^-1); relative Vmax (%); kcat (s^-1); KM (uM); kcat/KM (M^-1 s^-1). Printed enzyme line 'SnoaB-N'; column 'Vmax (umol min^-1 mg^-1)' = 6.3; column 'relative Vmax (%)' = 100; column 'kcat (s^-1)' = 1.5; column 'KM (uM)' = 140; column 'kcat/KM (M^-1 s^-1)' = 1.1 x 10^4. The value printed after the plus/minus sign beside the Vmax and KM cells of this line is the printed standard error and is not a catalog metric.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.5 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.5 s^(-1). Km: printed Table 3 cell 140 in a column headed KM (uM); 1 uM is 0.001 mM, so 140 / 1000 = 0.14 mM. kcat/Km: printed Table 3 cell 1.1 x 10^4 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11000.0 / 1000 = 11.0 s^-1 mM^-1. The catalog values for this identity are kcat 1.5 s^(-1), Km 0.14 mM and kcat_over_km 10.714285714285714 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, printed enzyme line 'SnoaB-N': kcat = 1.5 s^-1; KM = 140 uM; printed kcat/KM = 1.1 x 10^4 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 3, printed enzyme line 'SnoaB-N'