substrate_name: NADH

proof_lines: pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose

proof_lines: pH 7.0, 25°C, cofactor: NADH, wild-type enzyme, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose

substrate: NADH


enzyme_display_name: D-xylose reductase (NADPH)

organism: Yamadazyma tenuis

substrate_name: Unknown

source_db: brenda

kcat_display: Not reported

km_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

ki_unit: mM

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

enzyme: D-xylose reductase (NADPH)

substrate: Unknown

source: brenda


substrate_name: D-xylose

ki_display: Not reported

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

mutation_type: substitution

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme W23F, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose

substrate: D-xylose


proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose


enzyme_display_name: ADP-specific phosphofructokinase

organism: Pyrococcus horikoshii

substrate_name: D-fructose 6-phosphate

km_unit: mM

assay_conditions_summary: 323.15 K; cofactor ADP

enzyme: ADP-specific phosphofructokinase

substrate: D-fructose 6-phosphate


assay_conditions_summary: pH 6.5; 313.15 K; cofactor ADP


substrate_name: D-Fructose 6-phosphate

source_db: oed

substrate: D-Fructose 6-phosphate

source: oed


organism: Thermococcus kodakarensis

substrate_name: D-glucose

sequence_source: UniProtKB accession Q5JD05 confirmed; full sequence not embedded in verdict.

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ADP

substrate: D-glucose


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


substrate_name: ADP

substrate: ADP


organism: Debaryomyces nepalensis

substrate_name: D-erythrose

proof_lines: recombinant His-tagged enzyme, pH 7.0, 45°C

substrate: D-erythrose


organism: Rhizomucor pusillus

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


organism: Saccharomyces cerevisiae

substrate_name: NADPH

assay_conditions_summary: pH 5; 303.15 K; cofactor NADPH

proof_lines: pH 5.0, 30°C, recombinant engineered Pir-XR enzyme

proof_lines: pH 5.0, 30°C, recombinant engineered XR-GPI enzyme

substrate: NADPH


organism: Scheffersomyces stipitis

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH


organism: Thermomyces lanuginosus


organism: Escherichia coli

proof_lines: recombinant enzyme mutant G73S, pH 4.5, 37°C


proof_lines: recombinant enzyme mutant G73D, pH 4.5, 37°C


proof_lines: recombinant enzyme mutant G73E, pH 4.5, 37°C


substrate_name: phytate

substrate: phytate


substrate_name: myo-inositol hexakisphosphate

substrate: myo-inositol hexakisphosphate


proof_lines: recombinant enzyme mutant G73T, pH 4.5, 37°C


proof_lines: pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-glucose

proof_lines: pH 7.5, 50°C, recombinant enzyme, in presence of Mg2+, substrates ADP and D-fructose 6-phosphate


substrate_name: AMP

substrate: AMP


organism: Thermococcus litoralis

assay_conditions_summary: cofactor ADP


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

proof_lines:
pH 2.5, 0.5 M NaCl
pH 2.5, no salt
pH 6.0, no salt

source_databases_merged: brenda skid


organism: Xylanibacter ruminicola


organism: Yersinia pestis


organism: Yersinia rohdei


enzyme_display_name: dipeptidyl-peptidase III

organism: Arabidopsis thaliana

enzyme: dipeptidyl-peptidase III


proof_lines: recombinant wild-type enzyme, pH 4.5, 37°C


organism: Penicillium oxalicum


organism: Shigella sp. CD2

proof_lines: pH 5.5, 37°C, recombinant glycosylated enzyme expressed from Pichia pastoris

proof_lines: pH 5.5, 37°C, recombinant nonglycosylated enzyme expressed from Escherichia coli


organism: Oryza sativa Japonica Group


organism: Pectobacterium wasabiae


organism: Homo sapiens


proof_lines:
wild-type, pH 8.0, 37°C
pH 8.6, 37°C, wild-type
wild-type enzyme


organism: Corallococcus sp. EGB


organism: Drosophila melanogaster

substrate_name: Tyr-Gly-Gly-Phe-Met

substrate: Tyr-Gly-Gly-Phe-Met


assay_conditions_summary: pH 8

proof_lines:
mutant Y318F
mutant Y318F at pH 8.0


organism: Bacteroides thetaiotaomicron


organism: Caldithrix abyssi


substrate_name: L-Leu-valorphin-L-Arg

proof_lines: pH and temperature not specified in the publication

substrate: L-Leu-valorphin-L-Arg


organism: Physcomitrium patens


organism: Porphyromonas gingivalis


substrate_name: Arg-Arg-4-methylcoumarin 7-amide

substrate: Arg-Arg-4-methylcoumarin 7-amide


organism: Saccharomyces cerevisiae


substrate_name: L-Arg-L-Arg 2-naphthylamide

substrate: L-Arg-L-Arg 2-naphthylamide


substrate_name: L-Ala-L-Ala 2-naphthylamide

proof_lines: mutant K638L, pH 8.0, 25°C, presence of CoCl2

proof_lines: mutant K638L, pH 8.0, 25°C, absence of CoCl2

substrate: L-Ala-L-Ala 2-naphthylamide


proof_lines: mutant H578N, pH 8.0, 25°C, presence of CoCl2


proof_lines: wild-type, pH 8.0, 25°C, presence of CoCl2

proof_lines: wild-type, pH 8.0, 25°C, absence of CoCl2


enzyme_display_name: leukocyte elastase

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

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: leukocyte elastase


enzyme_display_name: enteropeptidase

organism: Bos taurus

substrate_name: APFDDDDRIVGG

proof_lines:
at 0.014-0.05 mM, holoenzyme
at 0.08-2 mM, holoenzyme
at 0.03-0.08 mM, EP light chain

enzyme: enteropeptidase

substrate: APFDDDDRIVGG


proof_lines: value obtained by impedance spectroscopy, pH not specified in the publication, at 37°C

proof_lines: value obtained by fluorescence spectroscopy, pH not specified in the publication, at 37°C


substrate_name: Z-Lys-SBzl

substrate: Z-Lys-SBzl


proof_lines: wild type enzyme, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C


proof_lines: mutant enzyme Y174R, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C


proof_lines: mutant enzyme R96Q, in 100 mM Tris, 0.02 mM CaCl2, 0.01% (v/v) Triton X-100, 10% (v/v) DMSO, pH 8.0, at 22°C


proof_lines: mutant R582Q, pH 8.0, 25°C, absence of CoCl2

proof_lines: mutant R582Q, pH 8.0, 25°C, presence of CoCl2


organism: Oryzias latipes


proof_lines:
wild type enzyme, at pH 8.3 and 30°C
wild-type enzyme, 37°C, pH 7.4


organism: Sus scrofa


enzyme_display_name: cathepsin D

substrate_name: DNA

enzyme: cathepsin D

substrate: DNA


enzyme_display_name: xylose isomerase

organism: Actinoplanes missouriensis

substrate_name: L-Arabinose

enzyme: xylose isomerase

substrate: L-Arabinose


substrate_name: D-Glucose

substrate: D-Glucose


proof_lines: mutant enzyme E136Y/R213L, at pH 8.3 and 30°C


enzyme_display_name: macrophage elastase

enzyme: macrophage elastase


organism: Bacillus coagulans

substrate_name: alpha-D-Xylose

substrate: alpha-D-Xylose


substrate_name: D-Fructose

substrate: D-Fructose


substrate_name: D-Xylose

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

substrate: D-Xylose


organism: Arthrobacter sp.

substrate_name: D-Ribose

substrate: D-Ribose


substrate_name: D-Lyxose

substrate: D-Lyxose


substrate_name: alpha-D-Fructofuranose

substrate: alpha-D-Fructofuranose


substrate_name: D-glucose; L-ribose

substrate: D-glucose; L-ribose


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


proof_lines: recombinant catalytic domain of MMP-12, pH 7.5, 30°C


organism: Mus musculus

proof_lines: below, full-length enzyme MMP-12, pH 7.5, 30°C


enzyme_display_name: respiratory dimethylsulfoxide reductase

organism: Cereibacter sphaeroides

substrate_name: Dimethylsulfoxide

assay_conditions_summary: pH 6

proof_lines: W-DMSOR, pH 6.0, temperature not specified in the publication

enzyme: respiratory dimethylsulfoxide reductase

substrate: Dimethylsulfoxide


organism: Rhodobacter capsulatus

substrate_name: dimethyl sulfoxide

proof_lines: enzyme Mo-DMSOR with molybdenum in the catalytic centre, pH not specified in the publication, temperature not specified in the publication

proof_lines: enzyme W-DMSOR with tungsten in the catalytic centre, pH not specified in the publication, temperature not specified in the publication

substrate: dimethyl sulfoxide


substrate_name: D-Xylose; L-Arabinose; D-Ribose; D-Lyxose


organism: Lactococcus lactis subsp. lactis

sequence_source: UniProtKB Q9CFG7 direct accession lookup confirmed a reviewed xylose isomerase entry with a sequence present; full sequence not emitted in this exact-accession worker verdict.


substrate_name: D-Xylulose

substrate: D-Xylulose


substrate_name: alpha-D-Glucose

substrate: alpha-D-Glucose


organism: Streptomyces pseudogriseolus

substrate_name: D-xylose

proof_lines: in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C

substrate: D-xylose


organism: Streptomyces rubiginosus


substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


organism: Streptomyces violaceoruber


organism: Escherichia coli

substrate_name: D-glucose

proof_lines: pH 7.0, 50°C, with 0.5 mM Mn2+ and 10 mM Mg2+

substrate: D-glucose


organism: Lactobacillus brevis


organism: Piromyces sp. E2

substrate_name: alpha-D-xylopyranose

substrate: alpha-D-xylopyranose


substrate_name: D-Glucose


organism: Thermoanaerobacter ethanolicus

assay_conditions_summary: pH 7; 353.15 K; buffer 100 mM MOPS


organism: Thermoanaerobacterium sp.


enzyme_display_name: protein xylosyltransferase

organism: Homo sapiens

substrate_name: bikunin

enzyme: protein xylosyltransferase

substrate: bikunin


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: Xylosyltransferase 1

enzyme: Xylosyltransferase 1


enzyme_display_name: biotinidase

substrate_name: H2O; Biotinyl-6-aminoquinoline

enzyme: biotinidase

substrate: H2O; Biotinyl-6-aminoquinoline


organism: Rattus norvegicus


substrate_name: alpha-D-Xylose

substrate: alpha-D-Xylose


enzyme_display_name: glucan 1,4-alpha-maltohydrolase

organism: Geobacillus stearothermophilus

substrate_name: maltotriose

enzyme: glucan 1,4-alpha-maltohydrolase

substrate: maltotriose


substrate_name: starch

proof_lines: cross-linked enzyme aggregates, pH 5.5, 65°C

substrate: starch


organism: Geobacillus thermoleovorans

substrate_name: amylopectin

proof_lines:
mutant enzyme D109A, at pH 7.0 and 80°C
mutant enzyme D109A at pH 7.0 and 80°C

substrate: amylopectin


substrate_name: alpha-cyclodextrin

proof_lines: monomeric enzyme form, at pH 7.0 and 80°C

substrate: alpha-cyclodextrin


organism: Pyrococcus sp.

substrate_name: maltopentaose

substrate: maltopentaose


organism: Shouchella lehensis

substrate_name: beta-cyclodextrin

proof_lines: porous cross-linked enzyme aggregates, pH 7, 40°C

proof_lines: free enzyme, 40°C, pH not specified in the publication

substrate: beta-cyclodextrin


organism: Staphylothermus marinus


organism: Thermococcus sp.


substrate_name: maltotetraose

substrate: maltotetraose


organism: Canis lupus familiaris


proof_lines:
mutant enzyme D109E, at pH 7.0 and 80°C
mutant enzyme D109E at pH 7.0 and 80°C


organism: Geobacillus sp.

assay_conditions_summary: pH 6; 333.15 K; buffer sodium-acetate

proof_lines: in sodium-acetate buffer (50 mM, pH 6.0), at 60°C


organism: Thermus thermophilus

substrate_name: L-Arabinose

substrate: L-Arabinose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: D-Mannose

substrate: D-Mannose


enzyme_display_name: diisopropyl-fluorophosphatase

organism: Sphingobium fuliginis

substrate_name: diisopropyl fluorophosphate

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM ethylamine

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethanolamine

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme, with 300 mM triethylamine

enzyme: diisopropyl-fluorophosphatase

substrate: diisopropyl fluorophosphate


proof_lines: pH 8.0, 25°C, recombinant mutant F132Y, with 300 mM triethanolamine


organism: Thermotoga petrophila


substrate_name: D-Xylose

substrate: D-Xylose


substrate_name: Succinyl-YVAD-p-nitroanilide; H2O

substrate: Succinyl-YVAD-p-nitroanilide; H2O


enzyme_display_name: ADAM 17 endopeptidase

enzyme: ADAM 17 endopeptidase


substrate_name: (EDANS)-EPLAQAVRSSSK-(DABCYL)

proof_lines: extracellular domain, presence of L-galactose, 25°C, pH not specified in the publication

proof_lines: extracellular domain, 25°C, pH not specified in the publication

proof_lines: catalytic domain, 25°C, pH not specified in the publication

substrate: (EDANS)-EPLAQAVRSSSK-(DABCYL)


organism: Alteromonas sp. JD6.5

substrate_name: VR

substrate: VR


substrate_name: D-Glucose

substrate: D-Glucose


organism: Loligo vulgaris


substrate_name: paraoxon

assay_conditions_summary: pH 7

substrate: paraoxon


proof_lines: pH 8.0, 25°C, recombinant mutant F132Y/L140Y, with 300 mM triethanolamine


proof_lines: pH 8.0, 25°C, recombinant mutant L140Y, with 300 mM triethanolamine


proof_lines: pH 10.5, 25°C, recombinant PON1-hFc fusion enzyme


proof_lines: pH 10.5, 25°C, recombinant PON1 wild-type enzyme


proof_lines: wild-type, pH 7.5, 25°C, in nitrogen atmosphere

proof_lines: wild-type, presence of 1 mM O,O-dicyclopentylphosphoroamidate, pH 7.5, 25°C, in nitrogen atmosphere


sequence_source: UniProtKB P26997 direct lookup: live reviewed entry XYLA_THET8, xylose isomerase, EC 5.3.1.5, Thermus thermophilus HB8, gene xylA; sequence exists but was not emitted in this lane.


sequence_source: UniProtKB P26997 direct lookup: live reviewed entry XYLA_THET8, xylose isomerase, EC 5.3.1.5, Thermus thermophilus HB8, gene xylA; source token '(P26997)*4' was treated as a bundled P26997 hint, not as an accepted top-level accession.


organism: Vibrio sp.

substrate_name: D-xylose

assay_conditions_summary: pH 7.5; 313.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer (pH 7.5), at 40°C

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: recombinant bikunin

source_db: uniprot

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

substrate: recombinant bikunin

source: uniprot


organism: Alteromonas sp

substrate_name: diisopropylfluorophosphate

substrate: diisopropylfluorophosphate


substrate_name: diisopropyl-fluorophosphate (in the presence of 10 mM NaCl)


enzyme_display_name: trypanothione-disulfide reductase

organism: Unknown

substrate_name: trypanothione disulfide

enzyme: trypanothione-disulfide reductase

substrate: trypanothione disulfide


organism: Homo sapiens

proof_lines:
XylT-I or XylT-II
37°C, pH 6.5
recombinant enzyme


substrate_name: bikunin

proof_lines: isoenzyme XT-I with mutant bikunin (sequence QEEEGSGHNMLV)

proof_lines: isoenzyme XT-II with mutant bikunin (sequence QEEEGSGGRSVLV)

proof_lines: isoenzyme XT-I with mutant bikunin (sequence QKEEGSGGGQLV)

substrate: bikunin


proof_lines: isoenzyme XT-I with wild-type bikunin (sequence QEEEGSGGGQLV)

proof_lines: isoenzyme XT-II with wild-type bikunin (sequence QEEEGSGGGQLV)


enzyme_display_name: aspartate kinase

organism: Spinacia oleracea

substrate_name: L-aspartate

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, isoenzyme I and II
pH 7.5, isoenzyme II
pH 7.5, isoenzyme I

enzyme: aspartate kinase

substrate: L-aspartate


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Brassica napus

substrate_name: myo-inositol hexakisphosphate

proof_lines:
isoenzyme I
isoenzyme II

substrate: myo-inositol hexakisphosphate


organism: Zea mays

substrate_name: myo-inositol pentakisphosphate

proof_lines:
isoenzyme with isoelectric point of 4.9
isoenzyme with isoelectric point of 4.8
isoenzyme with isoelectric point of 5.0

substrate: myo-inositol pentakisphosphate


substrate_name: beta-cyclodextrin

substrate: beta-cyclodextrin


substrate_name: Trypsinogen

substrate: Trypsinogen


substrate_name: p-(N-biotinylamino)benzoic acid

substrate: p-(N-biotinylamino)benzoic acid


substrate_name: diisopropyl fluorophosphate

substrate: diisopropyl fluorophosphate


substrate_name: D-Xylose

substrate: D-Xylose


enzyme_display_name: thiol oxidase

substrate_name: 5,5'-dithiobis(2-nitrobenzoic acid)

assay_conditions_summary: pH 7.4; 310.15 K; cofactor FAD

enzyme: thiol oxidase

substrate: 5,5'-dithiobis(2-nitrobenzoic acid)


proof_lines: pH 7.4, 37°C, salt bridge mutant R127A/E183A


proof_lines: pH 7.4, 37°C, dimer interface mutant E174A


proof_lines: pH 7.4, 37°C, salt bridge mutant R127E/E183R


organism: Aspergillus oryzae

substrate_name: glutathione

substrate: glutathione


substrate_name: dithiothreitol

substrate: dithiothreitol


substrate_name: L-Cys

substrate: L-Cys


substrate_name: D-Cys

substrate: D-Cys


organism: Rattus norvegicus


smiles: OCCS


proof_lines: pH 7.4, 37°C, dimer interface mutant H227A


proof_lines: pH 7.4, 37°C, dimer interface mutant E174K


proof_lines: pH 7.4, 37°C, dimer interface mutant E174A/H227A


enzyme_display_name: (R)-citramalate synthase

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

substrate_name: pyruvate

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 2.41 sec(-1) (PubMed:15292141). kcat is 10.3 sec(-1) with acetyl-CoA as substrate (PubMed:18498255). kcat is 9.13 sec(-1) with pyruvate as substrate (PubMed:18498255).

enzyme: (R)-citramalate synthase

substrate: pyruvate


enzyme_display_name: dipeptidyl-peptidase III

organism: Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 / VPI-5482 / E50)

proof_lines: kcat is 5.0 sec(-1) with Arg-Arg-2NA as substrate (PubMed:22628297). kcat is 0.384 sec(-1) with Arg-Arg-2NA as substrate (PubMed:29095893). kcat is 0.537 sec(-1) with Ala-Arg-2NA as substrate (PubMed:29095893). kcat is 0.178 sec(-1) with Ph

enzyme: dipeptidyl-peptidase III


organism: Caldithrix abyssi (strain DSM 13497 / VKM B-2286 / LF13)

substrate_name: Arg-Arg-2NA (at 50 degrees Celsius)

proof_lines: kcat is 3.07 sec(-1) with Arg-Arg-2NA as substrate (at 50 degrees Celsius) (PubMed:29420664). kcat is 2.53 sec(-1) with Gly-Arg-2NA as substrate (at 50 degrees Celsius) (PubMed:29420664). kcat is 0.20 sec(-1) with Arg-Arg-2NA as substrate (

substrate: Arg-Arg-2NA (at 50 degrees Celsius)


organism: Thermus thermophilus

substrate_name: D-Mannose

substrate: D-Mannose


substrate_name: D-xylose

substrate: D-xylose


organism: Trypanosoma brucei

substrate_name: rRNaseA

substrate: rRNaseA


substrate_name: L-Arabinose

substrate: L-Arabinose


substrate_name: D-Lyxose

substrate: D-Lyxose


organism: Aspergillus niger

substrate_name: RNAse A

proof_lines:
thiol per second
pH 5.5, 25°C

substrate: RNAse A


organism: Aspergillus tubingensis


organism: Bos taurus

substrate_name: 2-nitro-5-thiobenzoic acid

proof_lines: corresponds to a sulfhydryl concentration of 0.14 mM

substrate: 2-nitro-5-thiobenzoic acid


organism: Gallus gallus

substrate_name: DTT

substrate: DTT


organism: Glycine max


proof_lines: pH 7.5, 25°C, recombinant mutant C15A/C74A/C85A/C124A


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


proof_lines: pH 7.5, 25°C, recombinant mutants C74A/C85A and C15A/C124A


proof_lines: pH 7.5, 25°C, recombinant mutant C74A/C85A


proof_lines: pH 7.5, 25°C, recombinant mutant C15A/C124A


proof_lines:
mutant CIPHCII, pH 7.0, 25°C
mutant CIGPCII, pH 7.0, 25°C


organism: Cereibacter sphaeroides

substrate_name: Dimethylsulfoxide

proof_lines: mutant Y114A, pH 8.0, temperature not specified in the publication

substrate: Dimethylsulfoxide


proof_lines: mutant Y114F, pH 8.0, temperature not specified in the publication


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


organism: Escherichia coli

verification_status: unverified

proof_lines: pH 6.0, 25°C, recombinant NapA mutant C176D

status: unverified


substrate_name: reduced benzyl viologen

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

substrate: reduced benzyl viologen


proof_lines: mutant M147I, pH not specified in the publication, temperature not specified in the publication


substrate_name: Pyridine N-oxide

proof_lines: mutant M147L, pH not specified in the publication, temperature not specified in the publication

substrate: Pyridine N-oxide


proof_lines: mutant G167N, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant Q179I, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant R217Q, pH not specified in the publication, temperature not specified in the publication


substrate_name: GSH

substrate: GSH


organism: Saccharomyces cerevisiae

proof_lines: in the presence of 12.5 mM dithiothreitol

proof_lines: with 0.3 mM reduced thioredoxin as the substrate of the reductive half-reaction and an initial oxygen concentration of around 0.3 mM such that the reduced thioredoxin would be depleted by 10% during the course of the reaction


proof_lines: 25°C, recombinant mutant C30S/C33S, in presence of 10 mM DTT


proof_lines: 25°C, recombinant wild-type enzyme, in presence of 3.5 mM tris(2-carboxyethyl)phosphine

proof_lines: 25°C, recombinant wild-type enzyme, in presence of 10 mM DTT


proof_lines: 25°C, recombinant mutant C159S/C176S, in presence of 10 mM DTT

proof_lines: 25°C, recombinant mutant C159S/C176S, in presence of 10 3.5 mM tris(2-carboxyethyl)phosphine


substrate_name: glutathione

substrate: glutathione


organism: Lunaria biennis

substrate_name: Unknown

substrate: Unknown


organism: Plasmodium falciparum


organism: Trypanosoma brucei rhodesiense


organism: Trypanosoma congolense

substrate_name: trypanothione disulfide

proof_lines:
mutant E201D
mutant E201D, slopes
mutant E201D, intercepts

substrate: trypanothione disulfide


substrate_name: 3-acetylpyridine adenine dinucleotide

assay_conditions_summary: cofactor NADPH

substrate: 3-acetylpyridine adenine dinucleotide


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.5; 295.15 K; buffer system; cofactor NADPH

proof_lines:
recombinant enzyme
dependent on assay conditions
dependent on buffer system


substrate_name: NADPH

sequence_source: UniProtKB:P28593 FASTA fetched during PMID-linked review

substrate: NADPH


assay_conditions_summary: cofactor NADP+


enzyme_display_name: D-xylose reductase (NADPH)

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: 30°C, cosubstrate: D-xylose or L-arabinose

enzyme: D-xylose reductase (NADPH)


organism: Candida tropicalis

proof_lines:
pH 7.0, D-xylose reductase 2
pH 7.0, D-xylose reductase 3
pH 7.0, D-xylose reductase 1


organism: Neurospora crassa


assay_conditions_summary: pH 7; 295.15 K; cofactor NADPH


organism: Saitozyma flava


organism: Sungouiella intermedia

proof_lines: pH 7.0, 25Â°C, NADPH-dependent monospecific xylose reductase, cofactor: NADPH

proof_lines: pH 7.0, 25Â°C, monospecific xylose reductase (msXR)


organism: Crithidia fasciculata


organism: Homo sapiens

proof_lines: recombinant glutathione-trypanothione reductase-like enzyme


organism: Leishmania infantum


enzyme_display_name: mannan endo-1,4-beta-mannosidase

organism: Alicyclobacillus sp. A4

substrate_name: Mannotriose

enzyme: mannan endo-1,4-beta-mannosidase

substrate: Mannotriose


substrate_name: Mannotetraose

substrate: Mannotetraose


organism: Aspergillus nidulans

sequence_source: UniProtKB REST scalar check on 2026-07-05 found active reviewed entries Q5AZ53 and Q5B7X2 with sequence objects; sequence text was not emitted in this exact-accession worker output.


organism: Aspergillus niger

substrate_name: locust bean gum galactomannan

sequence_source: UniProtKB REST scalar check on 2026-07-05 found active unreviewed entry B6V876 with a sequence object; sequence text was not emitted in this exact-accession worker output.

substrate: locust bean gum galactomannan


organism: Bacillus licheniformis

substrate_name: glucomannan

substrate: glucomannan


organism: Bacillus sp. KW1

substrate_name: carob galactomannan

substrate: carob galactomannan


organism: Bacillus subtilis

substrate_name: H2O; Galactomannan

unit: g/(l*min)

substrate: H2O; Galactomannan


organism: Hordeum vulgare


organism: Klebsiella oxytoca

substrate_name: Mannopentaose

substrate: Mannopentaose


organism: Mytilus edulis


organism: Trichoderma reesei

substrate_name: 4-methylumbelliferyl mannotrioside

substrate: 4-methylumbelliferyl mannotrioside


substrate_name: mannohexaose

substrate: mannohexaose


substrate_name: locust bean gum

substrate: locust bean gum


sequence_source: UniProtKB reviewed accession Q99036 direct REST check; canonical sequence exists but was not emitted or reused as a row-specific R171K variant sequence.


enzyme_display_name: u-plasminogen activator

substrate_name: Plasminogen; H2O

sequence_source: UniProtKB reviewed accession P00749 direct REST check; canonical sequence exists but was not emitted into this exact-accession verdict.

proof_lines: pH and temperature not specified in the publication

enzyme: u-plasminogen activator

substrate: Plasminogen; H2O


organism: Aspergillus fumigatus

proof_lines:
isozyme MAN I
isozyme MAN II


organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293)

substrate_name: locust bean galactomannan

substrate: locust bean galactomannan


organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

substrate_name: locust bean gum mannan

substrate: locust bean gum mannan


substrate_name: mannotetraose

substrate: mannotetraose


organism: Podospora anserina (strain S / ATCC MYA-4624 / DSM 980 / FGSC 10383)

substrate_name: konjac glucomannan

substrate: konjac glucomannan


organism: Trichoderma reesei (strain ATCC 56765 / BCRC 32924 / NRRL 11460 / VTT-D-86271 / Rut C-30)


organism: Leptospira interrogans

substrate_name: pyruvate

proof_lines: mutant T179A, kinetic data for the catalytic reaction of the active site of LiCMS

substrate: pyruvate


substrate_name: acetyl-CoA

proof_lines: mutant D304A, kinetic data for the C-terminal region of LiCMS

substrate: acetyl-CoA


assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: LiCMSN, kinetic data for the catalytic reaction of the active site of LiCMS


proof_lines: mutant E146D, kinetic data for the catalytic reaction of the active site of LiCMS


proof_lines: mutant N310A, kinetic data for the C-terminal region of LiCMS


proof_lines: mutant L81V, kinetic data for the substrate-binding site of LiCMS


assay_conditions_summary: pH 7.7; cofactor CoA

proof_lines: mutant Q495A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant Q495A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant Q495A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: mutant L451V, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant L451V 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant L451V, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: mutant H400A/H408A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant H400A/H408A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant H400A/H408A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: mutant P493A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant P493A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation


proof_lines: mutant V468A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant V468A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant V468A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: mutant Y454A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant Y454A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant Y454A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


organism: Bacillus subtilis (strain 168)

proof_lines: kcat is 330 min(-1) for mannanase activity with galactomannan as substrate. kcat is 350 min(-1) for mannanase activity with glucomannan as substrate.


organism: Cellvibrio japonicus (strain Ueda107)

proof_lines: kcat is 140000 min(-1) for mannanase activity with galactomannan as substrate. kcat is 62000 min(-1) for mannanase activity with glucomannan as substrate.


proof_lines: kcat is 14.7 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMed:8973192). kcat is 20 sec(-1) for mannanase activity with 2,4-dinitrophenyl-beta-mannobioside (2,4-DNPM) as substrate (PubMe


organism: Cryptopygus antarcticus

proof_lines: kcat is 1659.90 sec(-1) for 0.5% locust bean gum (at pH 3.5 and 10 degrees Celsius in the presence of 50mM sodium citrate).


organism: Salipaludibacillus agaradhaerens

substrate_name: galactomannan

proof_lines: kcat is 38000 min(-1) for mannanase activity with galactomannan as substrate. kcat is 45000 min(-1) for mannanase activity with glucomannan as substrate.

substrate: galactomannan


organism: Rhodobacter capsulatus

substrate_name: Dimethylsulfoxide

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

substrate: Dimethylsulfoxide


proof_lines: mutant L311A, kinetic data for the C-terminal region of LiCMS


proof_lines: mutant Y144V, kinetic data for the substrate-binding site of LiCMS


proof_lines: mutant D17N, kinetic data for the catalytic reaction of the active site of LiCMS


proof_lines: mutant D17A, kinetic data for the catalytic reaction of the active site of LiCMS


proof_lines: mutant L104V, kinetic data for the substrate-binding site of LiCMS


proof_lines:
LiCMSN mutant
L104 mutant


substrate_name: glyoxylate

proof_lines: mutant L81A, kinetic data for the substrate-binding site of LiCMS

substrate: glyoxylate


proof_lines: mutant F83A, kinetic data for the catalytic reaction of the active site of LiCMS


proof_lines: mutant E146Q, kinetic data for the catalytic reaction of the active site of LiCMS


proof_lines: mutant Y144L, kinetic data for the substrate-binding site of LiCMS


organism: Homo sapiens

substrate_name: bikunin

mutation_signature: Δ1

mutation_type: deletion

proof_lines:
37°C, pH 6.5, mutant enzyme DELTA1-184
37°C, pH 6.5, mutant enzyme DELTA1-266
37°C, pH 6.5, mutant enzyme DELTA1-272

substrate: bikunin


organism: Mus musculus

substrate_name: QEEEGSGGGQKK

proof_lines:
in Xylt2
in Xylt1

substrate: QEEEGSGGGQKK


organism: Rattus norvegicus

substrate_name: CDEASGIGPEVPDDRD

proof_lines: cosubstrate: Smith-degraded chondroitin sulfate

substrate: CDEASGIGPEVPDDRD


enzyme_display_name: ADP-specific phosphofructokinase

organism: Archaeoglobus fulgidus

substrate_name: ADP

assay_conditions_summary: pH 6.6; 323.15 K; cofactor ADP

proof_lines: 50°C, pH not specified in the publication

enzyme: ADP-specific phosphofructokinase

substrate: ADP


organism: Pyrococcus horikoshii

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: 323.15 K; cofactor ADP

proof_lines:
D433A mutant
D433A mutant, at 50°C

substrate: D-fructose 6-phosphate


proof_lines:
R191E mutant
R191E mutant, at 50°C


organism: Escherichia coli

substrate_name: reduced benzyl viologen

proof_lines: mutant R149C, pH not specified in the publication, temperature not specified in the publication

substrate: reduced benzyl viologen


substrate_name: Pyridine N-oxide

proof_lines: mutant G190D, pH not specified in the publication, temperature not specified in the publication

substrate: Pyridine N-oxide


proof_lines: mutant T148S, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant W191G, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant W357F, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant W357Y, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant A178Q, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant G190V, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant A181T, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant W357C, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant W116F, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant I458A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant I458A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: mutant D431A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant D431A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant D431A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: mutant Y430L, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant Y430L, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant Y430L, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


proof_lines: wild-type, 1 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: wild-type, 60 microM isoleucine, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: wild-type, 4 microM isoleucine, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7


proof_lines: mutant T464A, 0.6 mM pyruvate, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, 0.1 M HEPES, pH 7.7

proof_lines: mutant T464A, 0.6 mM pyruvate, 4 mM acetyl CoA, 0.8 mM MnCl2, 50 mM KCl, 15 nM enzyme, variable inhibitor concentrations, 0.1 M HEPES, pH 7.7, calculated from the Cheng-Prusoff equation

proof_lines: mutant T464A, 0.8 mM MnCl2, 50 mM KCl, 15 nM CMS, in a total volume of 50 microL using 0.1 M Hepes, pH 7.7


organism: Malus domestica

proof_lines: cosubstrate: 2-oxobutanoate, pH and temperature not specified in the publication

proof_lines: cosubstrate: pyruvate, pH and temperature not specified in the publication


organism: Methanocaldococcus jannaschii


proof_lines:
wild-type
wild type enzyme


organism: Rhodospirillum rubrum


organism: Drosophila sp. (in: flies)

substrate_name: UDP-D-xylose

substrate: UDP-D-xylose


organism: Gallus gallus

substrate_name: Ser-Gly-Gly

proof_lines: Smith-degraded proteoglycan, value on serine basis

substrate: Ser-Gly-Gly


substrate_name: ADP / D-fructose 6-phosphate

proof_lines:
S263A mutant
S263A mutant, at 50°C

substrate: ADP / D-fructose 6-phosphate


proof_lines:
S189A mutant
S189A mutant, at 50°C


proof_lines:
N160A mutant
N160A mutant, at 50°C


proof_lines:
N15A mutant
N15A mutant, at 50°C


proof_lines:
R191A mutant
R191A mutant, at 50°C


proof_lines:
A71E mutant
A71E mutant, at 50°C


proof_lines:
Q97A mutant
Q97A mutant, at 50°C


proof_lines:
K158A mutant
K158A mutant, at 50°C


proof_lines:
D17A mutant
D17A mutant, at 50°C


proof_lines:
Q224A mutant
Q224A mutant, at 50°C


proof_lines:
S183E mutant
S183E mutant, at 50°C


organism: Saccharomyces cerevisiae

substrate_name: ATP

substrate: ATP


substrate_name: L-aspartate

substrate: L-aspartate


proof_lines: wild type, in the presence of 10 mM aspartate


proof_lines: mutant E279A, with aspartate as substrate


proof_lines: glutathione-S-transferase fusion protein, in the presence of 10 mM ATP

proof_lines: glutathione-S-transferase fusion protein, in the presence of 10 mM aspartate and 10 mM ATP


proof_lines: threonine insensitive mutant, in the presence of 10 mM ATP


organism: Thermus thermophilus

sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature G73A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature F136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature P183A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature A42S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature D154N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature D182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature D154A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature D154N/D182A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature G149A/G177A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature A23L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature R150A/D154A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P61489 with row-specific substitution reconstruction and applied mutation signature G149A to reconstruct the assayed variant sequence.


proof_lines: pH 7.5, 60°C, wild-type and mutant G152A


organism: Streptococcus mutans

substrate_name: L-Aspartate; ATP

assay_conditions_summary: pH 8.1; 302.15 K; cofactor ATP

proof_lines: pH 8.1, 29°C, noncompetitive inhibition with respect to aspartate, mixed with respect to ATP

substrate: L-Aspartate; ATP


organism: Streptomyces murayamaensis

assay_conditions_summary: pH 8


organism: Streptomyces noursei


organism: Stutzerimonas stutzeri

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


organism: Thermotoga maritima

assay_conditions_summary: pH 7; cofactor ATP


substrate_name: Unknown

substrate: Unknown


organism: Corynebacterium pekinense

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: mutant enzyme M372I/T379W, at pH 7.4 and 28Â°C


proof_lines: mutant enzyme T379L, at pH 8.0 and 26Â°C


organism: Daucus carota

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


proof_lines: recombinant wild-type bifunctional holoenzyme, asparate kinase activity

proof_lines: recombinant wild-type bifunctional holoenzyme, inhibition of asparate kinase activity


substrate_name: ATP; L-Aspartate

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity

substrate: ATP; L-Aspartate


organism: Geobacillus stearothermophilus

proof_lines:
pH 8.0, 55°C
pH 8.0, 55°C, in presence of inhibitor


organism: Paenibacillus polymyxa

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


organism: Pseudomonas putida

assay_conditions_summary: cofactor ATP


organism: Rhodocyclus tenuis


organism: Triticum aestivum

assay_conditions_summary: pH 7.8; 300.15 K; cofactor ATP


organism: Xenorhabdus bovienii


organism: Zea mays


organism: Acinetobacter sp. AC1-2

substrate_name: myo-inositol hexakisphosphate

substrate: myo-inositol hexakisphosphate


organism: Pyrococcus horikoshii

proof_lines:
R185A mutant
R185A mutant, at 50°C


assay_conditions_summary: pH 6.5; 323.15 K; cofactor ADP

proof_lines:
presence of Mn2+, pH 6.5, 50°C
presence of Mg2+, pH 6.5, 50°C
presence of Co2+, pH 6.5, 50°C


organism: uncultured bacterium

assay_conditions_summary: pH 6.5; 313.15 K; cofactor ADP


assay_conditions_summary: pH 6.5; 333.15 K; cofactor ADP

proof_lines:
pH 6.5, 60°C
MgADP, pH 6.5, 60°C


organism: Amycolatopsis mediterranei


organism: Arabidopsis thaliana

proof_lines:
20 mM ATP, presence of alanine
50 mM aspartate, presence of alanine
pH 8.0, 30°C


organism: Bacillus subtilis

substrate_name: aspartate

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines:
pH 7.0, 30°C
pH 7.0, 25°C
aspartokinase I

substrate: aspartate


proof_lines: mutant enzyme A380I, at pH 8.0 and 28Â°C


proof_lines:
wild type enzyme, at pH 8.0 and 26Â°C
wild type enzyme, at pH 8.0 and 28Â°C
wild type enzyme, at pH 7.5 and 25Â°C


proof_lines: mutant enzyme Y198N/D201M, at pH 7.5 and 25Â°C


organism: Typha latifolia


proof_lines: recombinant wild-type enzyme, pH 2.5, 40°C


organism: Vicia faba


organism: Vigna radiata var. radiata


organism: Wickerhamomyces anomalus


organism: Bacillus thermoalkalophilus

substrate_name: beta-cyclodextrin

substrate: beta-cyclodextrin


organism: Lactiplantibacillus plantarum

assay_conditions_summary: pH 6


organism: Thermofilum pendens

substrate_name: amylopectin

substrate: amylopectin


organism: Thermoplasma volcanium

substrate_name: maltoheptaose

proof_lines: kinetic parameters for C14-labelled maltooligosaccharides

proof_lines: estimated for monomeric conformation, in presence of 1 M NaCl

proof_lines: estimated for the high oligomer conformation

substrate: maltoheptaose


organism: Cavia porcellus


organism: Citrobacter braakii


organism: Corylus avellana

assay_conditions_summary: pH 5.6; cofactor ATP


organism: Cucurbita maxima

proof_lines:
phytase IC
phytase IB
phytase ID


organism: Enterobacter sp. ACSS


organism: Escherichia coli

substrate_name: p-nitrophenyl phosphate

assay_conditions_summary: pH 4.5; 310.15 K; buffer 0.1 M sodium acetate

proof_lines: in 0.1 M sodium acetate buffer, pH 4.5, at 37°C

proof_lines: 37°C, pH 3.5, enzyme expressed in Pichia pastoris (pGAPZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphos

proof_lines: 37°C, pH 5.5, enzyme expressed in Pichia pastoris (pGAPZalphaA) or Pichia pastoris (pPICZalphaA). The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. my

substrate: p-nitrophenyl phosphate


organism: Glycine max


organism: Hordeum vulgare


organism: Klebsiella aerogenes


organism: Lilium longiflorum


organism: Loigolactobacillus coryniformis


organism: Lupinus albus

substrate_name: GTP

assay_conditions_summary: pH 5; 308.15 K; cofactor ADP

proof_lines:
pH 5.0, 35°C, phytase LP2
pH 5.0, 35°C, phytase LP12
pH 5.0, 35°C, phytase LP11

substrate: GTP


organism: Papiliotrema laurentii


organism: Peniophora lycii


organism: Phaseolus vulgaris


organism: Pseudomonas sp.


organism: Pseudomonas syringae


organism: Rattus norvegicus


organism: Rhizopus microsporus var. oligosporus


organism: Rhodotorula mucilaginosa


organism: Scheffersomyces spartinae


organism: Schwanniomyces occidentalis


organism: Secale cereale

assay_conditions_summary: pH 6; 310.15 K; buffer 0.1 M sodium acetate

proof_lines: in 0.1 M sodium acetate buffer, pH 6.0, at 37°C


organism: Thermothelomyces heterothallicus


organism: Bacillus amyloliquefaciens

substrate_name: phytate

substrate: phytate


proof_lines: free, not complexed with Ca2+, competitive inhibitor

proof_lines: free, not complexed with phytate, competitive inhibitor


organism: Bacillus sp. (in: firmicutes)

assay_conditions_summary: pH 7


organism: Bacillus subtilis


organism: Blastobotrys adeninivorans


organism: Brassica rapa subsp. oleifera

proof_lines:
phytase 1
phytase 2


organism: Brassica sp.


organism: Aspergillus ficuum

proof_lines:
pH 5.0, 58°C
pH 5.0, 58°C, native enzyme
pH 5.0, 58°C, recombinant enzyme


organism: Aspergillus fumigatus


organism: Aspergillus niger

assay_conditions_summary: pH 3.5; 310.15 K; buffer 0.2 M glycine-HCl

proof_lines: wild type enzyme, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C

proof_lines: wild type enzyme, in 0.2 M glycine-HCl, at pH 2.5

proof_lines: wild type enzyme, in 0.2 M glycine-HCl, at pH 3.2


assay_conditions_summary: pH 3.5; 310.15 K; buffer conditions

proof_lines: mutant enzyme E228K, in 0.2 M glycine-HCl buffer at pH 3.5 and 37°C

proof_lines: mutant enzyme E228K, in 0.2 M citrate buffer at pH 5.5 and 37°C


proof_lines: mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 2.5

proof_lines: mutant enzyme E272Q, in 0.2 M glycine-HCl, at pH 3.2


proof_lines: mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 3.2

proof_lines: mutant enzyme E272K, in 0.2 M glycine-HCl, at pH 2.5


proof_lines: pH 2.5, 55°C. The enzyme may be a 3-phytase, EC 3.1.3.8, or a 6-phytase, EC 3.1.3.26. The product of the hydrolysis of myo-inositol hexakisphosphate i.e. myo-inositol 1,2,3,4,5-pentakisphosphate or myo-inositol 1,3,4,5,6-pentakisphosphate h


organism: Avena sativa

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Homo sapiens


proof_lines:
pH 7.4, 37°C, pro-uPA
pH 8.8, nonphosphorylated uPA
pH 7.5, nonphosphorylated uPA


enzyme_display_name: leukocyte elastase

proof_lines: mutant enzyme F192A, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C

enzyme: leukocyte elastase


proof_lines: mutant enzyme A213V, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: wild type enzyme, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: mutant enzyme F215A, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


assay_conditions_summary: pH 9; 310.15 K; buffer 50 mM sodium phosphate


organism: Mus musculus


organism: Oryctolagus cuniculus


organism: Ovis aries


organism: Rattus norvegicus

proof_lines:
pH 8.0, 37°C
pH 7.8
2 disaccharide units, pH 8.0, 37°C


proof_lines:
pH 7.4, 37°C, enzyme mutant H99Y
pH 7.4, 37°C, mutant H99Y


proof_lines: pH 7.4, 25°C, mutant K300H, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K300H, single-chain activator


proof_lines: pH 7.4, 25°C, mutant K313A, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K313A, single-chain activator


proof_lines: pH 7.4, 25°C, mutant K300A, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K300A, single-chain activator


proof_lines: pH 7.4, 25°C, wild-type, single-chain activator

proof_lines: pH 7.4, 25°C, wild-type and mutant S303E, two-chain activator

proof_lines: pH 7.4, 25°C, wild-type, two-chain activator


proof_lines: pH 7.4, 25°C, mutant K300A and K313A, single-chain activator


proof_lines: pH 7.4, 25°C, mutant E301H, single-chain activator

proof_lines: pH 7.4, 25°C, mutant E301H, two-chain activator


proof_lines: pH 7.4, 25°C, mutant K300W, two-chain activator

proof_lines: pH 7.4, 25°C, mutant K300W, single-chain activator


proof_lines: pH 7.4, 25°C, mutant E301D, single-chain activator

proof_lines: pH 7.4, 25°C, mutant E301D, two-chain activator


proof_lines: pH 7.4, 25°C, mutant Y306G, two-chain activator

proof_lines: pH 7.4, 25°C, mutant Y306G, single-chain activator


proof_lines: pH 7.4, 25°C, mutant S303E, single-chain activator


proof_lines: pH 7.4, 25°C, mutant E301A, two-chain activator

proof_lines: pH 7.4, 25°C, mutant E301A, single-chain activator


organism: Thermus sp.

substrate_name: acarbose

substrate: acarbose


proof_lines: pH 6.0, 60°C, hydrolysis, truncated mutant ThMA-DELTA124

proof_lines: pH 6.0, 60°C, hydrolysis, truncated mutant ThMA- DELTA124, 1 M KCl


substrate_name: starch

substrate: starch


proof_lines: pH 6.0, 60°C, hydrolysis, variants DM and 4B74


substrate_name: maltohexaose

proof_lines: pH 6.0, 60°C, hydrolysis, wild-type, 1 M KCl

substrate: maltohexaose


substrate_name: maltotriose

substrate: maltotriose


organism: Aspergillus oryzae

substrate_name: konjac flour

substrate: konjac flour


organism: Bifidobacterium animalis subsp. lactis

substrate_name: Mannopentaose

substrate: Mannopentaose


organism: Cellulomonas fimi


organism: Cellvibrio japonicus

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label D283A and applied mutation signature D283A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P49424 canonical wild-type sequence, cross-checked against RCSB 1J9Y and PMID 11382747 Man26A identity


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label H211N and applied mutation signature H211N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label H143A and applied mutation signature H143A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label Y285A and applied mutation signature Y285A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label W217A and applied mutation signature W217A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label E212A and applied mutation signature E212A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label W156A and applied mutation signature W156A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label D283H and applied mutation signature D283H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label W162A and applied mutation signature W162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P49424 canonical sequence and the selected PMID 11382747 mutation label H211A and applied mutation signature H211A to reconstruct the assayed variant sequence.


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

proof_lines:
endomorphin-1
with Co2+
pH 7.4, 37°C


organism: Pediococcus acidilactici

substrate_name: Arg-Arg-beta-naphthylamide

substrate: Arg-Arg-beta-naphthylamide


organism: Platyrrhini

substrate_name: Unknown

substrate: Unknown


proof_lines: wild-type in presence of Cu2+, pH 7.4, 25°C


substrate_name: Gly-Gly-Phe-Leu

substrate: Gly-Gly-Phe-Leu


organism: Cricetulus griseus


organism: Equus caballus

substrate_name: N-succinyl-Ala-Ala-Ala 4-nitroanilide

proof_lines:
pH 7.5, 25°C, proteinase 2B
pH 7.5, 25°C, proteinase 2A
pH 7.5, 25°C, proteinase B

substrate: N-succinyl-Ala-Ala-Ala 4-nitroanilide


organism: Gallus gallus


proof_lines: mutant enzyme N98T, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: mutant enzyme F215Y, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


proof_lines: mutant enzyme F192K, in 500 mM NaCl and 200 mM Tris-HCl, pH 8, at 37°C


organism: Glycine max

substrate_name: locust bean gum

substrate: locust bean gum


organism: Hypothenemus hampei

substrate_name: guar gum

sequence_source: NCBI Protein ADF22325.1

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

substrate: guar gum


organism: Medicago sativa

substrate_name: soluble mannan

substrate: soluble mannan


proof_lines: pH and temperature not specified in the publication


organism: Rhizomucor miehei

sequence_source: NCBI Protein AGC24277.1


organism: Shouchella clausii

substrate_name: konjac glucomannan

substrate: konjac glucomannan


organism: Solanum lycopersicum

sequence_source: UniProt Q8L5J1


organism: Streptomyces sp. NRRL B-24484

substrate_name: galactomannan

substrate: galactomannan


organism: Blaberus craniifer

substrate_name: Proctolin

substrate: Proctolin


organism: Capra hircus

proof_lines: in 50 mM Tris-HCl, pH 8.5, with 100 mM NaCl and 1 mM beta-mercaptoethanol, at 37°C


organism: Cavia porcellus

substrate_name: Arg-Arg-4-methylcoumarin 7-amide

substrate: Arg-Arg-4-methylcoumarin 7-amide


organism: Drosophila melanogaster

substrate_name: Arg-Tyr-Leu-Pro-Thr

sequence_source: UniProt Q9VHR8

substrate: Arg-Tyr-Leu-Pro-Thr


organism: Homo sapiens


proof_lines:
wild-type, pH 7.2, 37°C
wild-type, pH 4.75, 37°C


proof_lines:
mutant D179A, pH 4.75, 37°C
mutant D179A, pH 7.2, 37°C


proof_lines:
mutant DELTA176-181, pH 4.75, 37°C
mutant DELTA176-181, pH 7.2, 37°C


proof_lines: pH 7.4, 25°C, mutant K300A and S303E, two-chain activator


organism: Mus musculus

substrate_name: L-pyroGlu-Gly-L-Arg-p-NA

substrate: L-pyroGlu-Gly-L-Arg-p-NA


organism: Rattus norvegicus


enzyme_display_name: enteropeptidase

organism: Bos taurus

substrate_name: thiobenzyl benzyloxycarbonyl-L-lysinate

enzyme: enteropeptidase

substrate: thiobenzyl benzyloxycarbonyl-L-lysinate


assay_conditions_summary: pH 8; 310.15 K; buffer pH 8

proof_lines: 37 °C, 100 mM Tris-HCl (pH 8.0), 1 mM CaCl2, 120 nM soybean trypsin inhibitor, 0.45 nM enteropeptidase


assay_conditions_summary: pH 8; 310.15 K; buffer conditions

proof_lines: 25°C, 28 mM sodium succinate (pH 5.6), 10 mM CaCl2

proof_lines: 0.00036 1/sec/mg, incubates 30 min at 37°C, pH 9.0, spectrophotometrically measured at 415 nm


substrate_name: Caspase-9; Caspase-3 cleaved

substrate: Caspase-9; Caspase-3 cleaved


enzyme_display_name: macrophage elastase

enzyme: macrophage elastase


organism: Sus scrofa


substrate_name: p-(N-biotinylamino)benzoic acid

proof_lines:
76000 Da biotinidase
human serum
human plasma

substrate: p-(N-biotinylamino)benzoic acid


organism: Lacticaseibacillus casei

proof_lines: pH 7.0, 37°C, enzyme from membrane fraction

proof_lines: pH 7.0, 37°C, enzyme from supernatant fraction


organism: Lactobacillus casei

substrate_name: H2O; Biotinyl-6-aminoquinoline

substrate: H2O; Biotinyl-6-aminoquinoline


proof_lines: pH 7.0, 37°C, enzyme from membrane and supernatant fraction


substrate_name: tosyl-Arg methyl ester

substrate: tosyl-Arg methyl ester


organism: Canis lupus familiaris

substrate_name: LSDGIDE

proof_lines: pH 7.2, 37°C, recombinant enzyme, calculated by BRENDA

substrate: LSDGIDE


proof_lines:
pH 7.5
pH 7.0
pH 7.0, absence of EDTA


enzyme_display_name: cathepsin D

organism: Gallus gallus

substrate_name: Unknown

enzyme: cathepsin D

substrate: Unknown


proof_lines:
pH 4.0, 37°C
37°C, pH 4.0
human fibroblast


organism: Lamellidens corrianus

substrate_name: hemoglobin

substrate: hemoglobin


organism: Oryctolagus cuniculus

proof_lines: enzyme from animals with experimental neurofibrillary changes


proof_lines:
40°C, pH 4.0, spleen cathepsin D
enzyme from AH-130 hepatoma cells
40°C, pH 4.0, gastric cathepsin D


organism: Struthio camelus

assay_conditions_summary: pH 3.5; 318.15 K; buffer 0.05 M sodium acetate

proof_lines: in 0.05 M sodium acetate buffer, pH 3.5, at 45°C


substrate_name: EEISEVNLDAEFRG

substrate: EEISEVNLDAEFRG


organism: Todarodes pacificus


substrate_name: DQ-collagen IV

substrate: DQ-collagen IV


sequence_source: UniProt P39900 catalytic-domain context; not accepted as resolved sequence because the row remains manually blocked.

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


enzyme_display_name: cellodextrin phosphorylase

organism: Thermosipho africanus

substrate_name: cellotetraose

enzyme: cellodextrin phosphorylase

substrate: cellotetraose


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


substrate_name: alpha-D-glucose 1-phosphate

substrate: alpha-D-glucose 1-phosphate


substrate_name: cellotriose

substrate: cellotriose


organism: Ruminiclostridium cellulolyticum


substrate_name: cellopentaose

substrate: cellopentaose


organism: Acetivibrio thermocellus

substrate_name: phenyl beta-D-glucopyranoside

substrate: phenyl beta-D-glucopyranoside


proof_lines:
apparent value, at pH 7.5 and 21°C
Raw SKiD Env: Temp=21°C, pH=7.5


substrate_name: cellobiose

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

substrate: cellobiose


organism: Thermoclostridium stercorarium

substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


substrate_name: octyl beta-D-glucoside

substrate: octyl beta-D-glucoside


sequence_source: UniProtKB:B7IED6 direct lookup; sequence exists but was not emitted in this exact-accession review lane

proof_lines:
phosphoroyltic reaction, pH 7.5, 60°C
synthetic reaction, pH 7.5, 60°C


substrate_name: alpha-D-xylose

substrate: alpha-D-xylose


enzyme_display_name: plasmepsin I

organism: Plasmodium falciparum

sequence_source: UniProtKB:P39898 direct lookup; canonical sequence exists but variant/truncated K110pN row sequence was not reconstructed

proof_lines: pH 4.5, 37°C, recombinant truncated proPfPM1 K110pN mutant

enzyme: plasmepsin I


organism: Unknown


enzyme_display_name: semenogelase

organism: Homo sapiens

enzyme: semenogelase


substrate_name: glucose-6-phosphate (at pH 6.5)

data_origin: experimental

substrate: glucose-6-phosphate (at pH 6.5)


organism: Mus musculus

substrate_name: D-glucose 6-phosphate

proof_lines: wild-type, mixed lauryl maltose neopentyl glycol and -palmitoyl-2-oleoyl-glycero-3-phosphocholine detergent micelles, pH 6.5, 30Â°C

proof_lines: wild-type, lauryl maltose neopentyl glycol detergent micelles, pH 6.5, 30Â°C

proof_lines: wild-type, mixed lauryl maltose neopentyl glycol and cholesteryl hemisuccinate detergent micelles, pH 6.5, 30Â°C

substrate: D-glucose 6-phosphate


proof_lines: mutant N96A, lauryl maltose neopentyl glycol detergent micelles, pH 6.5, 30Â°C


organism: Rattus norvegicus

substrate_name: H2O; D-Glucose 6-phosphate

substrate: H2O; D-Glucose 6-phosphate


organism: Cavia porcellus


proof_lines:
pH 5.5, in disrupted vesicles
pH 6.5, in disrupted vesicles
pH 6.5, in not disrupted vesicles


substrate_name: D-Glucose 6-phosphate; H2O

substrate: D-Glucose 6-phosphate; H2O


proof_lines: 8 times less active compared to G6PC1 under the same experimental conditions.


enzyme_display_name: sedolisin

organism: Pseudomonas sp. (strain 101)

proof_lines: kcat is 59.3 sec(-1) with Lys-Pro-Ala-Leu-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:10488127). kcat is 14.5 sec(-1) with Lys-Pro-Ala-Lys-Phe-(4-nitro)Phe-Arg-Leu as substrate (PubMed:1562589). kcat is 5.5 sec(-1) with Lys-Pro-Al

enzyme: sedolisin


organism: Escherichia coli (strain K12)

substrate_name: KDPG

proof_lines: kcat is 83 sec(-1) with KDPG as substrate (PubMed:17962400). kcat is 80 sec(-1) with KDPG as substrate (PubMed:17981470). kcat is 11 sec(-1) with KHPB as substrate (PubMed:17962400). kcat is 0.0063 sec(-1) with KDPGal as substrate (PubMed:1

substrate: KDPG


organism: Pseudomonas sp.


substrate_name: Unknown

substrate: Unknown


organism: Escherichia coli

substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: celloheptaose

proof_lines: degradation direction, cellulose binding module fusion protein (binding module derived from Clostridium thermocellum CbhA (UniProt: A3DCH2)), pH 7.2, 30°C

proof_lines: degradation direction, cellulose binding module fusion protein (binding module derived from Cellvibrio mixtus Cel5B (UniProt: O07653)), pH 7.2, 30°C

proof_lines: synthesis direction, cellulose binding module fusion protein (binding module derived from Clostridium thermocellum CbhA (UniProt: A3DCH2)), pH 7.2, 30°C

substrate: celloheptaose


proof_lines: synthesis direction, wild type protein, pH 7.2, 30°C

proof_lines: degradation direction, wild type protein, pH 7.2, 30°C


substrate_name: alpha-D-galactose 1-phosphate

substrate: alpha-D-galactose 1-phosphate


organism: Aspergillus oryzae

substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Bos taurus

substrate_name: Carbamoyl phosphate

proof_lines:
enzyme from testes
enzyme from brain
enzyme from pancreas

substrate: Carbamoyl phosphate


organism: Dictyostelium discoideum

proof_lines:
pH 7.5, smlA mutant enzyme
pH 7.5, coutin mutant enzyme


proof_lines: cleared lysate of countin- cells with low activity of counting factor

proof_lines: crude cytosol of cells with low counting factor

proof_lines: crude cytosol of countin- cells with low activity of counting factor


proof_lines:
crude cytosol of wild-type
pH 7.5, wild-type enzyme
cleared lysate of wild-type


organism: Gallus gallus


proof_lines:
in detergent treated microsomes
in intact microsomes


organism: Limulus sp.


organism: Mustela vison

substrate_name: H2O; Glucose 6-phosphate

substrate: H2O; Glucose 6-phosphate


substrate_name: pyruvate

proof_lines: pH 7.5, wild-type and K133Q/T161K mutant

substrate: pyruvate


organism: Haloferax volcanii


proof_lines:
enzyme in disrupted microsomes
pH 6.5, in disrupted vesicles
microsomal enzyme suspension


organism: Streptococcus bovis

substrate_name: Glucose 6-phosphate; H2O

substrate: Glucose 6-phosphate; H2O


organism: Sus scrofa

proof_lines:
disrupted microsomes
intact microsomes


organism: Aspergillus fumigatus

substrate_name: Phe-Pro-Ala-p-nitroanilide

substrate: Phe-Pro-Ala-p-nitroanilide


organism: Pseudomonas sp. 101


organism: Homo sapiens

assay_conditions_summary: pH 7.8; 310.15 K; buffer 50 mM Tris

proof_lines: in 50 mM Tris buffer, 0.1 M NaCl, pH 7.8

proof_lines: prostate-specific antigen without inhibitor

proof_lines: prostate-specific antigen and inhibitor 2-(2-methyl-3-nitrophenyl)-4H-3,1-benzoxazin-4-one (25 micromol)


organism: Plasmodium falciparum

proof_lines:
pH 4.4, 37°C, recombinant enzyme
pH 4.4, 37°C, naturally occuring enzyme
pH 4.4, 37°C


enzyme_display_name: biotinidase

organism: Rattus norvegicus

proof_lines: pH 7.0, 37°C, enzyme from tigh muscle, female rat

proof_lines: pH 7.0, 37°C, enzyme from abdominal skin, female rat

proof_lines: pH 7.0, 37°C, enzyme from upper labial skin, male rat

enzyme: biotinidase


organism: Rattus rattus

substrate_name: lipoyllysine

proof_lines:
pH 6.0
crude liver extract
pH 9.5

substrate: lipoyllysine


substrate_name: epsilon-N-biotinyl-L-lysine

proof_lines:
serum
porcine liver
porcine serum

substrate: epsilon-N-biotinyl-L-lysine


enzyme_display_name: diisopropyl-fluorophosphatase

organism: Alteromonas sp.

substrate_name: diisopropyl fluorophosphate

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

enzyme: diisopropyl-fluorophosphatase

substrate: diisopropyl fluorophosphate


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

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

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


organism: Pseudomonas sp.


organism: Escherichia coli

proof_lines: mutant enzyme T161A, in 20 mM HEPES, pH 7.5, at 23°C


organism: Helicobacter pylori


organism: Pseudomonas fluorescens


organism: Pseudomonas putida


organism: Thermotoga maritima


organism: Zymomonas mobilis


enzyme_display_name: xylose isomerase

organism: Actinoplanes missouriensis

substrate_name: L-arabinose

enzyme: xylose isomerase

substrate: L-arabinose


proof_lines:
wild-type
wild-type enzyme


organism: Brevundimonas diminuta


organism: Doryteuthis pealeii


organism: Loligo vulgaris

proof_lines: pH 8, 35°C, effects of pH, temperature and ionic strength on kcat are studied


organism: Pseudoalteromonas undina


organism: Azotobacter vinelandii


proof_lines:
KA2 variant, pH 7.5, 25°C
KA3 variant, pH 7.5, 25°C
KA1-1 variant, pH 7.5, 25°C


proof_lines: wild type enzyme, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme S184D, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme S184L, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme S184A, in 100 mM HEPES, pH 7.5


proof_lines: mutant enzyme T161V, in 20 mM HEPES, pH 7.5, at 23°C


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:15713782 and selected BRENDA note anchor the F26W mutation; variant sequence reconstructed in this review. and applied mutation signature F26W to reconstruct the assayed variant sequence.

substrate: D-glucose


substrate_name: D-xylose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the E217S mutation; variant sequence reconstructed in this review. and applied mutation signature E217S to reconstruct the assayed variant sequence.

substrate: D-xylose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the H220Q mutation; variant sequence reconstructed in this review. and applied mutation signature H220Q to reconstruct the assayed variant sequence.

proof_lines:
mutant H220Q
D-glucose, mutant H220Q
D-xylose, mutant H220Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the H220N mutation; variant sequence reconstructed in this review. and applied mutation signature H220N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the E181D mutation; variant sequence reconstructed in this review. and applied mutation signature E181D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the D255N mutation; variant sequence reconstructed in this review. and applied mutation signature D255N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the E181Q mutation; variant sequence reconstructed in this review. and applied mutation signature E181Q to reconstruct the assayed variant sequence.

proof_lines:
mutant E181Q
D-xylose, mutant E181Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the D257N mutation; variant sequence reconstructed in this review. and applied mutation signature D257N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P12851 reviewed Actinoplanes missouriensis xylA sequence; PMID:1610791 and selected BRENDA note anchor the D257E mutation; variant sequence reconstructed in this review. and applied mutation signature D257E to reconstruct the assayed variant sequence.


organism: Arthrobacter sp.

sequence_source: UniProtKB:P12070 reviewed entry; PubMed PMID:1854338 characterizes Arthrobacter strain NRRL B3728 xylose/glucose isomerase and UniProt cites that paper for characterization.


organism: Bacillus sp. (in: firmicutes)


organism: Bacteroides stercoris

sequence_source: GenBank JF441172.1 / protein AEK21499.1; PubMed PMID:21655987 paper-linked Bacteroides stercoris strain HJ-15 xylA complete CDS.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 100 mM Tris-HCl

proof_lines: in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30°C


organism: Piromyces sp.


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2 and applied mutation signature E129D/V433I/E15D/E114G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E129D/V433I/E15D/E114G, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2 and applied mutation signature E129D/V433I/E15D/E114G/T142S/A177T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E129D/V433I/E15D/E114G/T142S/A177T, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2 and applied mutation signature E129D/V433I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E129D/V433I, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


sequence_source: UniProtKB:A0ACD6B9F5 plus PMID:22685138 Table 2

proof_lines: wild type enzyme, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C


organism: Streptomyces albus


organism: Streptomyces corchorusii


organism: Streptomyces flavogriseus

proof_lines:
soluble enzyme
immobilized enzyme


organism: Streptomyces olivochromogenes


organism: Streptomyces pseudogriseolus

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, wild-type

proof_lines: native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


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

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N


enzyme_display_name: chymotrypsin C

organism: Homo sapiens

substrate_name: succinyl-Ala-Ala-Pro-Phe 4-nitroanilide

enzyme: chymotrypsin C

substrate: succinyl-Ala-Ala-Pro-Phe 4-nitroanilide


organism: Bifidobacterium adolescentis


organism: Geobacillus stearothermophilus

substrate_name: D-xylulose

substrate: D-xylulose


organism: Heyndrickxia coagulans


organism: Lachnoclostridium phytofermentans

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


organism: Lactococcus lactis


organism: Lactococcus lactis subsp. lactis


organism: Levilactobacillus brevis

substrate_name: D-ribose

substrate: D-ribose


organism: Limosilactobacillus reuteri


organism: Opuntia ficus-indica

proof_lines: enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C


organism: Parabacteroides sp.

substrate_name: alpha-D-xylopyranose

substrate: alpha-D-xylopyranose


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


enzyme_display_name: acetate kinase (diphosphate)

organism: Entamoeba histolytica

substrate_name: acetate

smiles: CC(=O)O

enzyme: acetate kinase (diphosphate)

substrate: acetate


substrate_name: phosphate

proof_lines: mutant enzyme Q323A/M324A, at pH 7.0 and 37Â°C

proof_lines: mutant enzyme Q323A/M324A, at pH 5.5 and 45Â°C

substrate: phosphate


substrate_name: diphosphate

substrate: diphosphate


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


proof_lines:
wild type enzyme, at pH 5.5 and 45Â°C
wild type enzyme, at pH 7.0 and 37Â°C


substrate_name: acetyl phosphate

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

substrate: acetyl phosphate


enzyme_display_name: ribonuclease H

organism: Aquifex aeolicus

substrate_name: RNA-DNA hybrid

proof_lines: wild type enzyme, in 10 mM Tris/HCl (pH 9.0) containing 10 mM MgCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C

proof_lines: wild type enzyme, in 10 mM Tris/HCl (pH 9.0) containing 10 mM MnCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C

enzyme: ribonuclease H

substrate: RNA-DNA hybrid


proof_lines: mutant enzyme Y45A, in 10 mM Tris/HCl (pH 9.0) containing 2 mM MnCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C

proof_lines: mutant enzyme Y45A, in 10 mM Tris/HCl (pH 9.0) containing 10 mM MgCl2, 100 mM KCl, 1 mM beta-mercaptoethanol and 0.05 mg/ml bovine serum albumin, at 30°C


organism: Archaeoglobus fulgidus

substrate_name: RNA-DNA*DNA hybrid

proof_lines: recombinant mutant R46A and K143A, pH 8.0, 30°C

substrate: RNA-DNA*DNA hybrid


assay_conditions_summary: pH 7; cofactor ATP

proof_lines: mutant enzyme Q323G/M324I, at pH 7.0 and 37Â°C

proof_lines: mutant enzyme Q323G/M324I, at pH 5.5 and 45Â°C


assay_conditions_summary: pH 5.5; 355.15 K; cofactor ATP


proof_lines: mutant enzyme D272A/R274A/Q323G/M324I, at pH 7.0 and 37Â°C


assay_conditions_summary: pH 7; 355.15 K; cofactor ATP


organism: Aeropyrum pernix


assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


proof_lines:
pH 6.0, 37°C, recombinant enzyme
pH 7.0, 37°C, recombinant enzyme


organism: Shewanella sp.

substrate_name: M13 DNA-RNA hybrid

proof_lines:
pH 8.5, 15°C, recombinant enzyme
pH 8.5, 30°C, recombinant enzyme

substrate: M13 DNA-RNA hybrid


organism: Thermotoga maritima

substrate_name: M13 DNA/RNA hybrid

proof_lines: wild-type enzyme, pH 9.0, 30°C, in presence of 50 mM KCl

substrate: M13 DNA/RNA hybrid


organism: Homo sapiens


substrate_name: succinyl-Ala-Ala-Pro-Gln 4-nitroanilide

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

substrate: succinyl-Ala-Ala-Pro-Gln 4-nitroanilide


organism: Escherichia coli

proof_lines: pH 8.5, 15°C or 30°C, recombinant enzyme


organism: Geobacillus stearothermophilus

proof_lines: pH 8.5, 30°C, Mg2+, recombinant mutant K50A


proof_lines: pH 8.5, 30°C, Mg2+, recombinant wild-type enzyme


proof_lines: pH 8.5, 30°C, Mg2+, recombinant mutant V42A


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


proof_lines: mutant R291H, pH 8.0, temperature not specified in the publication


proof_lines: mutant K143I, pH 8.0, temperature not specified in the publication


substrate_name: DNA-RNA hybrid duplex RD12

proof_lines: at 28°C, pH not specified in the publication

substrate: DNA-RNA hybrid duplex RD12


organism: Pyrococcus furiosus

substrate_name: RNA-DNA heteroduplex

proof_lines: 50°C, pH 8.0, wild-type enzyme, divalent cation: Mn2+

proof_lines: 50°C, pH 8.0, wild-type enzyme, divalent cation: Mg2+

substrate: RNA-DNA heteroduplex


proof_lines: 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme A115E


proof_lines: 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme R113E


proof_lines: 50°C, pH 8.0, divalent cation: Mn2+, mutant enzyme F114E


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


organism: Xenotropic MuLV-related virus (isolate VP62)

substrate_name: RNA/DNA duplex

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

substrate: RNA/DNA duplex


sequence_source: UniProtKB:Q99895 direct lookup; canonical identity context only, variant sequence not reconstructed


proof_lines: mutant enzyme T58M, pH and temperature not specified in the publication


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: a hybrid RNA/DNA substrate

sequence_source: source_record; direct UniProt P9WLH5 FASTA match

proof_lines: Vmax value for RNase H activity is identical to that for dsRNase activity.

substrate: a hybrid RNA/DNA substrate


enzyme_display_name: dipeptidyl-peptidase II

substrate_name: Ser-Pro-p-nitroanilide

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

enzyme: dipeptidyl-peptidase II

substrate: Ser-Pro-p-nitroanilide


enzyme_display_name: cystinyl aminopeptidase

substrate_name: H2O; Arginine-4-nitroanilide

enzyme: cystinyl aminopeptidase

substrate: H2O; Arginine-4-nitroanilide


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature V87G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature H172A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature H117A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature I116A to reconstruct the assayed variant sequence.


proof_lines: co-substrate: hexanoate, 45°C, pH 7.5, mutant T223P


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature V87A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from PMID 22903977 / PMCID PMC3485911 ORF EHI_170010; UniProt C4M1C3 and NCBI XP_655990.1 canonical protein sequence and applied mutation signature I116L to reconstruct the assayed variant sequence.


substrate_name: valerate

proof_lines: co-substrate: propionate, 37°C, pH 7.5, wild-type

substrate: valerate


proof_lines:
pH 6.5-7.5, 30°C, recombinant enzyme
pH 7, 30°C


organism: Bos taurus

substrate_name: poly(rAdT)

substrate: poly(rAdT)


organism: Drosophila melanogaster

substrate_name: DNA-RNA hybrid duplex

proof_lines:
at pH 8.0 and 30°C
at pH 8.0 and 37°C

substrate: DNA-RNA hybrid duplex


proof_lines: pH 8.5, 30°C, recombinant soluble non-tagged enzyme


organism: Streptomyces pseudogriseolus

substrate_name: D-glucose

proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A

substrate: D-glucose


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N


proof_lines: 60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A


substrate_name: D-xylose

proof_lines: mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

substrate: D-xylose


proof_lines: mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C

proof_lines: mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C


proof_lines: mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C


enzyme_display_name: agmatine N(4)-coumaroyltransferase

organism: Hordeum vulgare

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
isoenzyme 1
isoenzyme 2
recombinant enzyme

enzyme: agmatine N(4)-coumaroyltransferase


substrate_name: feruloyl-CoA

proof_lines: wild type enzyme isoform ACT2, at pH 7.5 and 25°C

substrate: feruloyl-CoA


proof_lines: mutant enzyme E374A of isoform ACT1-1, at pH 7.5 and 25°C


proof_lines: wild type enzyme isoform ACT1-1, at pH 7.5 and 25°C


enzyme_display_name: 3',5'-cyclic-AMP phosphodiesterase

organism: Dictyostelium discoideum

substrate_name: Adenosine 3',5'-phosphate; H2O

enzyme: 3',5'-cyclic-AMP phosphodiesterase

substrate: Adenosine 3',5'-phosphate; H2O


substrate_name: cAMP; H2O

substrate: cAMP; H2O


substrate_name: agmatine

proof_lines: mutant enzyme E372A of isoform ACT1-1, at pH 7.5 and 25°C

substrate: agmatine


proof_lines: mutant enzyme W376A of isoform ACT1-1, at pH 7.5 and 25°C


organism: Oryza sativa Japonica Group


organism: Triticum aestivum

substrate_name: cinnamoyl-CoA

substrate: cinnamoyl-CoA


substrate_name: ADP-L-glycero-beta-D-manno-heptose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

substrate: ADP-L-glycero-beta-D-manno-heptose


substrate_name: alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]

proof_lines: pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A


substrate: alpha-Kdo-(2->4)-alpha-Kdo-(2->6)-[O-deacylated Escherichia coli Kdo2-lipid A]


substrate_name: H2O; Adenosine 3',5'-phosphate

proof_lines: pH and temperature not specified in the publication

substrate: H2O; Adenosine 3',5'-phosphate


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


proof_lines: pH 7.5, 37°C, mutant enzyme K64A/R63A/R61A/R60A


proof_lines: pH and temperature not specified in the publication, in absence of detergent

proof_lines: pH and temperature not specified in the publication, with Triton X-100


proof_lines: pH 7.5, 37°C, mutant enzyme K64A/R63A/R61/R60A


proof_lines: pH 7.5, 37°C, mutant enzyme R60A/R63A/R64A


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

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

source_databases_merged: sabio_rk brenda skid


substrate_name: cAMP

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

substrate: cAMP


proof_lines: mutant enzyme T748A, in 20 mM Tris-HCl, pH 7.5, 4 mM MnCl2, at 24°C


proof_lines: wild type PDE8A1 catalytic domain, in 20 mM Tris-HCl, pH 7.5, 4 mM MnCl2, at 24°C


substrate_name: guanosine 3',5'-cyclic phosphate

substrate: guanosine 3',5'-cyclic phosphate


organism: Leishmania major


enzyme_display_name: N-methylcarbamate hydrolase

organism: Novosphingobium sp. KN65.2

substrate_name: oxamyl

smiles: CN=C(O)O/N=C(\SC)C(=O)N(C)C

enzyme: N-methylcarbamate hydrolase

substrate: oxamyl


substrate_name: carbofuran

substrate: carbofuran


organism: Pseudomonas sp. C5pp

substrate_name: Carbaryl

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

proof_lines: recombinant enzyme rCHDELTA(Tmd)a, at pH 7.5, temperature not specified in the publication

substrate: Carbaryl


organism: Pseudomonas sp. XWY-1


organism: Mus musculus


organism: Pseudomonas aeruginosa

proof_lines: the addition of FeCl2 does not significantly influence substrate affinity of CdpA increases the rate of the 5-AMP production, pH and temperature not specified in the publication


organism: Rattus norvegicus


substrate_name: H2O; 3',5'-Cyclic AMP

substrate: H2O; 3',5'-Cyclic AMP


organism: Trypanosoma cruzi


organism: Trypanosoma brucei


organism: Marchantia polymorpha


organism: Rhizobium sp. AC100

proof_lines:
at pH 7.5 and 30Â°C
at pH 7.0 and 30°C


enzyme_display_name: apyrase

organism: Aedes albopictus

substrate_name: ATP; H2O

assay_conditions_summary: cofactor ATP

enzyme: apyrase

substrate: ATP; H2O


organism: Arabidopsis thaliana


substrate_name: IDP

substrate: IDP


organism: Bacillus thuringiensis

substrate_name: H2O; ATP

substrate: H2O; ATP


organism: Sphingobium sp. CFD-1


organism: Heligmosomoides polygyrus bakeri

substrate_name: ATP

assay_conditions_summary: pH 7.5; 297.15 K; cofactor ATP

substrate: ATP


organism: Homo sapiens

substrate_name: ADP; H2O

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines: pH 6.5, temperature not specified in the publication, NTPDase8

substrate: ADP; H2O


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


proof_lines: pH 6.5, temperature not specified in the publication, NTPDase3


proof_lines: pH 6.5, temperature not specified in the publication, NTPDase2


organism: Bos taurus


organism: Canis familiaris


organism: Gallus gallus


substrate_name: dCTP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: pH 6.5, temperature not specified in the publication, NTPDase1

substrate: dCTP


substrate_name: ADP

assay_conditions_summary: pH 7.4; 298.15 K; cofactor ADP

proof_lines: recombinant mutant EDC DELTA MIL, pH 7.4, 25°C

substrate: ADP


substrate_name: TDP

substrate: TDP


substrate_name: GDP

substrate: GDP


proof_lines: in presence of 0.1 mM AMP, recombinant wild-type enzyme, pH 7.4, 25°C

proof_lines: in presence of 0.1 mM UMP, recombinant wild-type enzyme, pH 7.4, 25°C


substrate_name: UTP

substrate: UTP


proof_lines: recombinant mutant EDC Y314F, pH 7.4, 25°C


substrate_name: GTP

substrate: GTP


proof_lines:
at pH 7.4 and 25°C
Raw SKiD Env: Temp=25°C, pH=7.4


substrate_name: AMPCPP

substrate: AMPCPP


substrate_name: ITP

substrate: ITP


proof_lines: recombinant mutant EDC K257M, pH 7.4, 25°C


substrate_name: UDP

substrate: UDP


proof_lines: recombinant mutant EDC Y409F, pH 7.4, 25°C


substrate_name: H2O; UTP

substrate: H2O; UTP


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


organism: Saccharomyces cerevisiae


organism: Sus scrofa


enzyme_display_name: geranylgeranyl diphosphate synthase

organism: Plasmodium falciparum

substrate_name: isopentenyl diphosphate

proof_lines: pH 7.5, 37°C, recombinant enzyme, with dimethylallyl diphosphate

proof_lines: pH 7.5, 37°C, recombinant enzyme, with isopentenyl diphosphate

proof_lines: pH 7.5, 37°C, recombinant enzyme, with (2E,6E)-farnesyl diphosphate

enzyme: geranylgeranyl diphosphate synthase

substrate: isopentenyl diphosphate


substrate_name: Isopentenyl diphosphate

smiles: C=C(C)CCOP(=O)(O)OP(=O)(O)O

substrate: Isopentenyl diphosphate


substrate_name: trans,trans-Farnesyl diphosphate

substrate: trans,trans-Farnesyl diphosphate


organism: Haematococcus lacustris


organism: Hevea brasiliensis


substrate_name: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate


substrate: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate


organism: Lutzomyia longipalpis

proof_lines: pH 7.2, 30°C, cosubstrate: (2E,6E)-farnesyl diphosphate

proof_lines: pH 7.2, 30°C, cosubstrate: isopentenyl diphosphate


organism: Picea abies

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Choristoneura fumiferana

substrate_name: Unknown

substrate: Unknown


organism: Eucommia ulmoides

proof_lines: fixed substrate: farnesyl diphosphate, enzyme EuFPS1, pH 7.0, 25°C

proof_lines: fixed substrate: isopentenyl diphosphate, enzyme EuFPS1, pH 7.0, 25°C

proof_lines: fixed substrate: dimethylallyl diphosphate, enzyme EuFPS1, pH 7.0, 25°C


substrate_name: geranyl diphosphate

proof_lines: fixed substrate: isopentenyl diphosphate, enzyme EuFPS2, pH 7.0, 25°C

proof_lines: fixed substrate: dimethylallyl diphosphate, enzyme EuFPS2, pH 7.0, 25°C

proof_lines: fixed substrate: farnesyl diphosphate, enzyme EuFPS2, pH 7.0, 25°C

substrate: geranyl diphosphate


organism: Geobacillus stearothermophilus

substrate_name: Isopentenyl diphosphate; Geranyl diphosphate


substrate_name: (E,E)-farnesyl diphosphate

substrate: (E,E)-farnesyl diphosphate


substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


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


proof_lines:
mutant DELTA1-6, pH 7.5, 25°C
mutant DELTA1-9, pH 7.5, 25°C
mutant DELTA1-7, pH 7.5, 25°C


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


organism: Taxus canadensis


organism: Thermococcus kodakarensis

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Toxoplasma gondii


enzyme_display_name: 1-phosphatidylinositol 4-kinase

organism: Homo sapiens

substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

enzyme: 1-phosphatidylinositol 4-kinase

substrate: ATP


substrate_name: ATP; 1-Phosphatidyl-1D-myo-inositol

substrate: ATP; 1-Phosphatidyl-1D-myo-inositol


organism: Hordeum vulgare

substrate_name: agmatine

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

assay_conditions_summary: cofactor CoA

substrate: agmatine


organism: Escherichia coli O18:K1:H7 (strain RS218 / NMEC)

substrate_name: ADP-heptose

assay_conditions_summary: cofactor ADP

substrate: ADP-heptose


organism: Escherichia coli (strain K12)

substrate_name: ADP-mannose

substrate: ADP-mannose


organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)

substrate_name: geranylgeranyl diphosphate (GGDP)

substrate: geranylgeranyl diphosphate (GGDP)


organism: Diaporthe amygdali

substrate_name: GPP

substrate: GPP


organism: Emericella variicolor

substrate_name: geranylgeranyl pyrophosphate

substrate: geranylgeranyl pyrophosphate


substrate_name: DMAPP

substrate: DMAPP


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Talaromyces verruculosus

substrate_name: DMAPP (for prenyltransferase activity)

substrate: DMAPP (for prenyltransferase activity)


substrate_name: PtdIns

substrate: PtdIns


organism: Rattus norvegicus

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


enzyme_display_name: polynucleotide 3'-phosphatase

organism: Arabidopsis thaliana

substrate_name: single-stranded oligonucleotide

enzyme: polynucleotide 3'-phosphatase

substrate: single-stranded oligonucleotide


organism: Dictyostelium discoideum

substrate_name: cAMP (catalytic domain expressed in vegetative AX2 cells)


substrate_name: cAMP

substrate: cAMP


organism: Drosophila melanogaster


substrate_name: cAMP (isoform 1)

substrate: cAMP (isoform 1)


substrate_name: 3',5'-cyclic AMP

substrate: 3',5'-cyclic AMP


substrate_name: ATP

assay_conditions_summary: pH 7.4; cofactor ATP

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


proof_lines: mutant enzyme R492G, at pH 7.4, temperature not specified in the publication


proof_lines: mutant enzyme R492G/E493G, at pH 7.4, temperature not specified in the publication


organism: Plasmodium falciparum


enzyme_display_name: ribonuclease Z

organism: Bacillus subtilis

substrate_name: pre-tRNA(Arg1); pre-tRNA(Arg2)

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

enzyme: ribonuclease Z

substrate: pre-tRNA(Arg1); pre-tRNA(Arg2)


proof_lines: 25 mM Tris-HCl pH 7.0, 1 mM MgCl2, 1 mM DTT, 50 mM KCl at 28°C


organism: Methanococcus maripaludis

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


organism: Unknown

substrate: ATP


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


organism: Methanolobus psychrophilus


organism: Sus scrofa

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP


substrate_name: ATP; H2O

substrate: ATP; H2O


organism: Toxoplasma gondii

proof_lines: mutant enzyme E493G, at pH 7.4, temperature not specified in the publication


organism: Taxus baccata


organism: Taxus canadensis

substrate_name: farnesyl diphosphate

proof_lines:
cosubstrate geranyl diphosphate
cosubstrate dimethylallyl diphosphate
cosubstrate farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Thermococcus kodakaraensis

substrate_name: Dimethylallyl diphosphate; Isopentenyl diphosphate


organism: Bos taurus

substrate_name: phosphatidylinositol

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines:
in presence of 20 mM MgCl2
ATP in form of MgATP2-
pH 7.0, 30°C

substrate: phosphatidylinositol


organism: Daucus carota

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Dunaliella parva

assay_conditions_summary: pH 7.8; 301.15 K; cofactor ATP

proof_lines:
pH 7.8, 28°C, at 30 mM MgCl2
pH 7.8, 28°C, at 0.75 mM Triton X-100
pH 7.8, 28°C, at 1.5 mM Triton X-100


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines:
pH 7.4, 30°C, enzyme form mPIK-I
pH 7.4, 25°C
pH 7.2, 37°C


organism: Legionella micdadei

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Mus musculus

assay_conditions_summary: pH 7.1; 298.15 K; cofactor ATP


organism: Oryctolagus cuniculus

assay_conditions_summary: cofactor ATP

proof_lines:
PI kinase II
PI kinase III
PI kinase I


organism: Ovis aries


organism: Rattus norvegicus

substrate_name: ATP; 1-Phosphatidyl-D-myo-inositol

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, in presence of at least 20 mM MgCl2

substrate: ATP; 1-Phosphatidyl-D-myo-inositol


organism: Saccharomyces cerevisiae

substrate_name: trans,trans-farnesyl diphosphate

substrate: trans,trans-farnesyl diphosphate


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/F108A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant F108A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant L135A/H139A


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/F108A


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


proof_lines: pH 7.5, 25°C, recombinant mutant Y107A/F108A/L135A/H139A


organism: Sinapis alba

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Sulfolobus acidocaldarius

substrate_name: (2E,6E)-farnesyl diphosphate

substrate: (2E,6E)-farnesyl diphosphate


organism: Methanothermobacter thermautotrophicus


organism: Micrococcus luteus

substrate_name: isopentenyl diphosphate

proof_lines: cosubstrate dimethylallyl diphosphate at 0.175 mM

substrate: isopentenyl diphosphate


organism: Monolepta hieroglyphica

proof_lines: pH 7.4, 37°C, cosubstrate: isopentenyl diphosphate

proof_lines: pH 7.4, 37°C, cosubstrate: (2E,6E)-farnesyl diphosphate


organism: Nicotiana tabacum

proof_lines: cosubstrate farnesyl diphosphate, GGPPS2


organism: Pantoea ananatis

substrate_name: geranyl diphosphate

substrate: geranyl diphosphate


organism: Phycomyces blakesleeanus


organism: Plasmodium vivax


proof_lines: pH 7.0, 37°C, carboxy-terminal deletion mutant DELTA-12


proof_lines: pH 7.0, 37°C, carboxy-terminal deletion mutant DELTA-8


proof_lines: pH 7.0, 37°C, carboxy-terminal deletion mutant DELTA-4


organism: Ricinus communis


organism: Hordeum murinum

substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: caffeoyl-CoA


organism: Hordeum vulgare

substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ADP

proof_lines: pH and temperature not specified in the publication


organism: Antirrhinum majus

proof_lines: heterodimer of geranyl phosphate synthase small subunit of Antirrhinum majus with Nicotiana tabacum geranylgeranyl diphosphate synthase GGPPS2

proof_lines: heterodimer of geranyl phosphate synthase small subunit of Antirrhinum majus with Nicotiana tabacum geranylgeranyl diphosphate synthase GGPPS1


organism: Bacillus subtilis


organism: Bos taurus


organism: Capsicum annuum


organism: Corynebacterium glutamicum

proof_lines: pH 7.5, 30°C, recombinant His-tagged enzyme


organism: Cucurbita pepo


organism: Homo sapiens

proof_lines: pH 7.7, 37°C, recombinant enzyme, versus trans,trans-farnesyl diphosphate


organism: Kitasatospora griseola


proof_lines:
cosubstrate farnesyl diphosphate
cosubstrate dimethylallyl diphosphate


organism: Gallus gallus


organism: Mus musculus


substrate_name: ATP (at pH 7.4)

substrate: ATP (at pH 7.4)