enzyme_display_name: DNA-3-methyladenine glycosylase II

substrate_name: duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine

assay_conditions_summary: pH 6.1; 310.15 K; buffer 50 mM Na-MES

proof_lines: at 37°C, in 50 mM Na-MES buffer (pH 6.1)

proof_lines: pH 8.0, 37°C, excision of 5-formyluracil

proof_lines: pH 8.0, 37°C, excision of 7-methylguanine

enzyme: DNA-3-methyladenine glycosylase II


organism: Homo sapiens

substrate_name: 1,N6-ethenoadenine residues in alkylated DNA

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: pH 7.5, 37°C, excision of1, N6-ethenoadenine

proof_lines: pH 7.5, 37°C, excision of 1, N6-ethenoadenine

source: brenda


organism: Mus musculus

kcat_display: Not reported

proof_lines:
37°C, pH 7.9
37°C, pH 7.9, presence of 250 mM Mg2+
37°C, pH 7.9, presence of 500 mM Mg2+

substrate: duplex oligonucleotide substrate containing ethenoadenine and hypoxanthine


mutation_type: deletion

proof_lines: pH 8.3, 37°C, release of 1,N6-ethenoadenine, truncated mutant N-DELTA100C-DELTA18

substrate: 1,N6-ethenoadenine residues in alkylated DNA


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

proof_lines: pH 8.3, 37°C, release of 1,N6-ethenoadenine, wild-type

proof_lines: pH 8.3, 37°C, release of 1,N6-ethenoadenine, wild type enzyme


enzyme_display_name: peptidyl-dipeptidase Dcp

organism: Escherichia coli

enzyme: peptidyl-dipeptidase Dcp


enzyme_display_name: muramoylpentapeptide carboxypeptidase

organism: Bacillus subtilis

enzyme: muramoylpentapeptide carboxypeptidase


organism: Enterococcus faecalis

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


organism: Bifidobacterium bifidum

protein_accession_database: UniProt

mutation_type: substitution


organism: Clostridium perfringens


organism: Prunus dulcis


organism: Tannerella forsythia

substrate_name: 4-nitrophenyl alpha-L-fucopyranoside

substrate: 4-nitrophenyl alpha-L-fucopyranoside


enzyme_display_name: isoamylase

organism: Lederbergia lenta

substrate_name: glycogen

km_display: Not reported

enzyme: isoamylase

substrate: glycogen


organism: Bos taurus

substrate_name: nitrocatechol sulfate

substrate: nitrocatechol sulfate


organism: Gallus gallus

substrate_name: UDP-N-acetylgalactosamine 4-sulfate

substrate: UDP-N-acetylgalactosamine 4-sulfate


substrate_name: 4-Methylumbelliferyl sulfate

substrate: 4-Methylumbelliferyl sulfate


substrate_name: p-nitrocatechol sulfate

proof_lines: pH 6.0, 37°C, Schistosoma-infected animals

substrate: p-nitrocatechol sulfate


organism: Rattus norvegicus


enzyme_display_name: (R)-specific secondary-alkylsulfatase (type III)

organism: Pseudomonas sp.

substrate_name: (5R)-nonan-5-yl sulfate

substrate: (5R)-nonan-5-yl sulfate


enzyme_display_name: beta-primeverosidase

organism: Aspergillus fumigatus

enzyme: beta-primeverosidase


organism: Camellia sinensis

substrate_name: 2-phenylethyl beta-vicianoside

substrate: 2-phenylethyl beta-vicianoside


organism: Penicillium multicolor

substrate_name: p-nitrophenyl beta-primeveroside

substrate: p-nitrophenyl beta-primeveroside


organism: Aspergillus niger


organism: Bacillus fulminans


enzyme_display_name: deoxyribonuclease I

organism: Basidiobolus haptosporus

substrate_name: Unknown

ki_unit: mM

enzyme: deoxyribonuclease I

substrate: Unknown


organism: Cyprinus carpio


organism: Homo sapiens

substrate_name: d(pGpGpCpApCpTpTpApC)

proof_lines: 20 mM Tris-HCl pH 7.5, 5 mM MgCl2, 1 mM EDTA, 37°C

substrate: d(pGpGpCpApCpTpTpApC)


organism: Potyvirus sp.

substrate_name: lambda phage DNA

substrate: lambda phage DNA


enzyme_display_name: Aspergillus nuclease S1

organism: Aspergillus oryzae

enzyme: Aspergillus nuclease S1


substrate_name: denaturated DNA

substrate: denaturated DNA


organism: Neurospora crassa


organism: Aquarana catesbeiana

substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


organism: Echinococcus granulosus

proof_lines: pH and temperature not specified in the publication


organism: Enterobacter asburiae

assay_conditions_summary: pH 3.5; 310.15 K; cofactor ATP

proof_lines: K0.5 value, Hill coefficient 1.2, pH 3.5, 37°C

proof_lines: K0.5 value, Hill coefficient 1.6, pH 3.5, 37°C

proof_lines: K0.5 value, Hill coefficient 2.3, pH 3.5, 37°C


organism: Escherichia coli

proof_lines: about, pH 7.8, 37°C, inhibition of 4-nitrophenyl phosphatase activity


organism: Fasciola gigantica


organism: Joyeuxiella pasqualei


organism: Leishmania donovani


organism: Leishmania tropica


organism: Macrobrachium olfersii

substrate_name: K+

proof_lines:
pH 7.5, 25°C, 21% salinity
pH 7.5, 25°C, fresh water
pH 7.5, 25°C

substrate: K+


organism: Moniezia expansa


organism: Rattus norvegicus

substrate_name: H2O; 4-Nitrophenyl phosphate

substrate: H2O; 4-Nitrophenyl phosphate


organism: Rodentolepis nana


organism: Toxocara cati


proof_lines: in the presence of 5 mM MgCl2, 0.5 mM EGTA, 50 mM Tris, pH 7.4, temperature not specified in the publication


organism: Trypanosoma brucei

proof_lines: mutant enzyme D360A/N362A, at pH 7.5 and 25°C


organism: Enterococcus gallinarum


organism: Priestia megaterium


organism: Streptomyces albus

substrate_name: diacetyl-L-diaminobutyryl-D-Ala-D-Ala

substrate: diacetyl-L-diaminobutyryl-D-Ala-D-Ala


organism: Streptomyces sp.


enzyme_display_name: cathepsin X

organism: Bos taurus

substrate_name: glucagon

enzyme: cathepsin X

substrate: glucagon


organism: Homo sapiens


substrate_name: hippuryl-L-Arg

substrate: hippuryl-L-Arg


enzyme_display_name: kallikrein 13

substrate_name: Abz-KLKSSKQ-EDDnp

proof_lines: in the presence of 0.0005 mM heparin, in 50 mM Tris, 1 mM EDTA, pH 7.5, at 37°C

proof_lines: in the presence of 1.4 M sodium citrate, in 50 mM Tris, 1 mM EDTA, pH 7.5, at 37°C

enzyme: kallikrein 13

substrate: Abz-KLKSSKQ-EDDnp


enzyme_display_name: caricain

organism: Carica papaya

substrate_name: Succinyl-albumin

enzyme: caricain

substrate: Succinyl-albumin


enzyme_display_name: gingipain R

organism: Porphyromonas gingivalis

substrate_name: prothrombin

proof_lines: HRgpA, pH 7.6, 37°C, in presence of Ca2+ and phospholipids

proof_lines: RgpB, pH 7.6, 37°C, in presence of Ca2+ and phospholipids

enzyme: gingipain R

substrate: prothrombin


enzyme_display_name: staphopain

organism: Staphylococcus aureus

substrate_name: N-Suc-Gly-Phe-Gly-p-nitroanilide

proof_lines: used for inhibition studies of staphopain identified from a novel staphylococcal thiol protease operon stpAB2CH-91

enzyme: staphopain

substrate: N-Suc-Gly-Phe-Gly-p-nitroanilide


organism: Lederbergia lenta

substrate_name: glycogen

substrate: glycogen


organism: Oryza sativa

substrate_name: amylopectin

substrate: amylopectin


organism: Rhizopus arrhizus


enzyme_display_name: inosine nucleosidase

organism: Arabidopsis thaliana

substrate_name: uridine

proof_lines: recombinant enzyme expressed in Escherichia coli

enzyme: inosine nucleosidase

substrate: uridine


enzyme_display_name: chymopapain

proof_lines: at pH 7.4, in 100 mM phosphate-buffered saline

enzyme: chymopapain


enzyme_display_name: asclepain

organism: Asclepias curassavica

assay_conditions_summary: pH 8; 310.15 K; buffer 0.1 M Tris-HCl

proof_lines: at 37°C, in 0.1 M Tris-HCl buffer (pH 8.0) containing 2 mM EDTA and 25 mM cysteine

enzyme: asclepain


organism: Asclepias syriaca

substrate_name: N-carbobenzoxy-Lys p-nitrophenyl ester

proof_lines:
asclepain A5
asclepain A2
asclepain B5

substrate: N-carbobenzoxy-Lys p-nitrophenyl ester


enzyme_display_name: gastricsin

enzyme: gastricsin


organism: Sus scrofa

proof_lines:
Km-value for the range 0.025-0.15 mM
Km-value for the range 0.1-0.5 mM
Km-value for the range 0.1-2.0 mM


enzyme_display_name: phytepsin

organism: Cynara cardunculus

enzyme: phytepsin


organism: Cynara cardunculus var. scolymus

assay_conditions_summary: pH 5


organism: Triticum aestivum


enzyme_display_name: leishmanolysin

organism: Leishmania sp.

substrate_name: Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr

enzyme: leishmanolysin

substrate: Leu-Ile-Ala-Tyr-Leu-Lys-Lys-Ala-Thr


enzyme_display_name: intramembrane prenyl-peptidase Rce1

organism: Saccharomyces cerevisiae

substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

enzyme: intramembrane prenyl-peptidase Rce1

substrate: Unknown


enzyme_display_name: N-acetylmuramoyl-L-alanine amidase

organism: Citrobacter freundii

assay_conditions_summary: pH 7

proof_lines: at pH 7.0, temperature not specified in the publication

enzyme: N-acetylmuramoyl-L-alanine amidase


organism: Escherichia coli


assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer (pH7.0) at 37°C


organism: Saccharolobus solfataricus

substrate_name: maize amylopectin

substrate: maize amylopectin


organism: Homo sapiens


organism: Mus musculus


organism: Staphylococcus epidermidis


organism: Streptomyces globisporus


enzyme_display_name: glutamin-(asparagin-)ase

organism: Achromobacter sp.

substrate_name: L-glutamine

enzyme: glutamin-(asparagin-)ase

substrate: L-glutamine


organism: Acinetobacter glutaminasificans

proof_lines: competitive inhibition of glutaminase activity


organism: Aspergillus niger

substrate_name: L-asparagine

substrate: L-asparagine


proof_lines:
asparaginase B
asparaginase A


organism: Delftia acidovorans


organism: Pseudomonas sp.


organism: Rhodotorula toruloides

substrate_name: N-carbamoyl-L-asparagine

substrate: N-carbamoyl-L-asparagine


organism: Streptomyces canarius

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


organism: Tilachlidium humicola

proof_lines: mixed type of competitive and non-competitive inhibition


organism: Mus sp.

substrate_name: oleamide

substrate: oleamide


organism: Rattus norvegicus

substrate_name: N-oleoylethanolamine

proof_lines:
mitochondrial enzyme
mitochondrial

substrate: N-oleoylethanolamine


enzyme_display_name: acetylputrescine deacetylase

organism: Micrococcus luteus

substrate_name: N-acetylputrescine

enzyme: acetylputrescine deacetylase

substrate: N-acetylputrescine


enzyme_display_name: urethanase

organism: Bacillus licheniformis

substrate_name: urethane

proof_lines:
strain IFO 12107
strain 1013, at pH 7.5
strain 1013, at pH 4.5

enzyme: urethanase

substrate: urethane


organism: Citrobacter sp.


organism: Micrococcus sp.


organism: Paenibacillus thiaminolyticus


organism: Prescottella equi


organism: Purpureocillium lilacinum


organism: Talaromyces variabilis


enzyme_display_name: acyl-homoserine-lactone acylase

organism: Delftia sp. VM4

substrate_name: N-3-oxo-hexanoyl-L-homoserine lactone

enzyme: acyl-homoserine-lactone acylase

substrate: N-3-oxo-hexanoyl-L-homoserine lactone


enzyme_display_name: L-tryptophan decarboxylase

organism: Bacillus sp. (in: firmicutes)

substrate_name: L-tryptophan

enzyme: L-tryptophan decarboxylase

substrate: L-tryptophan


organism: Camptotheca acuminata


organism: Catharanthus roseus

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


organism: Gelatoporia subvermispora


organism: Vinca minor


organism: Withania coagulans


organism: Felis catus


organism: Homo sapiens

proof_lines: in 50 mM 4-morpholinepropanesulfonic acid, pH 6.0, at 25°C


organism: Pseudomonas fluorescens

assay_conditions_summary: pH 7; buffer pH 7

proof_lines: alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Mn2+

proof_lines: alpha-amino-beta-carboxymuconate-epsilon-semialdehyde decarboxylase loaded with 1 molar equivalent Cd2+

proof_lines: in 25 mM HEPES buffer pH 7.0, the enzyme contains Co2+


assay_conditions_summary: pH 7; 295.15 K; buffer containing 5% glycerol, pH 7

proof_lines: mutant enzyme H228A, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt Q83V25 ACMSD_PSEFL, supported by RCSB 4IFK/4IFO/4IFR/4IG2 and PMID 24019523 family context and applied mutation signature H177A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H177A, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt Q83V25 ACMSD_PSEFL, supported by RCSB 4IFK/4IFO/4IFR/4IG2 and PMID 24019523 family context and applied mutation signature H9E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H9E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt Q83V25 ACMSD_PSEFL, supported by RCSB 4IFK/4IFO/4IFR/4IG2 and PMID 24019523 family context and applied mutation signature D294E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D294E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C


sequence_variant_note: Resolved canonical sequence from UniProt Q83V25 ACMSD_PSEFL, supported by RCSB 4IFK/4IFO/4IFR/4IG2 and PMID 24019523 family context and applied mutation signature H228E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H228E, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C


sequence_source: UniProt Q83V25 ACMSD_PSEFL, supported by RCSB 4IFK/4IFO/4IFR/4IG2 and PMID 24019523

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

proof_lines: wild type enzyme, in 25 mM HEPES buffer containing 5% glycerol, pH 7.0, at 22°C


organism: Sus scrofa


enzyme_display_name: phosphonopyruvate decarboxylase

organism: Bacteroides fragilis

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

enzyme: phosphonopyruvate decarboxylase


enzyme_display_name: 2-hydroxyacyl-CoA lyase

organism: Listeria monocytogenes

substrate_name: formaldehyde

enzyme: 2-hydroxyacyl-CoA lyase

substrate: formaldehyde


enzyme_display_name: trans-L-3-hydroxyproline dehydratase

organism: Azospirillum brasilense

enzyme: trans-L-3-hydroxyproline dehydratase


organism: Rattus norvegicus


enzyme_display_name: 4-oxalmesaconate hydratase

organism: Phytopseudomonas straminea

enzyme: 4-oxalmesaconate hydratase


organism: Pseudomonas aeruginosa

substrate_name: N-octanoyl-L-homoserine lactone

proof_lines: in 0.1 M phosphate buffer pH 7.4, at 30°C

substrate: N-octanoyl-L-homoserine lactone


enzyme_display_name: 6-aminohexanoate-cyclic-dimer hydrolase

organism: Flavobacterium sp.

enzyme: 6-aminohexanoate-cyclic-dimer hydrolase


organism: Paenarthrobacter ureafaciens

substrate_name: 6-amino-hexanoate cyclic dimer

verification_status: corrected

sequence_source: UniProtKB:P13398; RCSB 3A2P/3A2Q SIFTS mapping to P13398; PMID 19889645 Table 3

data_origin: experimental

substrate: 6-amino-hexanoate cyclic dimer

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13398; RCSB 3A2P/3A2Q SIFTS mapping to P13398; PMID 19889645 Table 3 and applied mutation signature N125A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13398; RCSB 3A2P/3A2Q SIFTS mapping to P13398; PMID 19889645 Table 3 and applied mutation signature C316G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13398; RCSB 3A2P/3A2Q SIFTS mapping to P13398; PMID 19889645 Table 3 and applied mutation signature C316S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13398; RCSB 3A2P/3A2Q SIFTS mapping to P13398; PMID 19889645 Table 3 and applied mutation signature C316D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13398; RCSB 3A2P/3A2Q SIFTS mapping to P13398; PMID 19889645 Table 3 and applied mutation signature C316A to reconstruct the assayed variant sequence.


organism: Pseudomonas sp.


enzyme_display_name: arginine dihydrolase

organism: Streptomyces sp.

substrate_name: L-arginine

enzyme: arginine dihydrolase

substrate: L-arginine


substrate_name: L-citrulline

substrate: L-citrulline


enzyme_display_name: diacylglycerol diphosphate phosphatase

organism: Saccharomyces cerevisiae

substrate_name: diacylglycerol diphosphate

enzyme: diacylglycerol diphosphate phosphatase

substrate: diacylglycerol diphosphate


enzyme_display_name: phenylalanine 3-monooxygenase

organism: Streptomyces coeruleorubidus

substrate_name: L-phenylalanine

proof_lines: pH 8.0, 28°C, cofactor: 6-methyl-5,6,7,8-tetrahydropterin

proof_lines: pH 8.0, 28°C, cofactor: 6,7-dimethyl-5,6,7,8-tetrahydropterin

enzyme: phenylalanine 3-monooxygenase

substrate: L-phenylalanine


source_db: uniprot

assay_conditions_summary: pH 3

proof_lines: kcat is 1.3 min(-1) for L-phenylalanine as substrate. kcat is 1.2 min(-1) for 6-methyltetrahydropterin as substrate.

source: uniprot


enzyme_display_name: HslU--HslV peptidase

organism: Escherichia coli (strain K12)

substrate_name: Arc-MYL-st11 (at 37 degrees Celsius)

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

assay_conditions_summary: cofactor ATP

proof_lines: Arc is a repressor protein, Arc-MYL-st11 is a hyperstable variant of Arc.

enzyme: HslU--HslV peptidase

substrate: Arc-MYL-st11 (at 37 degrees Celsius)


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

proof_lines: Arc-H(6)-SulA(CT) is a construct consisting of the Arc repressor protein fused to 6 His residues and the 11 carboxy terminal residues of SulA.


protein_accession_database: NCBI Protein

sequence_variant_note: Resolved canonical sequence from genbank_protein_reconstructed_variant:BAB21455.1:C186S and applied mutation signature C186S to reconstruct the assayed variant sequence.


organism: Escherichia coli

substrate_name: Arc-MYL-st11 plus

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
pH 7.6, 37°C, HslUV
pH 8, 37°C

substrate: Arc-MYL-st11 plus


proof_lines: deletion mutant DELTA175-209linker, pH 7.6, 37°C


organism: Haemophilus influenzae

substrate_name: SulA

proof_lines: pH 5.5, 37°C, wild-type SulA, recombinant enzyme

substrate: SulA


substrate_name: SulA mutant P8L

substrate: SulA mutant P8L


enzyme_display_name: MMP alpha-(1->4)-mannosyltransferase

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

substrate_name: sMetMan(4) (at 37 degrees Celsius)

proof_lines: kcat is 0.047 sec(-1) with sMetMan(4) as substrate (at 37 degrees Celsius). kcat is 0.025 sec(-1) with sMan(4) as substrate (at 37 degrees Celsius). kcat is 0.048 sec(-1) with GDP-mannose as substrate (in the presence of sMetMan(4), at 37 d

enzyme: MMP alpha-(1->4)-mannosyltransferase

substrate: sMetMan(4) (at 37 degrees Celsius)


organism: Mycolicibacterium hassiacum

sequence_variant_note: Resolved canonical sequence from UniProtKB:K5BE02 REST lookup on 2026-07-08 plus E313A reconstruction; RCSB 7QSG SIFTS maps the structure entity to K5BE02. and applied mutation signature E313A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E313A, with propyl-alpha-D-mannopyranosyl-(1->4)-3-O-methyl-alpha-D-mannopyranosyl-(1->4)-3-O-methyl-alpha-D-mannopyranoside as cosubstrate, at pH 8.5 and 37Â°C

proof_lines: mutant enzyme E313A, at pH 8.5 and 37Â°C


substrate_name: GDP-alpha-D-mannose; sMetMan4; sMan4

sequence_source: UniProtKB:K5BE02 REST lookup on 2026-07-08; RCSB 7QSG SIFTS maps the structure entity to K5BE02.

proof_lines: wild type enzyme, with propyl-alpha-D-mannopyranosyl-(1->4)-alpha-D-mannopyranosyl-(1->4)-alpha-D-mannopyranosyl-(1->4)-alpha-D-mannopyranoside as cosubstrate, at pH 8.5 and 45Â°C

proof_lines: wild type enzyme, with propyl-alpha-D-mannopyranosyl-(1->4)-3-O-methyl-alpha-D-mannopyranosyl-(1->4)-3-O-methyl-alpha-D-mannopyranoside as cosubstrate, at pH 8.5 and 45Â°C

substrate: GDP-alpha-D-mannose; sMetMan4; sMan4


organism: Mycolicibacterium smegmatis

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


enzyme_display_name: tyrosine--arginine ligase

organism: Homo sapiens

substrate_name: L-tyrosine

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication

proof_lines: pH 7.4, 37°C, recombinant His-tagged enzyme

enzyme: tyrosine--arginine ligase

substrate: L-tyrosine


organism: Rattus norvegicus

substrate_name: ATP; L-Arginine; L-Tyrosine

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines:
37°C, pH 8.0, enzyme from adrenal gland
37°C, pH 8.0, enzyme from spinal cord
37°C, pH 8.0

substrate: ATP; L-Arginine; L-Tyrosine


enzyme_display_name: glucosyl-3-phosphoglycerate phosphatase

organism: Persephonella marina

enzyme: glucosyl-3-phosphoglycerate phosphatase


organism: Thermus thermophilus


enzyme_display_name: neopullulanase

organism: uncultured microorganism

substrate_name: pullulan

proof_lines: optimal pH 7.0, optimal temperature 75°C

enzyme: neopullulanase

substrate: pullulan


enzyme_display_name: phosphomevalonate decarboxylase

organism: Anaerolinea thermophila

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: phosphomevalonate decarboxylase


organism: Haloferax volcanii

substrate_name: mevalonate 5-phosphate

substrate: mevalonate 5-phosphate


organism: Methanococcoides burtonii


organism: Geobacillus stearothermophilus


organism: Ruminococcus bromii


organism: Thermoanaerobacter ethanolicus


enzyme_display_name: deuterolysin

organism: Aspergillus oryzae

proof_lines: pH 9.0, 30°C, Co-substituted deuterolysin

enzyme: deuterolysin


organism: Bacillus sp

substrate_name: alpha-cyclodextrin (at pH 7.0 and 50 degrees Celsius)

proof_lines: kcat is 78.18 sec(-1) with beta-cyclodextrin as substrate. kcat is 22.11 sec(-1) with amylose as substrate. kcat is 50.36 sec(-1) with amylopectin as substrate (PubMed:16536613). kcat is 101 min(-1) for dimeric form of the enzyme with beta-


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)


enzyme_display_name: glutamate--prephenate aminotransferase

organism: Sorghum bicolor x Sorghum sudanesis

substrate_name: prephenate

assay_conditions_summary: pH 8

enzyme: glutamate--prephenate aminotransferase

substrate: prephenate


organism: Arabidopsis thaliana

substrate_name: L-glutamate

substrate: L-glutamate


organism: Sinorhizobium meliloti


organism: Streptomyces avermitilis

proof_lines: cosubstrate N-succinyl-L-2,6-diaminoheptanedioate, pH 8.0, 30°C


organism: Synechocystis sp.


substrate_name: aspartate for the asparte aminotransferase activity


organism: Petunia hybrida

substrate_name: prephenate (with 20 mM aspartate as cosubstrate)


organism: Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)

substrate_name: GPG (at 30 degrees Celsius)

substrate: GPG (at 30 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: glucosyl-3-phosphoglycerate (at 37 degrees Celsius)


organism: Persephonella marina (strain DSM 14350 / EX-H1)

substrate_name: GPG (at 70 degrees Celsius)

substrate: GPG (at 70 degrees Celsius)


enzyme_display_name: anthocyanin 6''-O-malonyltransferase

organism: Pericallis cruenta

substrate_name: malonyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: anthocyanin 6''-O-malonyltransferase

substrate: malonyl-CoA


enzyme_display_name: glutaredoxin-dependent peroxiredoxin

organism: Mus musculus

substrate_name: glutaredoxin 2

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: glutaredoxin-dependent peroxiredoxin

substrate: glutaredoxin 2


organism: Thermotoga maritima

assay_conditions_summary: cofactor NADH


enzyme_display_name: dissimilatory sulfite reductase

organism: Archaeoglobus fulgidus

substrate_name: sulfite

proof_lines: in the presence of DsrC, at pH 7.0 and 60Â°C

proof_lines: in the presence of DsrD, at pH 7.0 and 60Â°C

proof_lines: in the absence of DsrD, at pH 7.0 and 60Â°C

enzyme: dissimilatory sulfite reductase

substrate: sulfite


substrate_name: Unknown

substrate: Unknown


organism: Populus trichocarpa

substrate_name: phosphatidylcholine hydroperoxide

substrate: phosphatidylcholine hydroperoxide


organism: Dahlia pinnata


organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough)

proof_lines: kcat is 0.31 sec(-1) for sulfite. kcat is 0.038 sec(-1) for nitrite.


organism: Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)

substrate_name: oxaloacetate

proof_lines: kcat is 150 sec(-1) with oxaloacetate as substrate. kcat is 56 sec(-1) with prephenate as substrate.

substrate: oxaloacetate


organism: Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)

proof_lines: kcat is 33 sec(-1) with oxaloacetate as substrate. kcat is 0.8 sec(-1) with prephenate as substrate.


organism: Rhizobium meliloti (strain 1021)

proof_lines: kcat is 205 sec(-1) with oxaloacetate as substrate. kcat is 43 sec(-1) with prephenate as substrate.


organism: Bacillus sp

substrate: alpha-cyclodextrin (at pH 7.0 and 50 degrees Celsius)


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)


organism: Chrysanthemum x morifolium

substrate_name: cyanidin 3-O-beta-D-glucoside

substrate: cyanidin 3-O-beta-D-glucoside


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines: pH 7.0, 30°C, value is obtained by measurement of formation of pelargonidin 3-O-(6-O-malonyl-beta-D-glucoside)


organism: Populus x canadensis

substrate_name: tert-butyl hydroperoxide

substrate: tert-butyl hydroperoxide


organism: Allochromatium vinosum

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

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

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


organism: Desulfocurvibacter africanus

assay_conditions_summary: pH 6

proof_lines: pH 6.0, temperature not specified in the publication


organism: Nitratidesulfovibrio vulgaris

substrate_name: hydroxylamine

substrate: hydroxylamine


organism: Nicotiana tabacum


organism: Solanum tuberosum

substrate_name: 16-hydroxypalmitic acid

substrate: 16-hydroxypalmitic acid


organism: Arabidopsis thaliana

substrate_name: feruloyl-CoA

proof_lines: 16-hydroxypalmitic acid is the main acyl acceptor.

substrate: feruloyl-CoA


enzyme_display_name: dolichol kinase

organism: Ascaris suum

substrate_name: CTP

enzyme: dolichol kinase

substrate: CTP


organism: Bos taurus

proof_lines: pH 7.5, 35°C, in Triton X-100/dimyristoylphosphatidylcholine 1:1

proof_lines: pH 7.5, 35°C, in deoxycholate/dimyristoylphosphatidylcholine 1:1


organism: Glycine max

substrate_name: dolichol

substrate: dolichol


organism: Onchocerca volvulus


organism: Rattus norvegicus

proof_lines:
pH 7.4, 37°C
pH 7.4, 37°C, skeletal muscle enzyme
pH 7.4, 37°C, brain enzyme


organism: Tetrahymena pyriformis


organism: Homo sapiens


enzyme_display_name: sulfate adenylyltransferase (ADP)

substrate_name: adenosine 5'-phosphosulfate

assay_conditions_summary: pH 6.8; 303.15 K; buffer 0.1 M HEPES/KOH

proof_lines: in 0.1 M HEPES/KOH buffer (pH 6.8), 0.1 M potassium phosphate (pH 6.8), 0.1 M KH2PO4 (pH 4.2), at 30°C

enzyme: sulfate adenylyltransferase (ADP)

substrate: adenosine 5'-phosphosulfate


organism: Thiobacillus denitrificans


enzyme_display_name: ATP adenylyltransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

sequence_source: Selected source_record sequence for UniProtKB P22108; direct UniProtKB FASTA check matched exactly on 2026-07-08

proof_lines: kcat is 93.8 sec(-1) with Ap4A as substrate.

enzyme: ATP adenylyltransferase


sequence_source: Selected source_record sequence for UniProtKB P16550; direct UniProtKB FASTA check matched exactly on 2026-07-08

proof_lines: kcat is 81.2 sec(-1) with Ap4A as substrate.


organism: Caenorhabditis elegans

assay_conditions_summary: pH 6.8; 303.15 K; buffer 0.1 M HEPES/KOH; cofactor ADP


organism: Prosthecochloris vibrioformis

proof_lines:
pH 8.0, 50 mM phosphate
pH 8, 1 mM adenosine 5-phosphosulfate


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: 4 mM adenosine 5-phosphosulfate, 30°C, pH 8


organism: Saccharomyces fragilis

substrate_name: ADP

assay_conditions_summary: 303.15 K; cofactor ADP

substrate: ADP


enzyme_display_name: phenol 2-monooxygenase (FADH2)

organism: Rhodococcus erythropolis

substrate_name: FAD

assay_conditions_summary: cofactor NADPH

proof_lines:
with FMN as electron acceptor
with FAD as electron acceptor

enzyme: phenol 2-monooxygenase (FADH2)

substrate: FAD


enzyme_display_name: spleen exonuclease

organism: Plasmodium falciparum

mutation_signature: C-terminal truncation mutant

mutation_type: truncation

enzyme: spleen exonuclease


organism: Plasmodium yoelii


enzyme_display_name: adenosine nucleosidase

organism: Hordeum vulgare

substrate_name: adenosine

assay_conditions_summary: pH 5.4; buffer MES

enzyme: adenosine nucleosidase

substrate: adenosine


organism: Lathyrus oleraceus

substrate_name: Inosine

substrate: Inosine


organism: Lupinus luteus


organism: Solanum lycopersicum

proof_lines:
form R1
form R2
from Lf


organism: Triticum aestivum


organism: Parageobacillus thermoglucosidasius

substrate_name: riboflavin

source_db: oed

substrate: riboflavin

source: oed


assay_conditions_summary: pH 7; 298.15 K; cofactor FAD


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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines: NADH-dependent reduction, 25°C, pH 7.0, recombinant PheA2

source_databases_merged: brenda skid


substrate_name: FMN

substrate: FMN


organism: Auxenochlorella pyrenoidosa

substrate_name: phenol

substrate: phenol


organism: Bos taurus

substrate_name: thymidine 3'-(4-nitrophenyl)phosphate

substrate: thymidine 3'-(4-nitrophenyl)phosphate


organism: Cavia porcellus


organism: Homo sapiens


enzyme_display_name: galactosylceramidase

organism: Aspergillus oryzae

substrate_name: Unknown

proof_lines: pH 4.6, temperature not specified in the publication

enzyme: galactosylceramidase

substrate: Unknown


proof_lines: taurocholate and oleic acid activated, in leukocytes


substrate_name: galactosylceramide

substrate: galactosylceramide


organism: Mus musculus


organism: Arabidopsis thaliana

proof_lines: recombinant enzyme expressed in Escherichia coli


organism: Brassica oleracea


organism: Coffea arabica


organism: Helianthus tuberosus


substrate_name: glucosylceramide (at 37 degrees Celsius and pH 6.0)

proof_lines: kcat is 0.43 min(-1) for the hydrolysis of glucosylceramide (PubMed:17595169). kcat<0.01 min(-1) for the hydrolysis of galactosylceramide (PubMed:17595169). kcat is 7.26 min(-1) for the hydrolysis of C6-NBD-glucosylceramide (PubMed:17595169


proof_lines: kcat is 2500 min(-1) for the hydrolysis of beta-D-glucosyl-(1->3)-O-lithocholate (PubMed:9111029). kcat is 1300 min(-1) for the hydrolysis of beta-D-glucosyl-(1->3)-O-chenodeoxycholate (PubMed:9111029). kcat is 4700 min(-1) for the hydrolys


substrate_name: uridine

proof_lines: kcat is 2.65 sec(-1) with xanthosine as substrate (PubMed:30787180). kcat is 33.5 sec(-1) with uridine as substrate (PubMed:30787180). kcat is 23.3 sec(-1) with xanthosine as substrate (when in complex with URH2) (PubMed:30787180). kcat is

substrate: uridine


organism: Caenorhabditis elegans

substrate_name: inosine (at pH 7.0 and 37 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 0.79 sec(-1) with inosine as substrate (at pH 7.0 and 37 degrees Celsius) (PubMed:12777783). kcat is 0.203 sec(-1) with inosine as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:28218438). kcat is 0.78 sec(-1) with adenosine a


substrate_name: 5'-OH ApA diribonucleotide

substrate: 5'-OH ApA diribonucleotide


substrate_name: N-acyl-beta-D-galactosylsphingosine

substrate: N-acyl-beta-D-galactosylsphingosine


substrate_name: inosine

substrate: inosine


enzyme_display_name: beta-lactamase

organism: Serratia marcescens

substrate_name: H2O; Ampicillin

enzyme: beta-lactamase

substrate: H2O; Ampicillin


organism: Escherichia coli


organism: Klebsiella pneumoniae

substrate_name: Nitrocefin; H2O

substrate: Nitrocefin; H2O


organism: Pseudomonas aeruginosa

substrate_name: H2O; Penicillin G

substrate: H2O; Penicillin G


organism: Aeromonas hydrophila

substrate_name: H2O; Imipenem

substrate: H2O; Imipenem


organism: Bacillus licheniformis

substrate_name: H2O; Phenoxymethylpenicillin

substrate: H2O; Phenoxymethylpenicillin


organism: Enterobacter cloacae

substrate_name: Cefotaxime; H2O

substrate: Cefotaxime; H2O


substrate_name: H2O; Nitrocefin

substrate: H2O; Nitrocefin


source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.5

source: skid


substrate_name: nitrocefin

substrate: nitrocefin


substrate_name: cefepime

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: cefepime


substrate_name: ceftazidime

substrate: ceftazidime


substrate_name: ticarcillin

substrate: ticarcillin


substrate_name: Imipenem

substrate: Imipenem


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----


enzyme_display_name: carbonic anhydrase

organism: Candida albicans

substrate_name: H2O; CO2

enzyme: carbonic anhydrase

substrate: H2O; CO2


organism: Cryptococcus neoformans


organism: Homo sapiens

substrate_name: CO2; H2O

substrate: CO2; H2O


organism: Spinacia oleracea


enzyme_display_name: beta-glucosidase

organism: Prunus dulcis

substrate_name: beta-Methyl-D-glucopyranoside; H2O

enzyme: beta-glucosidase

substrate: beta-Methyl-D-glucopyranoside; H2O


organism: Oryza sativa

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

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


organism: Pyrococcus furiosus


enzyme_display_name: homomethionine N-monooxygenase

organism: Arabidopsis thaliana

substrate_name: Dihomomethionine; O2

proof_lines: pH and temperature not specified in the publication

enzyme: homomethionine N-monooxygenase

substrate: Dihomomethionine; O2


substrate_name: Hexahomomethionine; O2

substrate: Hexahomomethionine; O2


substrate_name: pseudouridine1915 in 23S rRNA

substrate: pseudouridine1915 in 23S rRNA


substrate_name: S-Adenosyl-L-methionine; Pseudouridine

substrate: S-Adenosyl-L-methionine; Pseudouridine


enzyme_display_name: dimethylsulfoniopropionate demethylase

organism: Candidatus Pelagibacter communis

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: dimethylsulfoniopropionate demethylase


organism: Candidatus Pelagibacter ubique

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


organism: Ruegeria pomeroyi

substrate_name: dimethylsulfoniopropionate

proof_lines: in cell extracts, similar to that of purified recombinant DmdA

substrate: dimethylsulfoniopropionate


enzyme_display_name: levansucrase

organism: Bacillus amyloliquefaciens

substrate_name: sucrose

proof_lines: recombinant Lev-(GGS)6-D272NInu fusion enzyme, pH 5.0, 50°C

proof_lines: recombinant D86NLev-(GGS)6-Inu fusion enzyme, pH 5.0, 50°C

proof_lines: recombinant Lev-(GGS)6-Inu fusion enzyme, pH 5.0, 50°C

enzyme: levansucrase

substrate: sucrose


proof_lines: recombinant wild-type enzyme Lev, pH 5.0, 50°C


proof_lines: mutant K82H/N83R, Hill model, Hill coefficient 1.18, hydrolysis of sucrose, pH 6, 50°C

proof_lines: mutant K82H/N83R, transfructosylation reaction, hydrolysis of sucrose, pH 6, 50°C

proof_lines: mutant K82H/N83R, Hill model, Hill coefficient 0.57, total reaction, pH 6, 50°C


proof_lines: wild-type, Michaelis-Menten model, total reaction, total reaction, pH 6, 50°C

proof_lines: wild-type, Hill model, Hill coefficient 0.59, total reaction, pH 6, 50°C

proof_lines: wild-type, transfructosylation reaction, pH 6, 50°C


organism: Bacillus subtilis

proof_lines: mutant enzyme Y429N, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


substrate_name: Sucrose

substrate: Sucrose


substrate_name: Sucrose; (2,6-beta-D-Fructosyl)n

substrate: Sucrose; (2,6-beta-D-Fructosyl)n


proof_lines: mutant enzyme G361F, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


proof_lines: mutant enzyme R360S, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


proof_lines: mutant enzyme I341V, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


proof_lines: mutant enzyme H243L, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


proof_lines: mutant S164A, hydrolysis of sucrose, pH 6, 37°C

proof_lines: mutant S164A, hydrolysis of sucrose, cosubstrate levan , 5 g/l, pH 6, 37°C

proof_lines: mutant S164A, transfer reaction, cosubstrate levan , 5 g/l, pH 6, 37°C


proof_lines: wild-type, transfer reaction, cosubstrate levan, 5 g/l, pH 6, 37°C

proof_lines: wild-type, transfer reaction, pH 6, 37°C

proof_lines: wild-type, hydrolysis of sucrose, cosubstrate levan, 5 g/l, pH 6, 37°C


organism: Brenneria sp. EniD312


organism: Beijerinckia indica subsp. indica


proof_lines: transfructosylating activity, at pH 6.0 and 37°C


proof_lines: mutant enzyme R369K, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


proof_lines: mutant enzyme R433A, 0.5 U/ml of enzyme activity at 37°C and pH 6.0


organism: Erwinia tasmaniensis

proof_lines:
at pH 6.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=6.5


organism: Gluconacetobacter diazotrophicus

proof_lines:
wild-type enzyme
30°C, pH 5.0, wild-type enzyme


substrate_name: H2O; Sucrose

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=5

substrate: H2O; Sucrose


organism: Gluconobacter oxydans


organism: Leuconostoc mesenteroides


organism: Novosphingobium aromaticivorans


organism: Paraburkholderia graminis


organism: Priestia megaterium

proof_lines:
wild-type, pH 6.6, 25°C
wild-type, pH 6.6, 37°C


proof_lines: variant carrying Lactobacillus johnsonii loop2, pH 6.6, 25°C

proof_lines: variant carrying Lactobacillus johnsonii loop3-4, pH 6.6, 37°C

proof_lines: variant carrying Lactobacillus johnsonii loop3-7, pH 6.6, 37°C


organism: Pseudomonas chlororaphis subsp. aurantiaca

proof_lines: inhibition of sucrose hydrolysis, pH 6.0-6.6, 60°C


organism: Pseudomonas syringae


organism: Pseudomonas syringae pv. tomato

proof_lines: inhibition of sucrose hydrolysis, pH 6.0, 60°C


organism: Streptococcus salivarius

substrate_name: D-Glucose

substrate: D-Glucose


substrate_name: D-Fructose

substrate: D-Fructose


organism: Vibrio natriegens


organism: Zymomonas mobilis

proof_lines:
levan synthesis activity
transfructosylation activity
total activity


enzyme_display_name: pyruvate kinase

organism: Rattus norvegicus

substrate_name: Phosphoenolpyruvate; ADP

assay_conditions_summary: cofactor ATP

enzyme: pyruvate kinase

substrate: Phosphoenolpyruvate; ADP


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor ADP


enzyme_display_name: N-acetyllactosaminidase

organism: Aquimarina sp. TRL1

proof_lines: 35°C, pH not specified in the publication

enzyme: N-acetyllactosaminidase


organism: Paludibaculum fermentans


organism: Parabacteroides distasonis


organism: Planctomycetales bacterium


organism: Treponema denticola


enzyme_display_name: fumarylacetoacetase

organism: Homo sapiens

enzyme: fumarylacetoacetase


organism: Escherichia coli

substrate_name: RlmH; S-Adenosyl-L-methionine

substrate: RlmH; S-Adenosyl-L-methionine


organism: Candidatus Pelagibacter communis

proof_lines: noncompetitive inhibition, product inhibition


organism: Actinomyces viscosus


organism: Aspergillus tamarii

proof_lines: transfructosylation reaction, pH 7.4, 50°C

proof_lines: application of a static magnetic field with a 1450 G magnetic flux density prior to assay, pH 5, 55°C


organism: Bacillus amyloliquefaciens


organism: Bacillus licheniformis

proof_lines: mutant enzyme N251W, total activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme N251W, hydrolytic activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme N251W, transfructosylation activity, at pH 6.0 and 50°C


proof_lines: wild type enzyme, total activity, at pH 6.0 and 50°C

proof_lines: wild type enzyme, hydrolytic activity, at pH 6.0 and 50°C

proof_lines: wild type enzyme, transfructosylation activity, at pH 6.0 and 50°C


proof_lines: mutant enzyme K372A, hydrolytic activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme K372A, total activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme K372A, transfructosylation activity, at pH 6.0 and 50°C


proof_lines: mutant enzyme N251W/K372Y, total activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme N251W/K372Y, transfructosylation activity, at pH 6.0 and 50°C


proof_lines: mutant enzyme K372Y, total activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme K372Y, hydrolytic activity, at pH 6.0 and 50°C

proof_lines: mutant enzyme K372Y, transfructosylation activity, at pH 6.0 and 50°C


organism: Bacillus subtilis

proof_lines: levansucrase-endolevanase fusion enzyme, pH and temperature not specified in the publication

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


organism: Rhodotorula diobovata


organism: Pelagibacter ubique (strain HTCC1062)

substrate_name: tetrahydrafolate

proof_lines: Upon expression and purification from E.coli.

substrate: tetrahydrafolate


organism: Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 164.6 sec(-1) with sucrose as substrate (PubMed:18596022). kcat is 236.7 sec(-1) with sucrose as substrate (PubMed:33303628). kcat is 71.2 sec(-1) with sucrose as substrate (for hydrolysis, in the absence of levan F4). kcat is 69.8


organism: Gluconacetobacter diazotrophicus


organism: Pseudomonas syringae pv. actinidiae

substrate_name: sucrose (at pH 5.0)

assay_conditions_summary: pH 5

proof_lines: kcat is 7300 min(-1) with sucrose as substrate (at pH 5.0). kcat is 7500 min(-1) with sucrose as substrate (at pH 7.0).

substrate: sucrose (at pH 5.0)


proof_lines: kcat is 8500 min(-1) with sucrose as substrate (at pH 5.0). kcat is 15000 min(-1) with sucrose as substrate (at pH 7.0).


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

proof_lines: kcat is 1700 min(-1) for sucrose hydrolase activity.


organism: Aquimarina sp. (strain TRL1)

substrate_name: pNP-LNB

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

substrate: pNP-LNB


organism: Paludibaculum fermentans

substrate_name: pNP-LacNAc

verification_status: verified

assay_conditions_summary: pH 6; 318.15 K; buffer pH 6

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

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

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

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

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

substrate: pNP-LacNAc

status: verified


organism: Parabacteroides distasonis

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


organism: Planctomycetales bacterium (strain ZRK34)

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


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

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


organism: Fructilactobacillus sanfranciscensis

substrate_name: sucrose (at 28 degrees Celsius)

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

substrate: sucrose (at 28 degrees Celsius)


organism: Arabidopsis thaliana


proof_lines: sucrose hydrolysis, mutants R331L and R331S


organism: Bacillus velezensis


organism: Clostridium acetobutylicum


organism: Erwinia amylovora


organism: Limosilactobacillus panis


organism: Pantoea agglomerans


organism: Priestia megaterium


organism: Pseudomonas orientalis


organism: Pseudomonas savastanoi pv. phaseolicola


organism: Rahnella aquatilis


organism: Zymomonas mobilis


enzyme_display_name: [phosphorylase] phosphatase

organism: Bos taurus

substrate_name: histone

enzyme: [phosphorylase] phosphatase

substrate: histone


organism: Oryctolagus cuniculus

substrate_name: H2O; Phosphorylase a

substrate: H2O; Phosphorylase a


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


substrate_name: butyropyruvate

substrate: butyropyruvate


organism: Homo sapiens

substrate_name: Fumarylacetoacetate

proof_lines:
liver, dependent on patients
37°C, recombinant enzyme

substrate: Fumarylacetoacetate


organism: Unknown

substrate_name: benzoyl-CoA

assay_conditions_summary: cofactor CoA

substrate: benzoyl-CoA


organism: Garcinia mangostana

substrate_name: malonyl-CoA

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines: pH 7.0, 30°C, recombinant His-tagged BPS

substrate: malonyl-CoA


enzyme_display_name: fatty-acyl-CoA synthase system

organism: Saccharomyces cerevisiae

substrate_name: NADPH; Acetyl-CoA; Malonyl-CoA; H+

assay_conditions_summary: cofactor NADP+

enzyme: fatty-acyl-CoA synthase system

substrate: NADPH; Acetyl-CoA; Malonyl-CoA; H+


organism: Hypericum androsaemum

assay_conditions_summary: pH 7; 308.15 K; cofactor CoA


organism: Mycolicibacterium phlei


substrate_name: lauroyl-CoA

substrate: lauroyl-CoA


proof_lines: kcat is 9.66 min(-1) with benzoyl-CoA as substrate.


enzyme_display_name: glucosylglycerate synthase

organism: Petrotoga mobilis

substrate_name: ADP-glucose

assay_conditions_summary: pH 6.7; 343.15 K; cofactor ADP

proof_lines:
pH 6.7, 70°C, native enzyme
pH 6.7, 60°C, native enzyme
pH 6.7, 60°C, recombinant enzyme

enzyme: glucosylglycerate synthase

substrate: ADP-glucose


organism: Petrotoga mobilis (strain DSM 10674 / SJ95)

substrate_name: ADP-glucose (for the native enzyme, at 60 degrees Celsius)


organism: Persephonella marina

substrate_name: D-glycerate

assay_conditions_summary: pH 6.5; 343.15 K; cofactor ADP

substrate: D-glycerate


enzyme_display_name: ipecoside beta-D-glucosidase

organism: Carapichea ipecacuanha

enzyme: ipecoside beta-D-glucosidase


substrate_name: N-deacetylipecoside

proof_lines: kcat is 28.2 sec(-1) with N-deacetylipecoside as substrate (PubMed:18927081). kcat is 86.3 sec(-1) with N-deacetylisoipecoside as substrate (PubMed:18927081). kcat is 31.1 sec(-1) with 6-O-methyl-N-deacetylipecoside as substrate (PubMed:189

substrate: N-deacetylipecoside


enzyme_display_name: N,N-dimethylformamidase

organism: Methylobacterium sp. DM1

substrate_name: N,N-Dimethylformamide

enzyme: N,N-dimethylformamidase

substrate: N,N-Dimethylformamide


organism: Paracoccus sp. SSG05

substrate_name: Formamide

proof_lines: pH not specified in the publication, 33°C

substrate: Formamide


enzyme_display_name: AMP nucleosidase

organism: Azotobacter vinelandii

substrate_name: NMN

enzyme: AMP nucleosidase

substrate: NMN


substrate_name: AMP

proof_lines:
mutant enzyme
mutant AMP nucleosidase

substrate: AMP


organism: Escherichia coli


organism: Alcaligenes sp.


organism: Pseudomonas sp.


organism: Escherichia coli (strain K12)

substrate_name: AMP (in the absence of Mg-ATP)

substrate: AMP (in the absence of Mg-ATP)


organism: Alcaligenes sp

substrate_name: N,N-dimethylformamide

smiles: CN(C)C=O

substrate: N,N-dimethylformamide


enzyme_display_name: scytalone dehydratase

organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958)

enzyme: scytalone dehydratase


organism: Phaeococcomyces sp.

substrate_name: Scytalone

substrate: Scytalone


organism: Pyricularia grisea


organism: Pyricularia oryzae

proof_lines:
mutant enzyme V75M with His-tag
mutant enzyme V75M without His-tag


proof_lines:
wild-type enzyme
pH 7.0, 30°C, wild-type enzme


proof_lines: pH 8.0, 25°C, inhibitor-resistant enzyme

proof_lines: pH 8.0, 25°C, inhibitor-sensitive enzyme


enzyme_display_name: stearoyl-CoA 9-desaturase

organism: Plasmodium falciparum

substrate_name: stearoyl-CoA

assay_conditions_summary: pH 7.2; 310.15 K; buffer pH 7; cofactor CoA

proof_lines: in 0.1 M potassium phosphate buffer pH 7.2, at 37°C

enzyme: stearoyl-CoA 9-desaturase

substrate: stearoyl-CoA


organism: Bos taurus

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Fusarium oxysporum

assay_conditions_summary: cofactor NADPH


organism: Gallus gallus

substrate_name: H+; O2; NADH; Stearoyl-CoA

substrate: H+; O2; NADH; Stearoyl-CoA


organism: Mycolicibacterium phlei

substrate_name: FAD

substrate: FAD


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

proof_lines: fatty acyl-CoA substrates with chain length of 14-19 carbon atoms show similar turnover number of about 22

proof_lines: in 150 mM KCl, 40 mM NaF, 100 mM sodium phosphate buffer, pH 7.4, at 37°C


organism: Spinacia oleracea

substrate_name: stearoyl-acyl-carrier protein

substrate: stearoyl-acyl-carrier protein


organism: Sus scrofa

substrate_name: N-hydroxy-benzenecarboximidamide

assay_conditions_summary: 310.15 K; cofactor CoA

substrate: N-hydroxy-benzenecarboximidamide


enzyme_display_name: L-histidine N(alpha)-methyltransferase

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

substrate_name: L-histidine

proof_lines: kcat is 0.58 sec(-1) for the methylation of L-histidine. kcat is 0.23 sec(-1) for the methylation of N-alpha-methyl-L-histidine. kcat is 0.23 sec(-1) for the methylation of N-alpha,N-alpha-dimethyl-L-histidine.

enzyme: L-histidine N(alpha)-methyltransferase

substrate: L-histidine


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)

substrate_name: hercynine

substrate: hercynine


organism: Mycolicibacterium smegmatis


substrate_name: Nalpha,Nalpha-dimethyl-L-histidine

substrate: Nalpha,Nalpha-dimethyl-L-histidine


substrate_name: L-tryptophan

substrate: L-tryptophan


organism: Arabidopsis sp.

sequence_source: UniProtKB/Swiss-Prot Q8VZU3 direct follow-up


organism: Raphanus sativus


organism: Sinapis alba


organism: Arabidopsis thaliana

substrate_name: sinapoylglucose

proof_lines: Measured in vitro at pH 7.0 and 30 degrees Celsius.

substrate: sinapoylglucose


enzyme_display_name: phenol beta-glucosyltransferase

substrate_name: UDPglucose; Caffeate

enzyme: phenol beta-glucosyltransferase

substrate: UDPglucose; Caffeate


substrate_name: quercetin

substrate: quercetin


organism: Carica papaya

substrate_name: UDPglucose

substrate: UDPglucose


organism: Leishmania donovani

substrate_name: lipophosphoglycan

substrate: lipophosphoglycan


organism: Nicotiana tabacum

substrate_name: UDP-xylose

substrate: UDP-xylose


enzyme_display_name: plant cystathionine gamma-synthase

organism: Lemna aequinoctialis

substrate_name: L-cysteine

enzyme: plant cystathionine gamma-synthase

substrate: L-cysteine


substrate_name: O-phospho-L-homoserine

proof_lines: pH and temperature not specified in the publication

substrate: O-phospho-L-homoserine


proof_lines:
at pH 7.5 and 30°C
at pH 7.5 and 20°C


proof_lines: kcat is 30 sec(-1) with L-cysteine as substrate.


verification_status: unverified

status: unverified


enzyme_display_name: undecaprenol kinase

organism: Unknown

substrate_name: ATP

enzyme: undecaprenol kinase

substrate: ATP


organism: Lactiplantibacillus plantarum

substrate_name: undecaprenol

assay_conditions_summary: pH 8; 306.15 K; cofactor ATP

proof_lines: pH 8.0, 33°C, reaction with undecaprenol

substrate: undecaprenol


organism: Lactobacillus plantarum

substrate_name: ATP; Undecaprenol

substrate: ATP; Undecaprenol


organism: Staphylococcus aureus

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP

proof_lines: pH 8.5, 25°C, reaction with C55-isoprenoid alcohols from Streptococcus faecalis or ficaprenol


organism: Streptococcus mutans

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


enzyme_display_name: (deoxy)nucleoside-phosphate kinase

organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines: at 30°C, pH 8.0 and saturating Mg2+ and K+ concentrations

enzyme: (deoxy)nucleoside-phosphate kinase


organism: Tequintavirus T5

substrate_name: dAMP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C
dTMP as substrate, pH 7.6, 37°C

substrate: dAMP


enzyme_display_name: glutathione-dependent peroxiredoxin

organism: Homo sapiens

enzyme: glutathione-dependent peroxiredoxin


substrate_name: palmitoyl-CoA (lysophosphatidylcholine acyltransferase activity at pH 4.0)


proof_lines: kcat is 22.5 min(-1) and 30.3 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.


enzyme_display_name: thiamine phosphate synthase

organism: Zea mays

enzyme: thiamine phosphate synthase


organism: Bacillus subtilis


organism: Escherichia coli


organism: Bacillus subtilis (strain 168)

substrate_name: HMP-PP

substrate: HMP-PP


organism: Escherichia coli (strain K12)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


assay_conditions_summary: pH 8; 310.15 K; buffer containing 50 mM phosphate and 10 mM MgSO4

proof_lines: wild type enzyme, in buffer containing 50 mM phosphate and 10 mM MgSO4, at pH 8.0 and 37°C


enzyme_display_name: feruloyl-CoA 6-hydroxylase

organism: Ipomoea batatas

substrate_name: trans-feruloyl-CoA

assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA

enzyme: feruloyl-CoA 6-hydroxylase

substrate: trans-feruloyl-CoA


organism: Arabidopsis thaliana

substrate_name: feruloyl CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 11 sec(-1) with feruloyl CoA as substrate.

substrate: feruloyl CoA


proof_lines: kcat is 4.79 sec(-1) with feruloyl CoA as substrate.


substrate_name: feruloyl-CoA

proof_lines: kcat is 0.35 sec(-1) with feruloyl-CoA as substrate. kcat is 0.33 sec(-1) with p-Coumaroyl-CoA as substrate.

substrate: feruloyl-CoA


proof_lines: kcat is 2.68 sec(-1) with feruloyl-CoA as substrate.


proof_lines: kcat is 0.28 sec(-1) with feruloyl-CoA as substrate. kcat is 0.28 sec(-1) with p-Coumaroyl-CoA as substrate.


proof_lines: kcat is 2.84 sec(-1) with feruloyl-CoA as substrate.


proof_lines: kcat is 0.55 sec(-1) with feruloyl-CoA as substrate. kcat is 0.64 sec(-1) with p-Coumaroyl-CoA as substrate.


organism: Ruta graveolens

proof_lines: kcat is 0.46 sec(-1) with feruloyl-CoA as substrate (PubMed:22168819). kcat is 0.71 sec(-1) with p-coumaroyl-CoA as substrate (PubMed:22168819).


enzyme_display_name: phylloquinone omega-hydroxylase

substrate_name: arachidonic acid

sequence_source: UniProtKB reviewed accession Q9HBI6, retrieved by direct UniProt REST check for human CYP4F11; used as paper-level identity context, not as sufficient accepted-row proof.

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM potassium phosphate

proof_lines: in 100 mM potassium phosphate buffer (pH 7.4), at 37°C

proof_lines: pH and temperature not specified in the publication

enzyme: phylloquinone omega-hydroxylase

substrate: arachidonic acid


substrate_name: docosanoate

proof_lines: kcat is 0.067 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). The omega-hydroxylation of VLCFAs follows dual-enzyme Michaelis-Menten kinetics, suggesting simultaneous binding of two substrate molecules. The high affinity M

substrate: docosanoate


substrate_name: hexadecanoic acid

proof_lines: kcat is 0.088 min(-1) with menaquinone-4 (MK-4) as substrate (PubMed:24138531). kcat is 1.8 min(-1) with hexadecanoic acid as substrate. kcat is 1.0 min(-1) with (9Z)-octadecenoic acid as substrate. kcat is 0.54 min(-1) with (5Z,8Z,11Z,14Z)

substrate: hexadecanoic acid


enzyme_display_name: mRNA m(6)A methyltransferase

substrate_name: adenine in single-stranded DNA

proof_lines: 14 nucleotides single-stranded DNA, target consensus sequence GGACT, at pH 7.5 and 22°C

proof_lines: target consensus sequence GAACA, at pH 7.5 and 22°C

proof_lines: target consensus sequence GAACT, at pH 7.5 and 22°C

enzyme: mRNA m(6)A methyltransferase

substrate: adenine in single-stranded DNA


sequence_source: source_record; confirmed against UniProt P32754 during review

proof_lines: kcat is 2.0 sec(-1) with 3-(4-hydroxyphenyl)pyruvate as substrate.


organism: Rattus norvegicus

substrate_name: 4-hydroxyphenylpyruvic acid

substrate: 4-hydroxyphenylpyruvic acid


proof_lines: 37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVb

proof_lines: 37°C, pH 7.5, recombinant full-length N-acetylglucosaminyltransferase-IVa

proof_lines: 37°C, pH 7.5, recombinant soluble human flag-GnTIVa


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


organism: Bos taurus


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


proof_lines:
isoenzyme AtSOT18 Co10, pH 9.0, 37°C
isoenzyme AtSOT16 C24, pH 9.0, 37°C
isoenzyme AtSOT17 C24, pH 9.0, 37°C


organism: Brassica juncea

substrate_name: desulfobenzylglucosinolate

substrate: desulfobenzylglucosinolate


organism: Lepidium sativum


substrate_name: desulfo-benzyl glucosinolate

substrate: desulfo-benzyl glucosinolate


enzyme_display_name: dihydrocoumarin hydrolase

organism: Unknown

substrate_name: methyl cetraxate hydrochloride

enzyme: dihydrocoumarin hydrolase

substrate: methyl cetraxate hydrochloride


organism: Acinetobacter calcoaceticus


organism: Geobacillus sp.


organism: Melilotus albus

substrate_name: dihydrocoumarin

substrate: dihydrocoumarin


enzyme_display_name: phosphonoacetate hydrolase

organism: Curtobacterium sp.

substrate_name: Phosphonoacetate

enzyme: phosphonoacetate hydrolase

substrate: Phosphonoacetate


organism: Penicillium oxalicum


organism: Pseudomonas fluorescens


organism: Pseudomonas sp.


organism: Sinorhizobium meliloti

proof_lines: pH 7.5, 30°C, recombinant enzyme, with 0.01 mM Zn2+


substrate_name: phosphonoacetate

substrate: phosphonoacetate


enzyme_display_name: tubulin-glutamate carboxypeptidase

organism: Mus musculus

substrate_name: biotin-Glu-Glu-Gly-Glu-Glu-Glu

enzyme: tubulin-glutamate carboxypeptidase

substrate: biotin-Glu-Glu-Gly-Glu-Glu-Glu


substrate_name: biotin-Glu-Glu

substrate: biotin-Glu-Glu


substrate_name: biotin-Glu-Glu-Glu

substrate: biotin-Glu-Glu-Glu


substrate_name: biotin-Glu-Glu-Glu-Gly-Glu-Glu

substrate: biotin-Glu-Glu-Glu-Gly-Glu-Glu


enzyme_display_name: NMN nucleosidase

organism: Azotobacter vinelandii

substrate_name: nicotinamide mononucleotide

proof_lines:
in absence of GTP
0.52 mM dGTP as effector
0.5 mM/1 mM GTP

enzyme: NMN nucleosidase

substrate: nicotinamide mononucleotide


organism: Nicotiana tabacum


organism: Oryctolagus cuniculus

substrate_name: H2O; Nicotinamide nucleotide

substrate: H2O; Nicotinamide nucleotide


enzyme_display_name: histolysain

organism: Entamoeba histolytica

substrate_name: Unknown

enzyme: histolysain

substrate: Unknown


organism: Entamoeba histolytica (strain ATCC 30459 / HM-1:IMSS / ABRM)

substrate_name: Z-Arg-Arg-NHMec

proof_lines: kcat is 130 sec(-1) with Z-Arg-Arg-NHMec as substrate and 0.4 sec(-1) with Z-Phe-Arg-NHMec as substrate.

substrate: Z-Arg-Arg-NHMec


proof_lines: isoform CP2, pH and temperature not specified in the publication

proof_lines: isoform CP5, pH and temperature not specified in the publication


enzyme_display_name: urocanate hydratase

organism: Bacillus subtilis

substrate_name: Urocanate

enzyme: urocanate hydratase

substrate: Urocanate


organism: Bos taurus


organism: Comamonas testosteroni


organism: Pseudomonas putida


enzyme_display_name: vitamin D 1,25-hydroxylase

organism: Streptomyces griseolus

substrate_name: vitamin D3 (at pH 7.4 and 30 degrees Celsius)

proof_lines: kcat is 0.0076 min(-1) for hydroxylase activity with 1-alpha-hydroxyvitamin D3 as substrate. kcat is 0.0026 min(-1) for hydroxylase activity with 25-hydroxyvitamin D3 as substrate.

enzyme: vitamin D 1,25-hydroxylase


substrate_name: urocanate

substrate: urocanate


substrate_name: calciol

proof_lines: vitamin D3 25-hydroxylation, pH 7.4, 30°C

proof_lines: vitamin D2 25-hydroxylation, pH 7.4, 30°C

proof_lines: 25-hydroxyvitamin D3 1alpha-hydroxylation, pH 7.4, 30°C

substrate: calciol


substrate_name: 1alpha-hydroxyvitamin D3

proof_lines: 25-hydroxylation, mutant R73V/R84A, pH not specified in the publication, temperature not specified in the publication

proof_lines: 26-hydroxylation, mutant R73V/R84A, pH not specified in the publication, temperature not specified in the publication

proof_lines: 1alpha-hydroxylation, mutant R73V/R84A, pH not specified in the publication, temperature not specified in the publication

substrate: 1alpha-hydroxyvitamin D3


enzyme_display_name: taurine--2-oxoglutarate transaminase

organism: Achromobacter superficialis

substrate_name: taurine

proof_lines: pH 8.0, 37°C, cosubstrate DL-3-aminoisobutyrate

enzyme: taurine--2-oxoglutarate transaminase

substrate: taurine


organism: Bifidobacterium catenulatum subsp. kashiwanohense

proof_lines:
pH 7.2, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.2


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


organism: Unknown


enzyme_display_name: alkyl sulfatase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 2-EHS (at pH 7 and 25 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 21.8 min(-1) with alpha-ketoglutarate and 2-EHS as substrates (at pH 7 and 25 degrees Celsius). kcat is 1.54 min(-1) for the oxidative decarboxylation of Ty38c (at pH 7 and 25 degrees Celsius).

enzyme: alkyl sulfatase

substrate: 2-EHS (at pH 7 and 25 degrees Celsius)


substrate_name: SDS (at pH 7 and 30 degrees Celsius)

substrate: SDS (at pH 7 and 30 degrees Celsius)


enzyme_display_name: oleate 10S-lipoxygenase

organism: Nostoc punctiforme

substrate_name: linoleate

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

enzyme: oleate 10S-lipoxygenase

substrate: linoleate


organism: Pseudomonas aeruginosa

substrate_name: linoleate (Ref.4)

proof_lines: kcat is 96 sec(-1) with linoleate as substrate (Ref.4).

substrate: linoleate (Ref.4)


substrate_name: alpha-linolenate

substrate: alpha-linolenate


enzyme_display_name: neurolysin

enzyme: neurolysin


organism: Homo sapiens

proof_lines: presence of 0.04 mM L-histidlyl-L-histidine, pH 7.2, 37°C

proof_lines: presence of 0.1 mM L-histidlyl-L-tyrosine, pH 7.2, 37°C

proof_lines: presence of 0.1 mM L-histidlyl-L-histidine, pH 7.2, 37°C


organism: Rattus norvegicus


substrate_name: neurotensin

proof_lines: recombinant mutant R470E/T499R, pH 7.5, 37°C

substrate: neurotensin


substrate_name: Abz-GFSAFRQEDDnp

proof_lines: pH 7.4, 37°C, recombinant GST-tagged mutant Y606A

substrate: Abz-GFSAFRQEDDnp


substrate_name: Abz-GFSRFRQEDDnp

proof_lines: pH 7.4, 37°C, recombinant GST-tagged mutant G608A

substrate: Abz-GFSRFRQEDDnp


substrate_name: Abz-GFSFFRQEDDnp

proof_lines: pH 7.4, 37°C, recombinant GST-tagged mutant Y606F

substrate: Abz-GFSFFRQEDDnp


substrate_name: Abz-GFSLFRQEDDnp

proof_lines: pH 7.4, 37°C, recombinant GST-tagged wild-type enzyme

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

substrate: Abz-GFSLFRQEDDnp


substrate_name: Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg

proof_lines: inhibition of hydrolysis of 7-methoxycoumarin-4-acetyl-Pro-Leu-Gly-Pro-D-Lys-(2,4-dinitrophenyl)

substrate: Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg


organism: Sus scrofa

proof_lines:
pH 7.4, 37°C, cleavage of F-S bond
pH 7.4, 37°C, cleavage of P-F bond
pH 7.4, 37°C


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.1 M CAPS; cofactor NADH

proof_lines: wild type enzyme, in 0.1 M HEPES at pH 7.5

proof_lines: pH 10.4, 25°C, recombinant wild-type enzyme

substrate: NADH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


sequence_source: UniProtKB P80702 direct metadata check; canonical sequence exists, but the S114A variant sequence was not reconstructed in this lane.

proof_lines: mutant enzyme S114A, in 0.1 M HEPES at pH 7.5


substrate_name: NAD+

sequence_source: UniProtKB P80702 direct metadata check; canonical sequence exists, but the D249A variant sequence was not reconstructed in this lane.

assay_conditions_summary: pH 10.2; 298.15 K; buffer 0.1 M CAPS; cofactor NAD+

proof_lines: mutant enzyme D249A, in 0.1 M CAPS buffer, at pH 10.2, at 25°C

substrate: NAD+


sequence_source: UniProtKB P80702 direct metadata check; canonical sequence exists, but the D249S variant sequence was not reconstructed in this lane.

proof_lines: mutant enzyme D249S, in 0.1 M CAPS buffer, at pH 10.2, at 25°C


sequence_source: UniProtKB P80702 direct metadata check; canonical sequence exists, but the D249K variant sequence was not reconstructed in this lane.

proof_lines: mutant enzyme D249K, in 0.1 M CAPS buffer, at pH 10.2, at 25°C


proof_lines: mutant N86A, pH 7.5, 25°C, steady-state kinetic study

proof_lines: mutant N86A, pH 7.5, 25°C, product inhibition study


proof_lines: mutant Y155F, pH 7.5, 25°C, steady-state kinetic study

proof_lines: mutant Y155F, pH 7.5, 25°C, product inhibition study


proof_lines: mutant K159A, pH 7.5, 25°C, product inhibition study


substrate_name: NAD+; Androsterone

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Androsterone


substrate_name: NADP+; Androsterone

assay_conditions_summary: cofactor NADP+

substrate: NADP+; Androsterone


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C1

proof_lines: pH 7.4, 25°C, recombinant isozyme AKR1C2


proof_lines:
isozyme AKR1C9
pH 7.0, 25, oxidation reaction
pH 7.0, 25, reduction reaction


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines:
pH 7.0, 37°, isozyme AKR1C1
pH 7.0, 37°, isozyme AKR1C4
pH 7.0, 25°C, isozyme AKR1C1


organism: Pseudomonas sp. B-0831

substrate_name: cholate

substrate: cholate


substrate_name: dehydrocholate

substrate: dehydrocholate


proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme


assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

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


organism: Ictalurus punctatus

substrate_name: testosterone

proof_lines: pH 7.4, 35°C, 3alpha-hydroxysteroid dehydrogenase activity

substrate: testosterone


organism: Mus musculus

proof_lines: also in this range: 5beta-pregnan-3,20-dione, 5alpha-androstan-3,17-dione

proof_lines: also in this range: 2,3-hexanedione, 1-phenyl-1,2-propanedione, 2,3-pentanedione, pyridine-4-aldehyde, 2,3-butanedione


substrate_name: cholic acid

substrate: cholic acid


organism: Pseudomonas sp.

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines:
pH 8.5, 37°C, with cofactor NAD+
pH 8.5, 37°C, with cofactor thio-NAD+


sequence_source: NCBI RefSeq NP_001129216.1, PubMed-linked protein UID 209364585 for PMID 17475203; gene synonym Akr1c17; organism Rattus norvegicus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

proof_lines: pH 7.4, 25°C, recombinant wild-type AKR1C17


organism: Bos taurus


organism: Canis lupus familiaris


organism: Comamonas testosteroni


substrate_name: androsterone

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant S114A

substrate: androsterone


proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant S114A/Y155F


proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant K159A


proof_lines: pH 9.0, 25°C, recombinant His-tagged wild-type


proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant Y155F


proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant Y155F/K159A


organism: Digitalis purpurea

assay_conditions_summary: cofactor NADPH

proof_lines: cytosolic NADH-linked 5beta-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase

proof_lines: microsomal NADPH-linked 5beta-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase


organism: Eggerthella lenta

proof_lines: also in this range: 3alpha,7alpha-dihydroxy-5beta-cholanoyl glycine

proof_lines: also in this range: 3alpha,12alpha-dihydroxy-5beta-cholanoyl glycine


organism: Gallus gallus


enzyme_display_name: arylmalonate decarboxylase

organism: Bordetella bronchiseptica

enzyme: arylmalonate decarboxylase


substrate_name: Phenylmalonate

substrate: Phenylmalonate


substrate_name: 2-vinyl-2-methylmalonic acid

substrate: 2-vinyl-2-methylmalonic acid


substrate_name: 2-hydroxy-2-phenylmalonic acid

substrate: 2-hydroxy-2-phenylmalonic acid


sequence_source: UniProtKB Q05115 reviewed canonical accession; row-specific variant sequence not reconstructed

proof_lines: mutant M159V, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant enzyme G74C/M159L, pH and temperature not specified in the publication


proof_lines: mutant enzyme G74C/V43A, pH and temperature not specified in the publication


proof_lines: mutant enzyme G74C, pH and temperature not specified in the publication


proof_lines: mutant enzyme G74C/M159L/C188G, pH and temperature not specified in the publication


proof_lines: mutant enzyme G74C/C188G, pH and temperature not specified in the publication


proof_lines: mutant enzyme Y48F/G74C/M159L/C188G, pH and temperature not specified in the publication


proof_lines: mutant enzyme G74C/C188S, pH and temperature not specified in the publication


proof_lines: mutant enzyme Y48F/G74C/C188G, pH and temperature not specified in the publication


substrate_name: hydroxy(thiophen-2-yl)propanedioic acid

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

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

substrate: hydroxy(thiophen-2-yl)propanedioic acid


proof_lines: mutant P14V/P15G, pH not specified in the publication, temperature not specified in the publication


organism: Pyrococcus horikoshii


organism: Unknown


organism: Alkaliphilus metalliredigens QYMF


substrate_name: alpha-methyl-alpha-phenylmalonate

assay_conditions_summary: pH 8; buffer Tris

proof_lines: ybbR-tagged AMDase, in Tris buffer (0.1 M, pH 8)

substrate: alpha-methyl-alpha-phenylmalonate


substrate_name: alpha-phenylmalonate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature C188S to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme Cys188Ser
mutant enzyme C188S

substrate: alpha-phenylmalonate


substrate_name: methyl(2-naphthyl)malonic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature G74C to reconstruct the assayed variant sequence.

substrate: methyl(2-naphthyl)malonic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature S36N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 308.15 K; buffer 1 M Tris-HCl

proof_lines: mutant enzyme S36N, in 1 M Tris-HCl buffer (pH 8.5), at 35°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature S36N/G74C/C188S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S36N/G74C/C188S, in 1 M Tris-HCl buffer (pH 8.5), at 35°C


sequence_source: UniProtKB Q05115 via RCSB PDB 3DG9 / PMID 18576402

proof_lines: wild type enzyme, in 1 M Tris-HCl buffer (pH 8.5), at 35°C

proof_lines: wild type enzyme, in 1 M Tris-HCl buffer pH 8.5, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature G74C/C188S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G74C/C188S, in 1 M Tris-HCl buffer (pH 8.5), at 35°C

proof_lines: mutant enzyme G74C/C188S, in 1 M Tris-HCl buffer pH 8.5, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature S71C/C188S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S71C/C188S, in 1 M Tris-HCl buffer pH 8.5, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature C101S to reconstruct the assayed variant sequence.


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

proof_lines: mutant enzyme G74C/S188S, in 1 M Tris-HCl buffer pH 8.5, at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 canonical sequence reconstructed with selected mutation signature and applied mutation signature C148S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q05115 plus C171S reconstruction; RCSB 3DG9 maps the structure to UniProt Q05115 and EC 4.1.1.76 and applied mutation signature C171S to reconstruct the assayed variant sequence.


organism: Chelativorans sp. BNC1

sequence_source: KEGG mes:Meso_3050 amino-acid sequence; KEGG orthology K06033 arylmalonate decarboxylase [EC:4.1.1.76]

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


enzyme_display_name: DNA-formamidopyrimidine glycosylase

organism: Escherichia coli

substrate_name: 23mer oligonucleotide duplex containing 8-oxoguanine

enzyme: DNA-formamidopyrimidine glycosylase


substrate: 23mer oligonucleotide duplex containing 8-oxoguanine


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

proof_lines:
wild-type, pH 7.5, 30°C
wild-type, pH 7.5, 37°C


substrate_name: 13mer oligonucleotide duplex containing 8-oxoguanine


substrate: 13mer oligonucleotide duplex containing 8-oxoguanine


substrate_name: DNA containing a broken link p(-2)-G(-1)


substrate_name: DNA containing ring-opened N7-methylguanine residues

proof_lines: pH 7.5, 37°C, 23-oligomer, wild-type Fpg

proof_lines: pH 7.5, 37°C, 24-oligomer, wild-type Fpg

proof_lines: pH 7.5, 20°C, 24-oligomer DNA containing AP sites, lyase activity, wild-type Fpg


proof_lines: pH 7.5, 37°C, 23-oligomer, K155A mutant Fpg

proof_lines: pH 7.5, 37°C, 24-oligomer, K155A mutant Fpg

proof_lines: pH 7.5, 20°C, 24-oligomer DNA containing AP sites, lyase activity, K155A mutant Fpg

substrate: DNA containing ring-opened N7-methylguanine residues


organism: Homo sapiens


enzyme_display_name: phosphorylase kinase

substrate_name: phosphorylase b

assay_conditions_summary: cofactor ATP

enzyme: phosphorylase kinase

substrate: phosphorylase b


organism: Oryctolagus cuniculus

substrate_name: ATP

assay_conditions_summary: pH 8.2; cofactor ATP

proof_lines:
at pH 8.2 in the presence of calcium
Raw SKiD Env: Temp=-----, pH=8.2

substrate: ATP


proof_lines: at different phosphorylase b concentrations


assay_conditions_summary: pH 7; cofactor ATP

proof_lines:
in the presence of glycogen
pH 7, activated enzyme
pH 8.5


proof_lines: Ser-Asp-Gln-Glu-Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, Lys-Arg-Lys-Gln-Ile-Ser-Val-Asp, nonactivated enzyme, pH 8.2


assay_conditions_summary: pH 8.2; 303.15 K; cofactor ATP

proof_lines:
gammadelta subunit complex
alphagammadelta subunit complex
nonactivated enzyme


mutation_signature: phosphorylase b, truncated form of phosphorylase kinase gamma subunit phosphorylase b, truncated form of phosphorylase kinase gamma subunit


organism: Rattus norvegicus

proof_lines: activated rabbit skeletal muscle enzyme, pH 8.2

proof_lines: nonactivated rabbit skeletal muscle enzyme, pH 6


organism: Saccharomyces cerevisiae

substrate_name: GTP

substrate: GTP


organism: Squalus acanthias

proof_lines: dogfish phosphorylase b, pH 8.2, dogfish enzyme


substrate_name: DNA

proof_lines: pH 7.5, 25°C, DNA containing an apurininc/apyrimidinic site

substrate: DNA


substrate_name: DNA containing 5,6-dihydrouracil

substrate: DNA containing 5,6-dihydrouracil


substrate_name: DNA containing 8-oxo-guanine residues

substrate: DNA containing 8-oxo-guanine residues


proof_lines: pH 7.8, 37°C, 34-oligomer, wild-type Fpg


substrate_name: DNA containing 8-hyroxyguanine

proof_lines: pH 7.8, 37°C, 34-oligomer, K57R mutant Fpg

proof_lines: pH 7.4, 37°C, K57R mutant Fpg, from DNA gamma-irradiated under NO2

substrate: DNA containing 8-hyroxyguanine


substrate_name: DNA containing 8-hydroxyguanine residues

proof_lines: pH 7.8, 37°C, 34-oligomer, K57G mutant Fpg

proof_lines: pH 7.4, 37°C, K57G mutant Fpg, from DNA gamma-irradiated under NO2


enzyme_display_name: nardilysin

enzyme: nardilysin


organism: Mus musculus


proof_lines: pH 7.0, hydrolysis of the peptide series 2-aminobenzoyl-GGFLRKXGQ-ethylenediamine-2,4-dinitrophenyl

proof_lines: pH 7.0, hydrolysis of the peptide series 2-aminobenzoyl-GGFXRKVGQ-ethylenediamine-2,4-dinitrophenyl

proof_lines: pH 7.0, hydrolysis of the peptide series 2-aminobenzoyl-GGFIXXVGQ-ethylenediamine-2,4-dinitrophenyl


enzyme_display_name: lactoylglutathione lyase

enzyme: lactoylglutathione lyase


substrate_name: trypanothione

substrate: trypanothione


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Glycine max


substrate_name: glutathione-phenylglyoxal

substrate: glutathione-phenylglyoxal


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


organism: Leishmania donovani

substrate_name: reduced trypanothione

proof_lines: recombinant enzyme, pH 7.2, room temperature

substrate: reduced trypanothione


organism: Leishmania infantum


organism: Leishmania major


proof_lines:
purified enzyme, pH 7.0, 27°C
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=27°C, pH=7


substrate_name: Unknown

proof_lines: inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics from 0.5 to 2 microM, competitive inhibition, pH 7.0, 30°C

proof_lines: inhibitor of osteoclast differentiation, osteoclastogenesis, inhibition kinetics, competitive inhibition, pH 7.0, 30°C

substrate: Unknown


organism: Oryza sativa Japonica Group

substrate_name: (R)-S-lactoylglutathione

proof_lines: recombinant enzyme, pH 7.2, temperature not specified in the publication

substrate: (R)-S-lactoylglutathione


organism: Plasmodium falciparum


organism: Pseudomonas aeruginosa


substrate_name: Methylglyoxal; Reduced glutathione

substrate: Methylglyoxal; Reduced glutathione


sequence_source: UniProt P50107 accession anchor checked directly; row-specific E163Q sequence not reconstructed.


sequence_source: UniProt P50107 accession anchor checked directly; selected grouped row still lacks resolved sequence.


sequence_source: UniProt P50107 accession anchor checked directly; selected row still lacks resolved sequence.


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines:
37°C, pH 6.6
presence of Ni2+, 37°C, pH 6.6
presence of Co2+, 37°C, pH 6.6


organism: Schizosaccharomyces pombe


substrate_name: Reduced glutathione; Methylglyoxal / Reduced glutathione; Phenylglyoxal


organism: Aloe vera


organism: Aspergillus niger


organism: Aves


organism: Bos taurus


organism: Brassica sp.


organism: Chlamydomonas reinhardtii


organism: Cyberlindnera mrakii


organism: Escherichia coli

proof_lines:
in the presence of Fe2+
in the presence of Mn2+
in the presence of Co+


organism: Glycine max


organism: Homo sapiens

proof_lines: in the presence of increasing amounts of inhibitor at different concentrations of the substrates methylglyoxal and glutathione, Dixon plot analysis, significantly lower inhibition than that with curcumin, competitive inhibition, pH 7.0, 30°


organism: Leishmania braziliensis

proof_lines: pH and temperature not specified in the publication


organism: Mammalia


organism: Mytilus galloprovincialis


organism: Neisseria meningitidis

assay_conditions_summary: pH 7

proof_lines:
presence of Co2+, pH 7.0
presence of Ni2+, pH 7.0
pH 7.0, 0.5 mM NiCl2


organism: Onchocerca volvulus


organism: Oryza sativa


organism: Ovis aries


organism: Pituophis catenifer


organism: Plasmodium falciparum


organism: Pseudomonas aeruginosa


organism: Pseudomonas putida


organism: Rana catesbeiana


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae

proof_lines: the apparent kinetic parameters are determined by using hemithioacetal as substrate, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal

proof_lines: the apparent kinetic parameters are determined by varying the hemithioacetal concentration between 0.3 and 1.5 mM, which is obtained by the nonenzymatic reaction between glutathione and methylglyoxal


organism: Schizosaccharomyces pombe

substrate_name: glutathione

substrate: glutathione


organism: Squalus acanthias


organism: Sus scrofa

substrate_name: Phenylglyoxal; Reduced glutathione

substrate: Phenylglyoxal; Reduced glutathione


organism: Trypanosoma cruzi


organism: Yersinia pestis

proof_lines:
presence of Co2+, pH 7.0
presence of Ni2+, pH 7.0
pH 7.0, 0.5 mM CoCl2


enzyme_display_name: omptin

organism: Escherichia coli

substrate_name: IAA-Arg-Arg-p-nitroanilide

enzyme: omptin

substrate: IAA-Arg-Arg-p-nitroanilide


proof_lines:
22°C, recombinant mutant variant 1.3.19
22°C, recombinant mutant variant 1.2.19


proof_lines: pH 6.5, 37°C, wild-type, purified from outer membrane and wild-type, recombinant expressed

proof_lines: pH 6.5, 37°C, wild-type, recombinant expressed in Escherichia coli


organism: Phanerodontia chrysosporium


substrate_name: WEEGGRRIGRGGK

proof_lines: used as a control substrate for determination of the activity of OmpT protease

proof_lines: different cleavage sites used by OmpP or OmpT proteases

substrate: WEEGGRRIGRGGK


substrate_name: Ac-GLLGDFFRKSKEKIGC

substrate: Ac-GLLGDFFRKSKEKIGC


enzyme_display_name: hydroxyacylglutathione hydrolase

organism: Arabidopsis thaliana

substrate_name: H2O; (R)-S-Lactoylglutathione

enzyme: hydroxyacylglutathione hydrolase

substrate: H2O; (R)-S-Lactoylglutathione


substrate_name: S-Lactoylglutathione

proof_lines:
25°C, pH 7.2
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.2

substrate: S-Lactoylglutathione


proof_lines: recombinant enzyme grown in medium not supplemented with metal ions, pH 7.2, 25°C

proof_lines: recombinant enzyme grown in medium supplemented with Mn2+, pH 7.2, 25°C

proof_lines: recombinant enzyme grown in medium supplemented with Fe2+, pH 7.2, 25°C


organism: Brassica juncea


organism: Homo sapiens

proof_lines:
enzyme from erythrocytes
recombinant enzyme


organism: Leishmania donovani

substrate_name: (R)-S-Lactoyltrypanothione; H2O

substrate: (R)-S-Lactoyltrypanothione; H2O


organism: Leishmania infantum

substrate_name: H2O; (R)-S-Lactoyltrypanothione

substrate: H2O; (R)-S-Lactoyltrypanothione


organism: Mus musculus


organism: Plasmodium falciparum

substrate_name: (R)-S-Lactoylglutathione; H2O

substrate: (R)-S-Lactoylglutathione; H2O


substrate_name: H2O; S-Lactoylglutathione

substrate: H2O; S-Lactoylglutathione


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


organism: Salmonella typhimurium


organism: Trypanosoma brucei

substrate_name: H2O; Lactoylglutathione

proof_lines:
pH 7.2, 25°C
recombinant enzyme, pH 7.2, 25°C
above, recombinant enzyme, pH 7.2, 25°C

substrate: H2O; Lactoylglutathione


proof_lines: recombinant cytosolic isozyme, minimal medium, pH 7.2, 25°C

proof_lines: pH 7.2, 25°C, growth on minimal medium without added metal ion

proof_lines: recombinant cytosolic isozyme, medium with Zn added, pH 7.2, 25°C


organism: Bos taurus

proof_lines: mitochondrial isozyme, pH 7.2, 25°C, in presence of cardiolipin

proof_lines: mitochondrial isozyme, pH 7.2, 25°C, in presence of dioleoyl phosphatidic acid


organism: Aves


organism: Candida albicans


organism: Mammalia


organism: Pituophis catenifer


organism: Rana catesbeiana


organism: Salmonella enterica

substrate_name: S-D-lactoylglutathione

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: S-D-lactoylglutathione


organism: Squalus acanthias


enzyme_display_name: lysyl endopeptidase

organism: Unknown

substrate_name: N-tosyl-L-Lys methyl ester

enzyme: lysyl endopeptidase

substrate: N-tosyl-L-Lys methyl ester


organism: Achromobacter lyticus

sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_UniProtKB:P15636_and_PMID:11820934 and applied mutation signature W169L with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_UniProtKB:P15636_and_PMID:11820934 and applied mutation signature W169G with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_UniProtKB:P15636_and_PMID:11820934 and applied mutation signature W169V with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature H210A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


sequence_source: UniProtKB:P15636 direct follow-up


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_UniProtKB:P15636_and_PMID:11820934 and applied mutation signature W169Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_UniProtKB:P15636_and_PMID:11820934 and applied mutation signature W169H with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed_variant_sequence_from_UniProtKB:P15636_and_PMID:11820934 and applied mutation signature W169A with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W169F matches the mutant residue at offset +8 and the reference residue at offset -15; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


substrate_name: benzoyl-Lys-p-nitroanilide

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

assay_conditions_summary: pH 9

proof_lines: pH 9, rate of carboxyl oxygen exchange reaction by Lys-C is accelerated at acidic pH conditions.

substrate: benzoyl-Lys-p-nitroanilide


organism: Porphyromonas gingivalis

substrate_name: tosyl-Gly-Pro-Lys-p-nitroanilide

substrate: tosyl-Gly-Pro-Lys-p-nitroanilide


organism: Pseudomonas aeruginosa


enzyme_display_name: tyrosine-ester sulfotransferase

substrate_name: phenol

enzyme: tyrosine-ester sulfotransferase

substrate: phenol


organism: Homo sapiens

proof_lines:
isoenzyme HAST4
isoenzyme HAST4v


organism: Euglena gracilis

proof_lines:
L-tyrosine ethyl ester, pH 7, 37°C
L-tyrosinamide, pH 7, 37°C
pH 7, 37°C


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P17988/ST1A1_RAT plus PMID 15100179 mutation identity; variant reconstructed by applying F138A to the canonical sequence. and applied mutation signature F138A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P17988/ST1A1_RAT plus PMID 15100179 mutation identity; variant reconstructed by applying Y236A to the canonical sequence. and applied mutation signature Y236A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P17988/ST1A1_RAT plus PMID 15100179 mutation identity; variant reconstructed by applying F77A to the canonical sequence. and applied mutation signature F77A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P17988/ST1A1_RAT; PMID 15100179 identifies rat AST IV as tyrosine-ester sulfotransferase/ST1A1 and the selected row is wild type.


substrate_name: N-acetylserotonin

sequence_source: UniProtKB reviewed accession P17988/ST1A1_RAT; PMID 6946725 and IUBMB EC 2.8.2.9 identify rat liver aryl sulfotransferase IV context.

substrate: N-acetylserotonin


enzyme_display_name: bacterial luciferase

organism: Vibrio harveyi

sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F117 to A and applied mutation signature F117A to reconstruct the assayed variant sequence.

enzyme: bacterial luciferase


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F49 to D and applied mutation signature F49D to reconstruct the assayed variant sequence.


substrate_name: decanal

sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F114 to A and applied mutation signature F114A to reconstruct the assayed variant sequence.

substrate: decanal


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F114 to S and applied mutation signature F114S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F46 to S and applied mutation signature F46S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F49 to S and applied mutation signature F49S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F46 to Y and applied mutation signature F46Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F117 to Y and applied mutation signature F117Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F114 to D and applied mutation signature F114D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue F114 to Y and applied mutation signature F114Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue E328 to F and applied mutation signature E328F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07740 FASTA; alpha-chain variant reconstructed from canonical residue A74 to G and applied mutation signature A74G to reconstruct the assayed variant sequence.


organism: Photobacterium phosphoreum

substrate_name: FMNH

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

substrate: FMNH


organism: Photorhabdus luminescens

assay_conditions_summary: cofactor FMN

proof_lines:
myristic aldehyde as second substrate
dodecanoic aldehyde as second substrate
decanoic aldehyde as second substrate


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

proof_lines: recombinant mutant alphaF261S, pH 7.0, 25°C

proof_lines: recombinant mutant alphaG275I, pH 7.0, 25°C

proof_lines: recombinant mutant alphaG284P, pH 7.0, 25°C


proof_lines: recombinant wild-type enzyme, pH 7.0, 25°C

proof_lines: recombinant wild type enzyme, at 22°C, pH not specified in the publication


proof_lines: pH 7.0, 23°C, recombinant mutants F49D, F117A, and F49A


proof_lines: pH 7.0, 23°C, recombinant mutants F46Y, F114A, F117Y, and F114Y


proof_lines: pH 7.0, 23°C, recombinant mutants E328Q and E328H


proof_lines: pH 7.0, 23°C, recombinant mutants E328L and E328A


assay_conditions_summary: pH 7; 295.15 K; buffer system; cofactor NADPH

proof_lines: pH 7.0, temperature not specified in the publication

proof_lines: in the presence of different flavin concentrations, 0.001 mM Fre oxidoreductase, 10 mM decanal, and 0.01 mM NADPH and 0.005 mM luciferase


enzyme_display_name: protein-tyrosine sulfotransferase

substrate_name: statherin

enzyme: protein-tyrosine sulfotransferase

substrate: statherin


organism: Danio rerio

substrate_name: ATEYEFLDYDFL

substrate: ATEYEFLDYDFL


substrate_name: [Y+3 peptide]-L-tyrosine

proof_lines:
isoform TPST2, at pH 7.5 and 25°C
pH 6.0, 30°C, isozyme TPST-2
disulfation of sY15CCR8

substrate: [Y+3 peptide]-L-tyrosine


proof_lines:
isoform TPST1, at pH 7.5 and 25°C
recombinant enzyme TPST1, pH 6.0, 30°C
monosulfation of non CCR8


organism: Asparagus officinalis

substrate_name: EEFHTDYIYTQDVK

mutation_signature: truncated sequence of preprophytosulfokinase / truncated sequence of preprophytosulfokinase

proof_lines: PP-PSK-(74-87), truncated sequence of preprophytosulfokinase, pH 7, 30°C

substrate: EEFHTDYIYTQDVK


organism: Bos taurus

proof_lines:
+ peptide CCKI
pH 6.5, 30°C


organism: Drosophila melanogaster

substrate_name: P-selectin glycoprotein ligand-1

assay_conditions_summary: pH 6.5; 310.15 K; buffer 50 mM MES

proof_lines: using P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C

proof_lines: using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as cosubstrate, in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C

proof_lines: using glutathione S-transferase-tagged P-selectin glycoprotein ligand-1 as substrate,in 50 mM MES buffer (pH 6.5), 5 mM 2-mercaptoethanol, at 37°C

substrate: P-selectin glycoprotein ligand-1


organism: Hirudo medicinalis

substrate_name: peptide Hir-(57-65)

substrate: peptide Hir-(57-65)


proof_lines: with VTDsYYYPDI as cosubstrate, in 20 mM MOPS, at pH 7.5, 100 mM NaCl, at 30°C


organism: Oryza sativa


proof_lines: acidic amino acid polymer, pH 6.2, 37°C, absence of prostaglandin E2


enzyme_display_name: N-terminal methionine N(alpha)-acetyltransferase NatC

organism: Saccharomyces cerevisiae

substrate_name: MFHLVGSRRR

substrate: MFHLVGSRRR


enzyme: N-terminal methionine N(alpha)-acetyltransferase NatC


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: MWHLVGSRRR

proof_lines:
wild-type, pH 7.5, 25°C
wild-type, below 0.02 mM, pH 7.5, 25°C
wild-type, below 0.020, pH 7.5, 25°C

substrate: MWHLVGSRRR


organism: Schizosaccharomyces pombe

substrate_name: MLRFVTKRWGRPVGRRRRP

substrate: MLRFVTKRWGRPVGRRRRP


enzyme_display_name: prolyl oligopeptidase

organism: Aeromonas caviae

enzyme: prolyl oligopeptidase


substrate_name: Unknown

proof_lines:
pH 7.5, 37°C, recombinant enzyme
pH 7, 30°C

substrate: Unknown


organism: Leishmania infantum

proof_lines: presence of 5 mM dithiothreitol, pH 7.5, 37°C


organism: Sphaerobacter thermophilus


organism: Sus scrofa

proof_lines:
pH 7.0, mutant enzyme D641A
pH 7.0, mutant enzymeD641A


substrate_name: benzyloxycarbonyl-Gly-Pro-p-nitrophenol

proof_lines:
pH 7.0, mutant enzyme D641N
pH 7.0, mutante enzyme D641N

substrate: benzyloxycarbonyl-Gly-Pro-p-nitrophenol


proof_lines:
pH 7.0, wild-type enzyme
pH 8.0, wild-type enzyme


proof_lines:
at 25°C between pH 5.5 and 9.5
brain


organism: Thermococcus onnurineus


organism: Trypanosoma brucei brucei

proof_lines:
in presence of DTT
in absence of DTT


organism: Trypanosoma cruzi

proof_lines:
pH 7.5, recombinant enzyme
pH 7.5, native enzyme


organism: Unknown


organism: Aspergillus oryzae

proof_lines:
at pH 5.0 and 35°C
at 40°C and pH 4.0


substrate_name: thyrotropin-releasing hormone

substrate: thyrotropin-releasing hormone


organism: Coprinopsis clastophylla


organism: Elizabethkingia meningoseptica

substrate_name: benzyloxycarbonyl-Ala-Ala-p-nitrophenol

proof_lines:
pH 7.0, 37°C
fluorogenic assay
chromogenic assay

substrate: benzyloxycarbonyl-Ala-Ala-p-nitrophenol


organism: Escherichia coli

substrate_name: furylacryloyl-Ala-Pro

substrate: furylacryloyl-Ala-Pro


organism: Eurygaster integriceps