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).


enzyme_display_name: N-acetyllactosaminidase

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

substrate_name: pNP-LNB

source_db: uniprot

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

enzyme: N-acetyllactosaminidase

substrate: pNP-LNB

source: uniprot


enzyme_display_name: levansucrase

organism: Fructilactobacillus sanfranciscensis

substrate_name: sucrose (at 28 degrees Celsius)

kcat_display: Not reported

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

data_origin: experimental

enzyme: levansucrase

substrate: sucrose (at 28 degrees Celsius)


enzyme_display_name: fumarylacetoacetase

organism: Arabidopsis thaliana

enzyme: fumarylacetoacetase


organism: Bacillus subtilis

substrate_name: sucrose

source_db: brenda

km_display: Not reported

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

mutation_type: substitution

substrate: sucrose

source: brenda


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


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

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

substrate: H2O; Phosphorylase a


organism: Rattus norvegicus

substrate_name: Unknown

ki_unit: mM

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+

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

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

assay_conditions_summary: cofactor NADPH

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)

assay_conditions_summary: cofactor ADP


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)

assay_conditions_summary: cofactor 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


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

assay_conditions_summary: pH 7

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

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

source_databases_merged: brenda skid

enzyme: glutathione-dependent peroxiredoxin


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

assay_conditions_summary: cofactor CoA


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

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

source_db: oed

enzyme: tubulin-glutamate carboxypeptidase

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

source: oed


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)

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.


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]


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


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

mutation_type: truncation


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

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

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


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

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

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

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


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

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


mutation_type: deletion


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


organism: Galerina marginata

substrate_name: IWGIGCNPWTAEHVDQTLASGNDIC

proof_lines:
at pH 8.0 and 37°C
at pH 8.0 and 20°C

substrate: IWGIGCNPWTAEHVDQTLASGNDIC


organism: Homo sapiens

proof_lines: mutant enzyme T202C/T590C, at pH 8.0 and 25°C


proof_lines:
pH 8.0, 37°C
human brain
intracellular enzyme


organism: Lyophyllum cinerascens

substrate_name: Benzyloxycarbonyl-Gly-Pro-Ala

substrate: Benzyloxycarbonyl-Gly-Pro-Ala


organism: Mus musculus

proof_lines: pH 7.4, 37°C, enzyme from thioglycollate-elicited macrophage

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: flavin-containing monooxygenase

substrate_name: Ethionamide

enzyme: flavin-containing monooxygenase

substrate: Ethionamide


substrate_name: thiacetazone

assay_conditions_summary: pH 9.5; 310.15 K; buffer 0.1 M potassium phosphate

substrate: thiacetazone


substrate_name: methyl p-tolyl sulfide

assay_conditions_summary: pH 9; 310.15 K; cofactor NADPH

substrate: methyl p-tolyl sulfide


substrate_name: NADPH

substrate: NADPH


substrate_name: calcitonin gene-related peptide

proof_lines: mutant D35A/K196A, diserine mutant of calcitonin gene-related peptide

proof_lines: mutant D35A/K196A, shorter peptide of calcitonin gene-related peptide

proof_lines: mutant D35A/K196A, full length calcitonin gene-related peptide

substrate: calcitonin gene-related peptide


proof_lines: wild type enzyme, full length calcitonin gene-related peptide

proof_lines: wild type enzyme, diserine mutant of calcitonin gene-related peptide

proof_lines: wild type enzyme, shorter peptide of calcitonin gene-related peptide


organism: Myxococcus xanthus


organism: Oryctolagus cuniculus


organism: Ovis aries

substrate_name: benzyloxycarbonyl-Gly-Pro-D-Leu

substrate: benzyloxycarbonyl-Gly-Pro-D-Leu


organism: Pleurotus eryngii

proof_lines: mutant enzyme M203Q/M570Q, at pH 8.0 and 25°C


proof_lines: oxidized wild type enzyme, at pH 8.0 and 25°C


proof_lines: mutant enzyme M142Q/M203Q/M570Q/M620Q, at pH 8.0 and 25°C


assay_conditions_summary: pH 8.4; 310.15 K; buffer 0.1 M potassium phosphate

proof_lines: isozyme FMO5, in 0.1 M potassium phosphate buffer (pH 8.4) at 37°C


substrate_name: clomiphene

proof_lines: recombinant His-tagged full-length mutant E158K, pH 7.4, 37°C

proof_lines: recombinant His-tagged truncated mutant E158K, pH 7.4, 37°C

substrate: clomiphene


proof_lines: recombinant His-tagged truncated mutant V257M, pH 7.4, 37°C

proof_lines: recombinant His-tagged full-length mutant V257M, pH 7.4, 37°C


substrate_name: tamoxifen

proof_lines: recombinant His-tagged truncated mutant E308G, pH 7.4, 37°C

proof_lines: recombinant His-tagged full-length mutant E308G, pH 7.4, 37°C

substrate: tamoxifen


substrate_name: Benzydamine

proof_lines: recombinant His-tagged full-length wild-type enzyme, pH 7.4, 37°C

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

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

substrate: Benzydamine


organism: Methylophaga aminisulfidivorans

substrate_name: indole

assay_conditions_summary: pH 8

proof_lines: wild-type, pH 8.0, temperature not specified in the publication

substrate: indole


proof_lines: mutant Y207S, pH 8.0, temperature not specified in the publication


organism: Rattus norvegicus

substrate_name: seleno-L-methionine

proof_lines:
pH 7.6, 37°C, purified FMO3 from liver
pH 7.6, 37°C, purified FMO3 from kidney

substrate: seleno-L-methionine


proof_lines: pH 8.5, 37°C, recombinant mutant isozyme FMO3 E158K

proof_lines: pH 8.5, 37°C, recombinant isozyme FMO1 and recombinant mutant isozyme FMO3 E158K


substrate_name: ethylenethiourea

proof_lines: pH 8.5, 37°C, recombinant wild-type isozyme FMO3

proof_lines: pH 8.4, 37°C, recombinant wild-type His6-tagged MBT-fusion-FMO1

substrate: ethylenethiourea


proof_lines: pH 8.5, 37°C, detergent is a minimal detergent, commercial recombinant FMO3

proof_lines: pH 8.5, 37°C, detergent is CHAPS, recombinant MBP-FMO3


proof_lines:
pH 8.5, FMO1
37°C, isozyme FMO3
pH 8.5, FMO2


organism: Callithrix jacchus

proof_lines: isoform FMO3, pH and temperature not specified in the publication


organism: Canis lupus familiaris

substrate_name: imipramine

substrate: imipramine


substrate_name: fenthion

substrate: fenthion


substrate_name: mercaptoimidazole

proof_lines: pH 8.4, 37°C, recombinant mutant H360P His6-tagged MBT-fusion-FMO1

substrate: mercaptoimidazole


proof_lines: pH 8.4, 37°C, recombinant mutant L360P His6-tagged MBT-fusion-FMO3


substrate_name: chlorpromazine

proof_lines: pH 8.4, 37°C, recombinant mutant L360A His6-tagged MBT-fusion-FMO3

substrate: chlorpromazine


proof_lines: pH 8.4, 37°C, recombinant mutant L360H His6-tagged MBT-fusion-FMO3


proof_lines: pH 8.4, 37°C, recombinant mutant L360Q His6-tagged MBT-fusion-FMO3


substrate_name: Methimazole

substrate: Methimazole


organism: Methylophaga sp.


proof_lines: pH 8.0, 25°C, recombinant C78I/Y207W/W319A


organism: Mycobacterium tuberculosis

proof_lines: recombinant EtaA, pH 9.0, 37°C, thiacetazone carbodiimide formation

proof_lines: recombinant EtaA, pH 9.0, 37°C, thiacetazone sulfinic acid formation


substrate_name: L-methionine

proof_lines:
recombinant FMO2, pH 7.4, 37°C
recombinant FMO1, pH 7.4, 37°C

substrate: L-methionine


organism: Squalus acanthias

substrate_name: N,N-Dimethylaniline

substrate: N,N-Dimethylaniline


organism: Sus scrofa

substrate_name: N-Aminopiperidine

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

substrate: N-Aminopiperidine


organism: Pyrococcus furiosus


substrate_name: Unknown

proof_lines:
rat brain
rat cortex

substrate: Unknown


organism: Setaria cervi


proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme and mutant C255T


organism: Bacillus subtilis

substrate_name: lichenan

proof_lines: pH 6.4, 40°C, substrate from Hordeum vulgare

proof_lines: pH 6.4, 40°C, purified recombinant His-tagged enzyme, substrate from Hordeum vulgare

substrate: lichenan


organism: Laceyella putida

substrate_name: laminaritetraose

substrate: laminaritetraose


organism: Acetivibrio thermocellus

substrate_name: beta-Glucan

substrate: beta-Glucan


organism: Aplysia kurodai


organism: Botrytis cinerea

substrate_name: D-glucose

substrate: D-glucose


organism: Cyberlindnera jadinii

substrate_name: Laminarin

substrate: Laminarin


organism: Paenibacillus macerans


organism: Periplaneta americana


organism: Rasamsonia emersonii

substrate_name: Barley beta-glucan

proof_lines: pH 5, 50°C, soluble, from barley, EG VII

substrate: Barley beta-glucan


organism: Rhizoctonia solani

substrate_name: short-chain pachyman

substrate: short-chain pachyman


organism: Rhizomucor miehei


organism: Thermothelomyces heterothallicus


enzyme_display_name: tryptophan synthase

organism: Arabidopsis thaliana

substrate_name: L-serine

proof_lines: recombinant isozyme AtTSBtype2, pH 8.2, 30°C

enzyme: tryptophan synthase

substrate: L-serine


organism: Archaeoglobus fulgidus

substrate_name: indole

substrate: indole


organism: Chlamydia trachomatis

proof_lines: TrpAB complex, pH 8.5, temperature not specified in the publication

proof_lines: isolated TrbB subunit, pH 8.5, temperature not specified in the publication


organism: Escherichia coli

proof_lines: alpha-subunit, mutant T183V/A158G, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant T183V/A180G, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant T183V/A71G, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant T183V/A59G, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant T183V, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant T183V/A185G, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant A71G, pH 7.6, 25°C


proof_lines: alpha-subunit, mutant T183V/A67G, pH 7.6, 25°C


proof_lines: reaction of TrpA/TrpB complex, wild-type, pH 7.5, temperature not specified in the publication


proof_lines: cosubstrate 5-hydroxyindole, wild-type, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant A67M, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant L80H, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant D381G, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant N64G/S352P, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant P257R, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant V231S/K382G, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant H313F, pH 8.5, 35Â°C


proof_lines: cosubstrate 5-hydroxyindole, mutant T319S, pH 8.5, 35Â°C


proof_lines: reaction of TrpA/TrpB complex, mutant A198W, pH 7.5, temperature not specified in the publication

proof_lines: reaction of subunit TrpB, mutant A198W, pH 7.5, temperature not specified in the publication

proof_lines: reaction of subunit TrpA, mutant A198W, pH 7.5, temperature not specified in the publication


organism: Psilocybe cubensis


organism: Pyrococcus furiosus

proof_lines: subunit TrpB1, mutant E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C


proof_lines: subunit TrpB1, mutant T292S, pH 8.0, 75°C


proof_lines:
subunit TrpB1, wild-type, pH 8.0, 75°C
wild-type, pH 8.0, 75°C
wild-type holoenzyme, pH 8.0, 75°C


proof_lines: subunit TrpB1, mutant P12L/E17G/I68V/F274S/T292S/T321A, pH 8.0, 75°C


proof_lines: cosubstrate L-serine, pH 8.0, temperature not specified in the publication

proof_lines: cosubstrate L-threonine, pH 8.0, temperature not specified in the publication


organism: Saccharolobus solfataricus

substrate_name: O-phospho-L-serine

proof_lines:
isoform TrpB2a, pH 7.5, 60°C
isoform TrpB2i, pH 7.5, 60°C

substrate: O-phospho-L-serine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: mutant Q114A, pH not specified in the publication, temperature not specified in the publication


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


organism: Thermococcus kodakarensis

proof_lines: pH 7.5, 85°C, the reaction is catalyzed by the complex of TrpB1 and TrpA

proof_lines: pH 7.5, 85°C, he reaction is catalyzed by TrpB1


organism: Thermotoga maritima


organism: Zea mays

proof_lines: recombinant isozyme TSB type 2, pH 8.2, 30°C


proof_lines: competitive in the catalysis of indoleglycerol phosphate cleavage


organism: Lathyrus oleraceus

proof_lines:
cosubstrate L-Ser
cosubstrate indole


organism: Mycobacterium tuberculosis


organism: Bacillus subtilis


organism: Bos taurus

proof_lines: pH not specified in the publication, temperature not specified in the publication, recombinant wild-type enzyme and mutant D396A


proof_lines: pH not specified in the publication, temperature not specified in the publication, recombinant mutant Y115A


proof_lines: pH not specified in the publication, temperature not specified in the publication, recombinant mutant G319D


proof_lines: pH not specified in the publication, temperature not specified in the publication, recombinant mutant K311A


substrate_name: (Polyphosphate)n

substrate: (Polyphosphate)n


substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


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


organism: Helicobacter pylori


organism: Homo sapiens

substrate_name: dCMP

assay_conditions_summary: pH 7; 310.15 K; cofactor ADP

proof_lines:
pH 7.0, 37°C, in presence of 1 mM ADP
pH 7.0, 37°C, without ADP

substrate: dCMP


substrate_name: Inosine

assay_conditions_summary: pH 7.4; 310.15 K; buffer mapping; cofactor ATP

proof_lines: presence of 2 mM ATP, Tris-buffer, pH 7.4

proof_lines: presence of 0.4 mM 2,3-bisphosphoglycerate, Tris-buffer, pH 7.4

proof_lines: presence of 2 mM ATP, phosphate-buffered saline, pH 7.4

substrate: Inosine


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


proof_lines: pH and temperature not specified in the publication


organism: Legionella pneumophila

proof_lines: biphasic kinetic profile, pH 8.0, temperature not specified in the publication

proof_lines: sigmoidal kinetic profile, pH 8.0, temperature not specified in the publication


organism: Mus musculus


organism: Ophiocordyceps sinensis

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


organism: Phaseolus vulgaris

substrate_name: TMP

substrate: TMP


organism: Pseudomonas aeruginosa


organism: Rattus norvegicus


organism: Streptococcus pyogenes

proof_lines: Km above 0.8 mM, mutant enzyme R392A, at pH 7.4 and 37°C


organism: Trichinella spiralis


organism: Xylella fastidiosa

substrate_name: 4-nitrophenyl phosphate

substrate: 4-nitrophenyl phosphate


enzyme_display_name: penicillin amidase

organism: Achromobacter xylosoxidans

substrate_name: penicillin G

enzyme: penicillin amidase

substrate: penicillin G


substrate_name: cefamandole

proof_lines: mutant alphaR141A/alphaF142I/betaF24G, pH 6.5, 25°C

substrate: cefamandole


substrate_name: (+)-methyl mandelate

substrate: (+)-methyl mandelate


organism: Escherichia coli

proof_lines:
alphaF146Y mutant protein, pH 7.5, 25°C
alphaF146A mutant protein, pH 7.5, 25°C
betaF24A mutant protein, pH 7.5, 25°C


substrate_name: D-4-hydroxyphenylglycine amide

proof_lines: pH 7.0, 30°C, analysis of complex kinetic parameters alpha, beta, gamma

proof_lines: enzyme immobilized on amino functionalized magnetic Ni(0.3)Mg(0.4)Zn(0.3)Fe2O4 nanoparticles, pH and temperature not specified in the publication

substrate: D-4-hydroxyphenylglycine amide


organism: Kluyvera cryocrescens


organism: Lysinibacillus sphaericus

substrate_name: Penicillin V

proof_lines: pH 6.0, 37°C, mutant enzyme T63S/S110C/N198Y

substrate: Penicillin V


organism: Priestia megaterium


organism: Providencia rettgeri

substrate_name: amoxicillin

proof_lines: pH 7.0, 30°C, cross-linked enzyme aggregates

proof_lines: pH 7.0, 30°C, poly-lysine supported cross-linked enzyme aggregates

substrate: amoxicillin


organism: Rhizobium viscosum


organism: Streptomyces lavendulae subsp. lavendulae

substrate_name: penicillin F

substrate: penicillin F


organism: Streptomyces mobaraensis


organism: Thermus thermophilus

proof_lines: pH 5.5, 65°C, recombinant mutant L188F/S189F

proof_lines: pH 5.5, 65°C, recombinant mutants L188F and S189F


substrate_name: penicillin K

proof_lines: pH 5.5, 65°C, recombinant wild-type enzyme

substrate: penicillin K


proof_lines: pH 5.5, 65°C, recombinant mutant L188F/L24F/I57F


proof_lines: pH 5.5, 65°C, recombinant mutant L24F/I57F


organism: uncultured bacterium

substrate_name: ampicillin

substrate: ampicillin


organism: Bos taurus

proof_lines:
isoenzyme 5-NT-3
isoenzyme 5-NT-1
isoenzyme 5-NT-2 and 5-NT-4


organism: Unknown


enzyme_display_name: aryl sulfotransferase

substrate_name: Unknown

proof_lines: pH 7.4, 25°C, recombinant SULT1A1, method B

proof_lines: pH 7.4, 25°C, recombinant SULT1A1, method A

enzyme: aryl sulfotransferase

substrate: Unknown


substrate_name: 3'-phosphoadenylyl sulfate

proof_lines: mutant W53L, pH 7.4, temperature not specified in the publication

substrate: 3'-phosphoadenylyl sulfate


proof_lines: mutant W53Y, pH 7.4, temperature not specified in the publication


proof_lines: wild-type, pH 7.4, temperature not specified in the publication


proof_lines: mutant W53A, pH 7.4, temperature not specified in the publication


organism: Canis lupus familiaris

substrate_name: dopamine

substrate: dopamine


organism: Homo sapiens

proof_lines: wild-type SULT1A3: native enzyme, and recombinant from COS-7 cells, Escherichia coli, Saccharomyces cerevisiae, pH 7.4, 37°C

proof_lines: wild-type SULT1A3: purified recombinant enzyme from Escherichia coli, pH 7.4, 37°C


assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM Tris/HCl

proof_lines:
SULT1A1 allozyme 2, pH 7.0, 37°C
pH 6.5, 37°C, allozyme SULT1A1*2
pH 6.5, 37°C, allozyme SULT1A1*3


substrate_name: serotonin

proof_lines: dopamine 3-O-sulfate formation, recombinant SULT1A3

substrate: serotonin


proof_lines: mutant enzyme Q56E/L67V/A101S/T117S/H213R/F222L/V243I/D249G, in 50 mM HEPES, pH 7.5, 7 mM MgCl2, and 1.5 mM dithiothreitol, at 22°C


proof_lines: mutant enzyme D249G, in 50 mM HEPES, pH 7.5, 7 mM MgCl2, and 1.5 mM dithiothreitol, at 22°C


proof_lines: mutant enzyme Q56E/A101S/T117S/Q177K/M223I/V243L, in 50 mM HEPES, pH 7.5, 7 mM MgCl2, and 1.5 mM dithiothreitol, at 22°C


substrate_name: rotigotine

substrate: rotigotine


proof_lines: heterodimer of mutants K266E and E275K, pH 7.4, 37°C


proof_lines: wild-type, initial rate value, pH 7.5, 25°C

proof_lines: wild type enzyme, in 50 mM HEPES, pH 7.5, 7 mM MgCl2, and 1.5 mM dithiothreitol, at 22°C


substrate_name: tapentadol

substrate: tapentadol


substrate_name: O-desmethyl tramadol

substrate: O-desmethyl tramadol


substrate_name: acetaminophen

substrate: acetaminophen


proof_lines: recombinant wild-type M-PST, pH 7.0, 37°C

proof_lines: recombinant wild-type P-PST, pH 7.0, 37°C


organism: Mus musculus

substrate_name: xanthurenic acid

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM Tris/HCl

proof_lines: isoform SULT1B1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C

substrate: xanthurenic acid


organism: Oryctolagus cuniculus


organism: Rattus norvegicus


organism: Squalius cephalus

substrate_name: genistein

substrate: genistein


proof_lines: with dopamine, isoenzyme A, pH 6.0, 37°C

proof_lines: with dopamine, isoenzyme B, pH 9.5, 37°C


substrate_name: daidzein

proof_lines: enzyme form SULT1A3, 4-sulfate formation

proof_lines: enzyme form SULT1A1, 7-sulfate formation

proof_lines: enzyme form SULT1E1, 7-sulfate formation

substrate: daidzein


proof_lines:
isoenzyme I
isoenzyme II
ST1A1


proof_lines: substrate inhibition, wild-type enzyme, enzyme form SULT1D1


proof_lines: substrate inhibition, mutant enzyme D247L, enzyme form SULT1D1


enzyme_display_name: chitinase

organism: Bacillus licheniformis

proof_lines:
wild-type, strain DSM13, pH 3.0, 37°C
wild-type, strain DSM8785, pH 3.0, 37°C
wild-type, strain DSM13, pH 6.0, 37°C

enzyme: chitinase


organism: Bacillus thuringiensis

substrate_name: colloidal chitin

proof_lines: mature enzyme lacking its signal peptide sequence, at pH 7.0 and 40°C

substrate: colloidal chitin


organism: Candida albicans


organism: Chromobacterium sp.


organism: Clostridium paraputrificum


organism: Corallococcus sp. EGB


proof_lines: truncated protein lacking the CBD domain, pH 6, 50°C


proof_lines: truncated protein lacking both the CBD and FN3-2 domains, pH 6, 50°C


proof_lines: truncated protein lacking the FN3-2 domain, pH 6, 50°C


organism: Dioscorea polystachya

substrate_name: glycol chitin

substrate: glycol chitin


organism: Drosera rotundifolia

substrate_name: FITC-chitin

proof_lines: pH 5.2, recombinant protein lacking the 5 signal peptide, temperature not specified in the publication

proof_lines: recombinant protein lacking the thioredoxin tag, pH 5.2, temperature not specified in the publication

proof_lines: recombinant protein lacking the 5 signal peptide, pH 5.2, temperature not specified in the publication

substrate: FITC-chitin


organism: Ephemerocybe congregata


organism: Euphorbia characias

substrate_name: 4-nitrophenyl N-acetyl-D-glucosaminide

substrate: 4-nitrophenyl N-acetyl-D-glucosaminide


proof_lines:
wild-type, pH 2.2, 37°C
wild-type, pH 7.0, 37°C
wild-type, pH 4.6, 37°C


organism: Listeria innocua


organism: Macaca fascicularis

substrate_name: 4-methylumbelliferyl chitobioside

substrate: 4-methylumbelliferyl chitobioside


organism: Moritella marina

assay_conditions_summary: pH 5

proof_lines: pH 5.0, 0°C, purified recombinant enzyme

proof_lines: pH 5.0, 5°C, purified recombinant enzyme

proof_lines: pH 5.0, 15°C, purified recombinant enzyme


organism: Ostrinia furnacalis

proof_lines:
domain ChtII-C1, at pH 6.0 and 30°C
domain ChtII-C2, at pH 6.0 and 30°C
domain ChtII-C1C2, at pH 6.0 and 30°C


proof_lines: 30°C, pH not specified in the publication


organism: Paenibacillus barengoltzii


organism: Paenibacillus sp.

substrate_name: 4-nitrophenyl N,N'-diacetylchitobiose

substrate: 4-nitrophenyl N,N'-diacetylchitobiose


organism: Paenibacillus xylanexedens


organism: Penaeus vannamei

proof_lines:
pH 5.5, 25°C, presence of 0.6 M NaCl
pH 6.0, 25°C


organism: Pochonia chlamydosporia


organism: Pyrococcus furiosus


organism: Rhizomucor miehei


proof_lines:
mutant ChiADC-C, pH 4.5, 50Â°C
mutant ChiAD2L, pH 4.5, 50Â°C


organism: Saccharomyces cerevisiae


organism: Serratia marcescens

substrate_name: Unknown

substrate: Unknown


proof_lines:
pH 6.5, isozyme ChiC
pH 6.5, isozyme ChiB
pH 6.5, isozyme ChiA


substrate_name: beta-chitin

proof_lines: presence of lytic polysaccharide monooxygenase Cbp21, pH 8.0, 37°C

substrate: beta-chitin


proof_lines: presence of lytic polysaccharide monooxygenase Cbp21, pH 6.1, 37°C


organism: Streptomyces sp. DA11

substrate_name: powdered chitin

substrate: powdered chitin


organism: Trichoderma harzianum

proof_lines: pH 6.5, wild-type enzyme from Trichoderma harzianum

proof_lines: pH 6.5, wilde-type recombinant enzyme expressed in Escherichia coli


organism: Trichoderma virens


enzyme_display_name: orotidine-5'-phosphate decarboxylase

organism: Homo sapiens

substrate_name: orotidine 5'-phosphate

enzyme: orotidine-5'-phosphate decarboxylase

substrate: orotidine 5'-phosphate


organism: Methanobacterium thermoautotrophicus


organism: Methanothermobacter thermautotrophicus


organism: Plasmodium falciparum

proof_lines: monofunctional enzyme expressed in Escherichia coli

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

proof_lines: multienzyme complex of orotate phosphoribosyltransferase and orotidine 5-monophosphate decarboxylase


proof_lines:
pH 7.2, 25°C, D37A mutant
mutant D37A, pH 7.1, 25°C
pH 7.4, 25°C, D37A mutant


substrate_name: orotidine 5'-monophosphate

proof_lines:
wild type enzyme
pH 7.2, 25°C, wild-type enzyme
wild-type, pH 7.1, 25°C

substrate: orotidine 5'-monophosphate


proof_lines:
Q215A mutant
pH 7.1, 25°C, mutant Q215A
mutant Q215A, pH 7.1, 25°C


proof_lines:
pH 7.1, 25°C, mutant Y217F
mutant Y217F, pH 7.1, 25°C


substrate_name: 5-Fluoroorotidine 5'-phosphate

substrate: 5-Fluoroorotidine 5'-phosphate


proof_lines:
pH 7.1, 25°C, mutant R235A
mutant R235A, pH 7.1, 25°C


proof_lines:
mutant T100A, pH 7.1, 25°C
pH 7.2, 25°C, T100A mutant
pH 7.4, 25°C, T100A mutant


organism: Bombyx mori

proof_lines:
isoenzyme 1
isoenzyme 2


organism: Hexagrammos otakii

substrate_name: glycolchitin

proof_lines:
isoenzyme HoChiA
isoenzyme HoChiB
isoenzyme HoChiC

substrate: glycolchitin


organism: Scomber japonicus


organism: Unknown


organism: Danio rerio

substrate_name: L-thyroxine

substrate: L-thyroxine


enzyme_display_name: firefly luciferase

organism: Amydetes vivianii

substrate_name: D-firefly luciferin

assay_conditions_summary: pH 8; 295.15 K; cofactor ATP

enzyme: firefly luciferase

substrate: D-firefly luciferin


substrate_name: ATP

substrate: ATP


organism: Lamprigera yunnana

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Lampyris turkestanicus

substrate_name: D-luciferin

assay_conditions_summary: cofactor ATP

substrate: D-luciferin


assay_conditions_summary: pH 7.8; buffer 50 mM Tricine-NaOH; cofactor ATP

proof_lines: at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4

proof_lines: in 50 mM Tricine-NaOH buffer with 10 mM MgSO4, at pH 7.8


proof_lines:
mutant E354K/ins356K
mutant E354K


proof_lines:
mutant E354R
mutant E354R/ins356K


proof_lines: pH and temperature not specified in the publication, mutant enzyme L300E


proof_lines: pH and temperature not specified in the publication, mutant enzyme L300K


proof_lines: pH and temperature not specified in the publication, mutant enzyme L300R


organism: Luciola parvula

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Nipponoluciola cruciata

substrate_name: lauric acid

substrate: lauric acid


organism: Photinus pyralis

substrate_name: D-luciferyl-O-adenosine monophosphate

substrate: D-luciferyl-O-adenosine monophosphate


proof_lines:
pH 7.5, 25°C
native luciferase
recombinant luciferase


assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: mutant enzyme I432L, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2


assay_conditions_summary: pH 7.8; 298.15 K; buffer 25 mM glycylglycine; cofactor ATP

proof_lines: recombinant mutant enzyme V241I/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme V241I/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme G246A, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme V241I/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme G246A/F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme V241I, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme V241I/G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme V241I/G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme G246A/F250S, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme G246A/F250T, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: recombinant mutant enzyme F250G, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C


proof_lines: mutant enzyme D436G, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2

proof_lines: mutant enzyme D436G, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2


proof_lines: mutant enzyme I423L/D436G/L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2


proof_lines: mutant enzyme I423L, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2


proof_lines: mutant enzyme L530R, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2

proof_lines: mutant enzyme L530R, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2


assay_conditions_summary: pH 7.4; 298.15 K; buffer 25 mM glycylglycine; cofactor ATP

proof_lines: wild type enzyme, in 50 mM Tris/HCl, at pH 7.4 and in the presence of 10 mM MgCl2

proof_lines: recombinant wild type enzyme, in 25 mM glycylglycine buffer, at pH 7.8, in the presence of 2 mM Mg2+, at 25°C

proof_lines: wild type enzyme, in 50 mM Tris-HCl, pH 7.4, and 10 mM MgCl2


substrate_name: Luciferin

assay_conditions_summary: pH 7.8; buffer 0.02 M Tris-acetate; cofactor ATP

proof_lines: free enzyme, in 0.02 M Tris-acetate buffer, pH 7.8, containing 12 mM magnesium acetate, 0.2 mM EDTA, and 0.3 mM dithiothreitol

proof_lines: at pH 7.8, in 50 mM Tricine-NaOH buffer with 10 mM MgSO4

substrate: Luciferin


proof_lines:
mutant ins356R
mutant ins356Q
mutant ins356K


assay_conditions_summary: pH 7.8; 295.15 K; cofactor ATP

proof_lines: pH 7.8, 22°C, recombinant mutant R213K/T214N


assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: pH 7.8, temperature not specified in the publication, mutant enzyme H461D


proof_lines: pH 7.8, temperature not specified in the publication, mutant enzyme H489D


proof_lines: pH 7.8, temperature not specified in the publication, mutant enzyme H489M


proof_lines: pH 7.8, temperature not specified in the publication, mutant enzyme H489K


proof_lines: pH 7.8, 25°C, mutant enzyme I423L/D436G/L530R


proof_lines: 25°C, pH 7.8, mutant enzyme T214A/A215L/I232A/F295L/E345K

proof_lines: pH 7.8, 25°C, mutant enzyme T214A/A215L/I232A/F295L/E345K


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


organism: Photinus scintillans


proof_lines: pH 7.8, 22°C, recombinant wild-type enzyme


organism: Pyrocoelia sp. RF-2016

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: alcohol dehydrogenase (NADP+)

organism: Escherichia coli

substrate_name: NADP+; 1-Propanol

assay_conditions_summary: cofactor NADP+

enzyme: alcohol dehydrogenase (NADP+)

substrate: NADP+; 1-Propanol


organism: Homo sapiens

substrate_name: H+; NADPH; 4-Nitrobenzaldehyde

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; 4-Nitrobenzaldehyde


substrate_name: H+; Succinate semialdehyde; NADPH

substrate: H+; Succinate semialdehyde; NADPH


organism: Lactobacillus brevis

substrate_name: 2-Butanone; NADPH; H+

substrate: 2-Butanone; NADPH; H+


organism: Mus musculus

substrate_name: NADPH; Benzaldehyde

substrate: NADPH; Benzaldehyde


organism: Mycobacterium bovis

substrate_name: H+; NADPH; Benzaldehyde

substrate: H+; NADPH; Benzaldehyde


organism: Mycobacterium smegmatis

substrate_name: H+; NADPH; Octanal

substrate: H+; NADPH; Octanal


organism: Rana perezi

substrate_name: NADPH; all-trans-Retinal; H+

substrate: NADPH; all-trans-Retinal; H+


organism: Rattus norvegicus


substrate_name: Methylglyoxal; NADPH; H+

substrate: Methylglyoxal; NADPH; H+


organism: Saccharomyces cerevisiae

substrate_name: H+; NADPH; Cinnamaldehyde

substrate: H+; NADPH; Cinnamaldehyde


organism: Sus scrofa

substrate_name: 4-Cyanobenzaldehyde; NADPH; H+

substrate: 4-Cyanobenzaldehyde; NADPH; H+


enzyme_display_name: cysteine synthase

organism: Bacillus anthracis

substrate_name: O-acetyl-L-serine

enzyme: cysteine synthase

substrate: O-acetyl-L-serine


proof_lines: production of H2S, mutant A72S, pH 8.2, 37°C


proof_lines: production of H2S, wild-type, pH 8.2, 37°C

proof_lines: wild-type, production of H2S, pH 8.2, 37°C


organism: Geobacillus stearothermophilus

substrate_name: L-cysteine

substrate: L-cysteine


organism: Glycine max

substrate_name: Sulfide

substrate: Sulfide


enzyme_display_name: 4-hydroxyphenylpyruvate dioxygenase

organism: Arabidopsis thaliana

proof_lines:
wild-type, pH 7,20°C
wild-type, pH 7, 25°C

enzyme: 4-hydroxyphenylpyruvate dioxygenase


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

proof_lines: 30°C, pH not specified in the publication


organism: Coptis japonica var. dissecta


proof_lines: pH 6.5, 37°C, mutant DELTAG388 and DELTAL385


proof_lines: pH 6.5, 37°C, wild-type enzyme and mutant DELTAG388


proof_lines: mutant lacking 12 N-terminal residues, pH 6.5, 37°C

proof_lines: mutant lacking 17 N-terminal residues, pH 6.5, 37°C


substrate_name: Unknown

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

substrate: Unknown


organism: Picrophilus oshimae


organism: Sphingobium sp.


organism: Haemophilus influenzae

proof_lines: 100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration

proof_lines: 100 mM HEPES, pH 8.0, 1 microM enzyme, 20°C, steady state fluorescence titration


proof_lines: wild type serine acetyltransferase motif, 100 mM HEPES, pH 7.0, 1 microM enzyme, 20°C, steady state fluorescence titration


organism: Lacticaseibacillus casei

substrate_name: O-acetyl-L-Ser

substrate: O-acetyl-L-Ser


organism: Leishmania donovani


organism: Leucaena leucocephala

substrate_name: hydrogen sulfide

proof_lines: pH 7.5, 22°C, recombinant enzymem, Michaelis-Menten model

proof_lines: pH 7.5, 22°C, recombinant enzyme, Lineweaver-Burke model

substrate: hydrogen sulfide


organism: Microcystis aeruginosa

proof_lines: recombinant enzyme, pH 7.0, 25°C, with DTT

proof_lines: recombinant enzyme, pH 7.0, 25°C, with glutathione, GSSG


organism: Mimosa pudica


organism: Oryza sativa Japonica Group


organism: Streptomyces lavendulae

proof_lines: 30°C, pH 8.0, cosubstrate: hydrogen sulfide


enzyme_display_name: non-specific serine/threonine protein kinase

substrate_name: ATP; L-Threonyl-AtSERK1

substrate: ATP; L-Threonyl-AtSERK1


substrate_name: Histone; ATP

enzyme: non-specific serine/threonine protein kinase

substrate: Histone; ATP


substrate_name: ATP; CRCK1

substrate: ATP; CRCK1


substrate_name: Protein; ATP

substrate: Protein; ATP


enzyme_display_name: corrinoid adenosyltransferase

organism: Homo sapiens

substrate_name: ATP

proof_lines: mutant S68F, in presence of 0.05 mM cob(I)alamin

enzyme: corrinoid adenosyltransferase

substrate: ATP


proof_lines: mutant C119Y, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant G97E, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant D218N, in presence of 0.05 mM cob(I)alamin


proof_lines:
native wild-type
N-terminally octa-His tagged wild-type
C-terminally octa-His tagged wild-type


proof_lines: mutant S126L, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant H183Y, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant D64G, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant R76G, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant F83S, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant G63E, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant K78R, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant T161I, in presence of 0.05 mM cob(I)alamin


proof_lines: mutant G97R, in presence of 0.05 mM cob(I)alamin


organism: Listeria monocytogenes

proof_lines: mutant enzyme K98Q, pH and temperature not specified in the publication


substrate_name: cob(II)alamin

proof_lines: mutant enzyme D110N, pH and temperature not specified in the publication

substrate: cob(II)alamin


proof_lines: mutant enzyme T88V, pH and temperature not specified in the publication


proof_lines: mutant enzyme R200K, pH and temperature not specified in the publication


proof_lines: mutant enzyme E207Q, pH and temperature not specified in the publication


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


organism: Salmonella enterica

substrate_name: cob(II)inamide

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

substrate: cob(II)inamide


organism: Thermoplasma acidophilum

substrate_name: hydroxocobalamin

assay_conditions_summary: pH 8; 343.15 K; cofactor ATP

proof_lines: pH 8.0, 70°C, mutant R124A, in presence of Mg2+

substrate: hydroxocobalamin


substrate_name: Ser/Thr peptide; ATP

substrate: Ser/Thr peptide; ATP


substrate_name: Peptide; ATP

substrate: Peptide; ATP


organism: Bacillus subtilis

substrate_name: ATP; SpoIIAA

substrate: ATP; SpoIIAA


organism: Caenorhabditis elegans

substrate_name: ATP; Peptide

substrate: ATP; Peptide


substrate_name: ATP; Kemptide

substrate: ATP; Kemptide


substrate_name: ATP; p65

substrate: ATP; p65


substrate_name: Myelin basic protein; ATP

substrate: Myelin basic protein; ATP


substrate_name: Myosin; ATP

substrate: Myosin; ATP


substrate_name: ATP; NFAT3

substrate: ATP; NFAT3


substrate_name: ATP; CASK CaM-kinase domain

substrate: ATP; CASK CaM-kinase domain


substrate_name: ATP; Sox-AKT-tide peptide

substrate: ATP; Sox-AKT-tide peptide


substrate_name: S6K1; Pi

substrate: S6K1; Pi


substrate_name: ATP; Protein

substrate: ATP; Protein


substrate_name: ATP; alpha-Casein

substrate: ATP; alpha-Casein


organism: Mus musculus


organism: Mycobacterium tuberculosis

substrate_name: EmbR; ATP

substrate: EmbR; ATP


substrate_name: ATP; GarA

substrate: ATP; GarA


organism: Oryza sativa

substrate_name: ATP; XA21K intracellular domain

substrate: ATP; XA21K intracellular domain


organism: Physarum polycephalum

substrate_name: ATP; Fragmin-actin complex

substrate: ATP; Fragmin-actin complex


organism: Rattus norvegicus

substrate_name: ATP; Protein tyrosine

substrate: ATP; Protein tyrosine


substrate_name: eIF-2alpha; ATP

substrate: eIF-2alpha; ATP


organism: Arabidopsis thaliana

substrate_name: diphosphate

substrate: diphosphate


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: dTTP

proof_lines:
pH 7.5, 25°C
cosubstrate: UTP, pH 7.5, 25°C
cosubstrate: dTTP, pH 7.5, 25°C

substrate: dTTP


substrate_name: UTP

proof_lines:
pH 7.5, 25°C
cosubstrate: UTP, pH 7.5, 25°C

substrate: UTP


organism: Cucumis melo

substrate_name: UDP-galactose

substrate: UDP-galactose


organism: Danio rerio


organism: Drosophila melanogaster


organism: Giardia duodenalis

proof_lines: cosubstrate alpha-D-galactose 1-phosphate, S0.5 value, hyperbolic behaviour, pH 8.0, 37°C

proof_lines: cosubstrate TTP, S0.5 value, hyperbolic behaviour, pH 8.0, 37°C


organism: Gracilaria chouae

proof_lines: pH 7.5, temperature not specified in the publication


organism: Homo sapiens

proof_lines: pH 7.5, 37°C, recombinant mutant S309N/S311R


proof_lines: pH 7.5, 37°C, recombinant mutant P414G/T415P


proof_lines: pH 7.5, 37°C, recombinant mutant T406K/M407L


proof_lines: pH 7.5, 37°C, recombinant mutant N491P/L492E


organism: Hordeum vulgare


proof_lines:
recombinant wild-type, pH 7.6, 25°C
wild-type protein


proof_lines:
Ccut-8 mutant protein
Ccut-32 mutant protein
Ncut-21 mutant protein


mutation_signature: Δ1

proof_lines:
Delta 1-8 mutant protein
Delta 1-4 mutant protein


organism: Leishmania major


organism: Nostoc sp.


organism: Saccharina japonica


organism: Saccharomyces cerevisiae


organism: Streptococcus equi


organism: Sulfurisphaera tokodaii


organism: Synechocystis sp.


organism: Thermocrispum agreste


organism: Trypanosoma brucei

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


organism: Xanthomonas campestris pv. campestris


organism: Xanthomonas citri

substrate_name: TTP

substrate: TTP


enzyme_display_name: subtilisin

organism: Bacillus licheniformis

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

proof_lines: recombinant wild-type enzyme, pH 7.5, 30°C

enzyme: subtilisin


enzyme_display_name: aralkylamine N-acetyltransferase

organism: Antheraea pernyi

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

enzyme: aralkylamine N-acetyltransferase

substrate: acetyl-CoA


organism: Bombyx mori

substrate_name: tryptamine

assay_conditions_summary: cofactor CoA

substrate: tryptamine


organism: Bos taurus


organism: Chlamydomonas reinhardtii

substrate_name: serotonin

substrate: serotonin


organism: Danio rerio


organism: Drosophila melanogaster

assay_conditions_summary: pH 8; cofactor CoA

proof_lines: pH 8.0, temperature not specified in the publication


organism: Homo sapiens


organism: Mycobacterium tuberculosis

substrate_name: histamine

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

proof_lines:
cosubstrate acetyl-CoA, pH 7.0, 25°C
cosubstrate histamine, pH 7.0, 25°C

substrate: histamine


organism: Mycolicibacterium smegmatis

substrate_name: propionyl-CoA

proof_lines:
cosubstrate tyramine, pH 7.0, 25°C
cosubstrate acetyl-CoA, pH 7.0, 25°C

substrate: propionyl-CoA


organism: Oryza sativa


organism: Ovis aries

proof_lines: pH 6.8, 37°C, recombinant mutant I57A/V59A


substrate_name: Unknown

substrate: Unknown


proof_lines: above, pH 6.8, 37°C, recombinant mutants P64A, P64G, P64W, and recombinant truncation mutants


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


organism: Rattus norvegicus

assay_conditions_summary: pH 6.8; 310.15 K; cofactor CoA


organism: Sparus aurata

assay_conditions_summary: pH 6.8; 300.15 K; cofactor CoA


organism: Sus scrofa


organism: Tribolium castaneum

substrate_name: decanoyl-CoA

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

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

substrate: decanoyl-CoA


proof_lines: pH 8.0, 25°C, recombinant mutant P210G/T211G/N212G


proof_lines: pH 8.0, 25°C, recombinant mutant P210G/T211G


proof_lines: recombinant mutant T58A/G165Y/L216W, pH 7.5, 30°C


proof_lines: recombinant mutant T58A/L216W, pH 7.5, 30°C


proof_lines: recombinant mutant T58A/G165L/L216W, pH 7.5, 30°C


proof_lines: recombinant mutant T58A/G165I/L216W, pH 7.5, 30°C


organism: Bacillus subtilis

proof_lines: pH 8.5, 37°C, recombinant mutant S62I/A153V/G166S/I205V, in presence of 2 M GdmCl

proof_lines: pH 8.5, 37°C, recombinant mutant S62I/A153V/G166S/I205V, in absence of GdmCl or SDS

proof_lines: pH 8.5, 37°C, recombinant mutant S62I/A153V/G166S/I205V, in presence of SDS


proof_lines: pH 8.5, 37°C, recombinant mutant S62I, in presence of SDS

proof_lines: pH 8.5, 37°C, recombinant mutant S62I, in absence of GdmCl or SDS


proof_lines: pH 8.5, 37°C, recombinant mutant S62I/G166M, in presence of SDS

proof_lines: pH 8.5, 37°C, recombinant mutant S62I/G166M, in presence of 2 M GdmCl

proof_lines: pH 8.5, 37°C, recombinant mutant S62I/G166M, in absence of GdmCl or SDS


proof_lines: pH 8.5, 37°C, recombinant mutant G166M, in presence of SDS

proof_lines: pH 8.5, 37°C, recombinant mutant G166M, in presence of 2 M GdmCl

proof_lines: pH 8.5, 37°C, recombinant mutant G166M, in absence of GdmCl or SDS


proof_lines: pH 8.5, 37°C, recombinant wild-type enzyme, in presence of 2 M GdmCl

proof_lines: pH 8.5, 37°C, recombinant wild-type enzyme, in absence of GdmCl or SDS

proof_lines: pH 8.5, 37°C, recombinant wild-type enzyme, in presence of SDS


proof_lines:
recombinant enzyme, 5°C, pH 8.6
recombinant enzyme, 45°C, pH 8.6
recombinant enzyme, 25°C, pH 8.6


substrate_name: casein

proof_lines: pH 10.0, 80°C, recombinant enzyme, calculated by BRENDA

substrate: casein


organism: Shewanella frigidimarina


organism: Shouchella clausii

proof_lines: synthetic peptide corresponding to the N-terminal extension behaves as a mixed noncompetitive inhibitor of active ISP, pH and temperature not specified in the publication


organism: Aspisoma lineatum

substrate_name: ATP

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, temperature not specified in the publication, isoenzyme AL1

proof_lines: pH 8.0, temperature not specified in the publication, isoenzyme AL2

substrate: ATP


organism: Unknown

substrate_name: D-luciferin

substrate: D-luciferin


substrate_name: cob(I)alamin

assay_conditions_summary: cofactor ATP

substrate: cob(I)alamin


organism: Allium tuberosum

substrate_name: O-acetyl-L-Ser

substrate: O-acetyl-L-Ser


organism: Allochromatium vinosum

substrate_name: O-acetyl-L-serine

proof_lines:
pH 7.4, 37°C, isoenzyme 2
pH 7.4, 37°C, isoenzyme 1
pH 7.4, 37°C, enzyme 1

substrate: O-acetyl-L-serine


organism: Arabidopsis sp.

proof_lines:
pH 7.5, 37°C, isoenzyme A
pH 7.5, 37°C, isoenzyme C
pH 7.5, 37°C, isoenzyme B


organism: Chlamydomonas reinhardtii

proof_lines:
pH 7.5, 50°C
pH 7.5, 50°C, isoenzyme 1 and 2
pH 7.5, 50 C


organism: Citrullus lanatus

proof_lines:
pH 8.0, 30°C, isoenzyme 1
pH 8.0, 30°C, isoenzyme 2


organism: Lathyrus oleraceus

proof_lines:
pH 7.8, 35°C, isoenzyme 2
pH 7.8, 35°C
pH 8.0, 30°C, isoenzyme 2


organism: Rhodocyclus tenuis

proof_lines:
isoenzyme 1
isoenzyme 1 and 2
isoenzyme 2


organism: Spinacia oleracea

proof_lines:
pH 7.5, 25°C, chloroplast enzyme
pH 8.0, 30°C
pH 8.0, 25°C, isoenzyme 3


organism: Synechococcus sp.


organism: Xanthium pennsylvanicum

proof_lines:
,isoenzyme 3
isoenzymes 1 and 2
,isoenzyme 2


organism: Sphingomonas elodea

proof_lines:
isoenzyme UgpG, 30°C, pH 7.8
isoenzyme RmlA, 30°C, pH 7.8


organism: Arabidopsis thaliana

substrate_name: Sulfide

substrate: Sulfide


organism: Photinus pyralis