proof_lines: mutant enzyme E188K/H125R, at pH 4.3 and 25°C


organism: Dictyostelium discoideum

substrate_name: UDP-GlcNAc

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: The low Vmax value suggests that the enzyme may be down-regulated under the assay conditions.

substrate: UDP-GlcNAc

source: uniprot


enzyme_display_name: DNA primase DnaG

organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: NTPs

enzyme: DNA primase DnaG

substrate: NTPs


enzyme_display_name: beta-galactosidase

organism: Arabidopsis thaliana

substrate_name: para-nitrophenyl-beta-D-galactoside

proof_lines: Measured at pH 4.5 and 37 degrees Celsius for all experiments.

enzyme: beta-galactosidase

substrate: para-nitrophenyl-beta-D-galactoside


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

substrate_name: lactose

substrate: lactose


organism: Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)

substrate_name: Gal-beta-PNP

substrate: Gal-beta-PNP


organism: Caldicellulosiruptor owensensis (strain ATCC 700167 / DSM 13100 / OL)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (pNPGal) (at pH 5.5 and 75 degrees Celsius)

proof_lines: kcat is 4522 sec(-1) with pNPGal as substrate. kcat is 3750.6 sec(-1) with pNPGlu as substrate. kcat is 944.3 sec(-1) with pNPC as substrate. kcat is 652.6 sec(-1) with pNPX as substrate. kcat is 2149 sec(-1) with cellobiose as substrate.


organism: Escherichia coli (strain K12)

substrate_name: p-nitrophenyl beta-D-galactoside

proof_lines: The values for the enzymatic assays using manganese as cofactor are very close.

substrate: p-nitrophenyl beta-D-galactoside


enzyme_display_name: dye decolorizing peroxidase

organism: Auricularia auricula-judae

substrate_name: Reactive Black 5

source_db: brenda

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

assay_conditions_summary: pH 3; 293.15 K; buffer sodium tartrate

proof_lines: manganese-independent peroxidase I, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C

proof_lines: manganese-independent peroxidase II, at pH 3.0 in sodium tartrate buffer (50 mM), at 20°C

proof_lines: manganese-independent peroxidase II, at pH 4.5 in sodium tartrate buffer (50 mM), at 20°C

enzyme: dye decolorizing peroxidase

substrate: Reactive Black 5

source: brenda


organism: Bacillus subtilis

proof_lines: pH and temperature not specified in the publication

proof_lines: with 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) as cosubstrate, at pH 4.0 and 30°C


organism: Basidiomycota sp.

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


mutation_type: substitution


proof_lines: mutant enzyme D222E/R390K, at pH 3.0 and 25°C


organism: Bjerkandera adusta

proof_lines:
at pH 4.0 and 30°C
at pH 4.0 and 50°C
at pH 3.0 and 70°C


organism: Cellulomonas bogoriensis

substrate_name: Reactive Blue 19

assay_conditions_summary: pH 5

proof_lines: wild type enzyme, at pH 5.0, temperature not specified in the publication

proof_lines: wild type enzyme, with Reactive Blue 19 as cosubstrate, at pH 5.0, temperature not specified in the publication

substrate: Reactive Blue 19


proof_lines: mutant enzyme E201D, at pH 5.0, temperature not specified in the publication

proof_lines: mutant enzyme E201D, with Reactive Blue 19 as cosubstrate, at pH 5.0, temperature not specified in the publication


organism: Geotrichum candidum

proof_lines: using AQ2 as cosubstrate, at pH 3.2 and 30°C

proof_lines: using Reactive Blue 5 as cosubstrate, at pH 3.2 and 30°C


organism: Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46)

substrate_name: ONPG (at 30 degrees Celsius and pH 6.5)

substrate: ONPG (at 30 degrees Celsius and pH 6.5)


organism: Bacillus subtilis (strain 168)

substrate_name: p-nitrophenyl beta-D-galactopyranoside (at pH 7.0 and 37 degrees Celsius)


organism: Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 / E194a)

substrate_name: Gal(beta1-4)Gal (at 37 degrees Celsius and pH 6.0)


organism: Carnobacterium maltaromaticum

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 30 degrees Celsius)


organism: Clostridium cellulovorans (strain ATCC 35296 / DSM 3052 / OCM 3 / 743B)

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


organism: Enterobacter agglomerans

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (at 37 degrees Celsius)


organism: Geobacillus kaustophilus

substrate_name: ONPG (at 55 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7

substrate: ONPG (at 55 degrees Celsius and pH 7.0)


organism: Haloferax lucentense (strain DSM 14919 / JCM 9276 / NCIMB 13854 / Aa 2.2)

substrate_name: ONPG (in the presence of 2.5 M NaCl, at room temperature and pH 7.2)


organism: Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)

substrate_name: o-nitrophenyl-beta-D-galactopyranoside (ONPG) (at 37 degrees Celsius and pH 6.0)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Planococcus sp. (strain L4)

substrate_name: ONPG (at 5 degrees Celsius and at pH 6.8)


organism: Pseudomonas putida


organism: Streptomyces albidoflavus


organism: Streptomyces avermitilis

proof_lines:
at pH 4.0 and 25°C
at pH 4.5 and 30°C
at pH 4.5 and 25°C


organism: Streptomyces griseosporeus

substrate_name: o-Dianisidine

substrate: o-Dianisidine


organism: Streptomyces lividans


organism: Vibrio cholerae

proof_lines:
mutant enzyme D138V, at pH 4.0 and 25°C
mutant enzyme D138V, at pH 6.5 and 25°C


proof_lines:
wild type enzyme, at pH 4.5 and 25°C
wild type enzyme, at pH 7.0 and 25°C


organism: Xylaria grammica


enzyme_display_name: prostaglandin-endoperoxide synthase

organism: Bos taurus

substrate_name: arachidonic acid

enzyme: prostaglandin-endoperoxide synthase

substrate: arachidonic acid


organism: Homo sapiens

substrate_name: (5Z,8Z,11Z,14Z)-eicosatetraenoate (in absence of sodium nitroprusside NO donor)

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


substrate_name: arachidonate

data_origin: experimental

substrate: arachidonate


organism: Ovis aries


enzyme_display_name: abscisate beta-glucosyltransferase

organism: Solanum lycopersicum

substrate_name: abscisic acid

enzyme: abscisate beta-glucosyltransferase

substrate: abscisic acid


enzyme_display_name: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase

organism: Escherichia coli (strain K12)

substrate_name: lipid IV(A) (at pH 8)

assay_conditions_summary: pH 8

substrate: lipid IV(A) (at pH 8)


substrate_name: fructose

substrate: fructose


enzyme_display_name: 2-phospho-L-lactate transferase

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

substrate_name: FO

enzyme: 2-phospho-L-lactate transferase

substrate: FO


enzyme_display_name: L-arabinonolactonase

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

substrate_name: L-arabino-gamma-lactone

enzyme: L-arabinonolactonase

substrate: L-arabino-gamma-lactone


organism: Alicyclobacillus acidocaldarius subsp. acidocaldarius (strain ATCC 27009 / DSM 446 / BCRC 14685 / JCM 5260 / KCTC 1825 / NBRC 15652 / NCIMB 11725 / NRRL B-14509 / 104-IA)

substrate_name: ONPG (at 60 degrees Celsius and pH 6.0)

assay_conditions_summary: pH 6

substrate: ONPG (at 60 degrees Celsius and pH 6.0)


organism: Arthrobacter sp

substrate_name: ONPG (at 10 degrees Celsius)

substrate: ONPG (at 10 degrees Celsius)


substrate_name: ONPG

substrate: ONPG


organism: Bifidobacterium bifidum

substrate_name: lactose

proof_lines: hydrolysis transgalactosylation

substrate: lactose


organism: Bifidobacterium longum


organism: Bifidobacterium longum subsp. infantis

substrate_name: o-nitrophenyl beta-D-galactopyranoside

substrate: o-nitrophenyl beta-D-galactopyranoside


organism: Caldariella acidophila

substrate_name: 4-nitrophenyl beta-D-galactopyranoside

substrate: 4-nitrophenyl beta-D-galactopyranoside


organism: Caldicellulosiruptor saccharolyticus

proof_lines:
at pH 6.0 and 80°C
at 80°C and pH 6.0


organism: Clostridium perfringens

assay_conditions_summary: pH 6; 310.15 K; buffer 20 mM sodium acetate

proof_lines: mutant enzyme E467A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: mutant enzyme E354A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: wild type enzyme, in 20 mM sodium acetate buffer at pH 6.0, 37°C


proof_lines: mutant enzyme D429A, in 20 mM sodium acetate buffer at pH 6.0, 37°C


organism: Corynebacterium murisepticum

substrate_name: o-nitrophenyl-beta-D-galactoside

substrate: o-nitrophenyl-beta-D-galactoside


organism: Enterobacter cloacae

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

substrate: 2-nitrophenyl beta-D-galactopyranoside


organism: Kluyveromyces lactis


organism: Kluyveromyces marxianus

assay_conditions_summary: pH 6.8; 298.15 K; buffer mixture

proof_lines:
pH 6.8
dimeric enzyme, 25°C
strain A60


organism: Kluyveromyces sp.

proof_lines: free enzyme, substrate is milk, pH 7.5, 41°C

proof_lines: immobilized enzyme MP-MCC-Gal, substrate is milk, pH 7.5, 41°C

proof_lines: immobilized enzyme Fe-ALK-Gal, pH 7.5, 41°C


organism: Lactiplantibacillus pentosus


organism: Lactiplantibacillus plantarum


organism: Lactiplantibacillus plantarum WCFS1

proof_lines:
at pH 7.5 and 55°C
at pH 7.0 and 60°C


organism: Lactobacillus acidophilus


organism: Lactobacillus crispatus


organism: Lactobacillus delbrueckii


organism: Alicyclobacillus acidocaldarius

proof_lines:
pH 6.0, 65°C
strain HM-1
strain 11-1O


organism: Arthrobacter psychrolactophilus


organism: Arthrobacter sp.

sequence_source: UniProtKB Q7WTU5; BRENDA EC 3.2.1.23 page links Q7WTU5 to Arthrobacter sp. SB and PMID 16736094


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTU5; BRENDA EC 3.2.1.23 page links Q7WTU5 to Arthrobacter sp. SB and PMID 16736094 and applied mutation signature E229D/V405A to reconstruct the assayed variant sequence.

proof_lines: 15°C, recombinant mutant BgaS7, i.e. E229D/V405A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7WTU5; BRENDA EC 3.2.1.23 page links Q7WTU5 to Arthrobacter sp. SB and PMID 16736094 and applied mutation signature E229D/V405A/G803D to reconstruct the assayed variant sequence.

proof_lines: 15°C, recombinant mutant BgaS6, i.e.E229D/V405A/G803D


organism: Aspergillus aculeatus


organism: Aspergillus carbonarius


organism: Aspergillus niger

proof_lines: enzyme immobilized on sucrose sulfate-polyacrolein


organism: Aspergillus oryzae

assay_conditions_summary: pH 4.5; 310.15 K; buffer mixture

proof_lines:
cross-linked enzyme, pH 4.5, 37°C
free enzyme, pH 4.5, 37°C
adsorbed enzyme, pH 4.5, 37°C


organism: Averrhoa carambola

substrate_name: nitrophenyl beta-D-galactoside

proof_lines:
37°C, pH 4.1,beta-galactosidase IV
37°C, pH 4.1,beta-galactosidase III
37°C, pH 4.1,beta-galactosidase II

substrate: nitrophenyl beta-D-galactoside


organism: Bacillus sp. (in: firmicutes)

proof_lines:
pH 7.6 enzyme
pH 10.2 enzyme


organism: Bacteroides polypragmatus


organism: Erythrina variegata


organism: Escherichia coli

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

assay_conditions_summary: pH 7.3; 298.15 K; buffer mixture

proof_lines:
dimeric enzyme, 25°C
tetrameric enzyme, 25°C
with 0.05 M NaCl


organism: Felis catus

substrate_name: ganglioside GM1

substrate: ganglioside GM1


organism: Geobacillus stearothermophilus


substrate_name: lactosucrose

substrate: lactosucrose


organism: Hamamotoa singularis


organism: Heyndrickxia coagulans

proof_lines:
at 55°C
at 30°C


organism: Hymenaea courbaril

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Irpex lacteus


organism: Planococcus sp. (strain 'SOS Orange')

substrate_name: ONPG (at 1.9 degrees Celsius and at pH 6.5)

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


organism: Pseudoalteromonas haloplanktis

substrate_name: lactose (at pH 7.5 and at 25 degrees Celsius)


organism: Thermus sp

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


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

verification_status: corrected

substrate: ONPG (at 70 degrees Celsius and pH 7.0)

status: corrected


organism: Thermus thermophilus

substrate_name: lactose (at pH 6.5 and at 70 degrees Celsius)


enzyme_display_name: maleylpyruvate hydrolase

organism: Aquipseudomonas alcaligenes

substrate_name: maleylpyruvate

enzyme: maleylpyruvate hydrolase

substrate: maleylpyruvate


organism: Homo sapiens

substrate_name: arachidonic acid

proof_lines:
mutant Y348F, cyclooxygenase activity
mutant enzyme Y348F

substrate: arachidonic acid


proof_lines:
mutant Y504F, cyclooxygenase activity
mutant enzyme Y504F
mutant Y504F, cyclooxygenase inhibition


proof_lines: mutant Y348F/Y504F, cyclooxygenase activity

proof_lines: mutant Y348F/Y504F, cyclooxygenase inhibition


organism: Oryctolagus cuniculus


organism: Ovis aries

substrate_name: cis-5,8,11,14-eicosatetraenoic acid

substrate: cis-5,8,11,14-eicosatetraenoic acid


organism: Dictyostelium sp.


organism: Macleaya microcarpa

substrate_name: abscisic acid

proof_lines: apparent value, at pH 5.0, temperature not specified in the publication

substrate: abscisic acid


organism: Escherichia coli

enzyme: lipid IVA 3-deoxy-D-manno-octulosonic acid transferase


organism: Pseudomonas aeruginosa

substrate_name: D-fructose[side 1]

substrate: D-fructose[side 1]


organism: Salmonella typhimurium

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


organism: Achatina achatina

substrate_name: 2-nitrophenyl beta-D-galactoside

substrate: 2-nitrophenyl beta-D-galactoside


organism: Actinomyces viscosus

substrate_name: lactose


organism: Cavia porcellus


substrate_name: arachidonate

substrate: arachidonate


proof_lines:
pH 7.2, 30°C, mutant enzyme N382L
pH 8.0, 23°C, mutant enzyme N382L


proof_lines:
pH 8.0, 23°C, wild-type enzyme
wild-type, cyclooxygenase activity
pH 7.2, 30°C, PGHS-2 wild-type enzyme


organism: Rhizomucor sp.

substrate_name: p-nitrophenyl beta-D-galactopyranoside

substrate: p-nitrophenyl beta-D-galactopyranoside


organism: Saccharolobus solfataricus

proof_lines:
pH 6.5, 30°C
pH 6.5, 75°C
at 75°C and pH 6.5

substrate: lactose


organism: Saccharomyces fragilis

substrate_name: o-nitrophenyl-beta-D-galactoside

proof_lines: enzyme immobilized on sucrose-polyacrolein


organism: Saccharopolyspora rectivirgula


organism: Sterigmatomyces elviae


organism: Streptococcus pneumoniae


organism: Streptococcus sp.


organism: Streptococcus thermophilus

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

proof_lines: in presence of 0.05 mM Mg2+ and 50 mM K+

proof_lines: in presence of 0.25 mM Mg2+, 50 mM K+ and 50 mM Na+


organism: Tenebrio molitor

substrate_name: 4-methylumbelliferyl beta-D-galactoside

proof_lines: hydrolysis of p-nitrophenyl beta-D-galactoside

proof_lines: hydrolysis of 4-methylumbellipheryl beta-D-galactoside

proof_lines: hydrolysis of 4-methylumbelliferyl beta-D-galactoside

substrate: 4-methylumbelliferyl beta-D-galactoside


organism: Thermoanaerobacter sp.

substrate: o-nitrophenyl-beta-D-galactoside


substrate_name: p-nitrophenyl-beta-D-galactoside

proof_lines:
at 25°C, in presence of 10 mM Mg2+
at 50°C, in presence of 10 mM Mg2+

substrate: p-nitrophenyl-beta-D-galactoside


organism: Thermomyces dupontii

proof_lines: native enzyme, substrate 2-nitrophenyl beta-D-galactoside, pH 6.5, 40°C


enzyme_display_name: histidine decarboxylase

organism: Raoultella planticola

substrate_name: L-His

enzyme: histidine decarboxylase

substrate: L-His


organism: Rattus norvegicus

substrate_name: L-Histidine

proof_lines:
membrane-bound enzyme
enzyme form 1
soluble enzyme

substrate: L-Histidine


organism: Tetragenococcus muriaticus

substrate_name: L-histidine

substrate: L-histidine


organism: Cupriavidus necator


organism: Herbaspirillum seropedicae


organism: Roseateles saccharophilus


organism: Paenibacillus macerans


organism: Papiliotrema laurentii


organism: Penicillium canescens


organism: Penicillium chrysogenum

substrate_name: o-nitrophenyl beta-D-galactopyranoside

substrate: o-nitrophenyl beta-D-galactopyranoside


organism: Penicillium citrinum


organism: Penicillium multicolor


organism: Petunia x hybrida

proof_lines:
enzyme form H3
enzyme form H4
enzyme form H2


organism: Phaseolus vulgaris


organism: Prunus persica


organism: Pseudarthrobacter oxydans

substrate_name: H2O; o-Nitrophenyl-beta-D-galactoside

substrate: H2O; o-Nitrophenyl-beta-D-galactoside


organism: Raphanus sativus


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

assay_conditions_summary: pH 3; buffer presence of 50 mM glycine/HCl

proof_lines: 97000 da enzyme form and 84000 Da enzyme form

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


organism: Lactobacillus helveticus


organism: Lactococcus lactis subsp. lactis


organism: Lathyrus oleraceus

proof_lines: in 50 mM sodium acetate-acetic acid, pH 4.0, at 37°C

proof_lines: enzyme immobilized on Amberlite MB-150 beads


organism: Limosilactobacillus reuteri

proof_lines: pH 6.5, 30°C, substrate: o-nitrophenyl-beta-D-galactoside, strain L461


organism: Macrotyloma geocarpum

substrate_name: Unknown

substrate: Unknown


organism: Marchantia polymorpha


organism: Mus musculus

proof_lines:
in presence of inhibitor
without inhibitor


organism: Neurospora crassa

proof_lines: beta-D-galactoside galactohydrolase pH 4.2

proof_lines: beta-D-galactoside galactohydrolase pH 4.5


organism: Niallia circulans


organism: Oreochromis niloticus


organism: Oryctolagus cuniculus


organism: Paecilomyces variotii


organism: Aquipseudomonas alcaligenes

proof_lines: pH and temperature not specified in the publication


organism: Clostridium perfringens


organism: Homo sapiens

proof_lines: pH 6.8, 37°C, recombinant enzyme, versus L-histidine


organism: Klebsiella aerogenes


organism: Lactobacillus sp.


organism: Lactobacillus sp. (strain 30a)


organism: Morganella morganii


organism: Oenococcus oeni


enzyme_display_name: 7,8-dihydroneopterin oxygenase

organism: Mycobacterium tuberculosis

source_db: oed

enzyme: 7,8-dihydroneopterin oxygenase

source: oed


enzyme_display_name: 2,5-dihydroxypyridine 5,6-dioxygenase

organism: Pseudomonas putida

substrate_name: O2; 2,5-Dihydroxypyridine

enzyme: 2,5-dihydroxypyridine 5,6-dioxygenase

substrate: O2; 2,5-Dihydroxypyridine


organism: Streptomyces avermitilis

substrate_name: (+/-)-1-deoxypentalenic acid

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

proof_lines: pH 6.0, temperature not specified in the publication

source_databases_merged: brenda skid

substrate: (+/-)-1-deoxypentalenic acid


enzyme_display_name: pyridinium-3,5-biscarboxylic acid mononucleotide synthase

organism: Lactiplantibacillus plantarum

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8; 295.15 K; cofactor NAD+

proof_lines:
pH 8.0, 22°C
Raw SKiD Env: Temp=22°C, pH=8

substrate: deamido-NAD+


enzyme_display_name: cysteine transaminase

organism: Rattus norvegicus

substrate_name: L-Cysteine; 2-Oxoglutarate

enzyme: cysteine transaminase

substrate: L-Cysteine; 2-Oxoglutarate


enzyme_display_name: putrescine--2-oxoglutarate transaminase

organism: Escherichia coli

substrate_name: 2-Oxoglutarate; Putrescine

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

source_databases_merged: sabio_rk brenda skid

enzyme: putrescine--2-oxoglutarate transaminase

substrate: 2-Oxoglutarate; Putrescine


enzyme_display_name: 2-phospho-L-lactate guanylyltransferase

organism: Methanocaldococcus jannaschii

substrate_name: (2S)-2-Phospholactate; GTP

enzyme: 2-phospho-L-lactate guanylyltransferase

substrate: (2S)-2-Phospholactate; GTP


enzyme_display_name: (S)-nandinine synthase

organism: Eschscholzia californica

substrate_name: H+; NADPH; O2; (S)-Scoulerine

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH

enzyme: (S)-nandinine synthase

substrate: H+; NADPH; O2; (S)-Scoulerine


enzyme_display_name: sulfite reductase (coenzyme F420)

substrate_name: sulfite

proof_lines: pH 7.0, temperature not specified in the publication

enzyme: sulfite reductase (coenzyme F420)

substrate: sulfite


organism: Methanosarcina barkeri


enzyme_display_name: 3-oxoadipyl-CoA thiolase

organism: Pseudomonas sp.

substrate_name: Coenzyme A; 3-Oxoadipyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: 3-oxoadipyl-CoA thiolase

substrate: Coenzyme A; 3-Oxoadipyl-CoA


organism: Gentiana triflora


enzyme_display_name: jasmonate O-methyltransferase

organism: Populus trichocarpa

substrate_name: benzoate

enzyme: jasmonate O-methyltransferase

substrate: benzoate


substrate_name: jasmonate

substrate: jasmonate


enzyme_display_name: [phosphatase 2A protein]-leucine-carboxy methyltransferase

organism: Homo sapiens

substrate_name: S-Adenosyl-L-methionine; [phosphatase 2A protein]-leucine


enzyme_display_name: molybdopterin adenylyltransferase

organism: Arabidopsis thaliana

substrate_name: ATP

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: 10 mM MgCl2, pH 7.2, temperature not specified in the publication

enzyme: molybdopterin adenylyltransferase

substrate: ATP


enzyme_display_name: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate

organism: Campylobacter jejuni


enzyme_display_name: ent-cassa-12,15-diene 11-hydroxylase

organism: Oryza sativa

proof_lines: in 0.1 M Tris-HCl, pH 7.2, 20% (v/v) glycerol, 0.5 mM EDTA, 1 mM dithiothreitol, temperature not specified in the publication

enzyme: ent-cassa-12,15-diene 11-hydroxylase


enzyme_display_name: monacolin L hydroxylase

organism: Aspergillus terreus

substrate_name: Monacolin L acid; O2; [reduced NADPH-hemoprotein reductase]

assay_conditions_summary: cofactor NADPH

enzyme: monacolin L hydroxylase


enzyme_display_name: tryptophan N-monooxygenase

substrate_name: L-Tryptophan; O2; NADPH; H+

assay_conditions_summary: pH 7.9; 307.15 K; cofactor NADPH

proof_lines:
in 100 mM Tricine, pH 7.9, at 34°C
recombinant enzyme, pH 7.9, 34°C

enzyme: tryptophan N-monooxygenase

substrate: L-Tryptophan; O2; NADPH; H+


enzyme_display_name: Glutarate 2-hydroxylase

sequence_source: UniProtKB:P76621 direct REST accession check (identity context only; sequence not emitted)

proof_lines:
pH 7.2, 30°C
Raw SKiD Env: Temp=30°C, pH=7.2

enzyme: Glutarate 2-hydroxylase


enzyme_display_name: Benzoyl-CoA oxygenase component A

organism: Aromatoleum evansii

substrate_name: benzoyl-CoA

sequence_source: UniProtKB:Q9AIX6 direct REST accession check (identity context only; sequence not emitted)

assay_conditions_summary: pH 8; 295.15 K; cofactor CoA

proof_lines: pH 8, 22°C, addition of the putative ring cleaving enzyme BoxC leads to a several-fold acceleration of the initial rate and completes conversion of benzoyl-CoA. Because of this complex behaviour of the oxygenase system, the apparent Km valu

enzyme: Benzoyl-CoA oxygenase component A

substrate: benzoyl-CoA


enzyme_display_name: benzoyl-CoA 2,3-epoxidase

organism: Azoarcus evansii

substrate_name: H+; NADPH; O2; Benzoyl-CoA

enzyme: benzoyl-CoA 2,3-epoxidase

substrate: H+; NADPH; O2; Benzoyl-CoA


enzyme_display_name: Ent-cassadiene C11-alpha-hydroxylase 1

substrate_name: O2; ent-Cassadiene; NADPH; H+

sequence_source: UniProtKB:Q69X58 direct REST accession check (identity context only; sequence not emitted)

enzyme: Ent-cassadiene C11-alpha-hydroxylase 1

substrate: O2; ent-Cassadiene; NADPH; H+


organism: Picea abies

proof_lines:
pH 7.0, 18°C, isozyme PtJAMT2
pH 7.0, 18°C, isozyme PtJAMT3
pH 6.5, 27°C, isozyme PtJAMT1


organism: Mycobacterium tuberculosis

substrate_name: alpha-ribazole 5'-phosphate

proof_lines:
full length protein
maltose binding protein fusion protein
Raw SKiD Env: Temp=-----, pH=-----

substrate: alpha-ribazole 5'-phosphate


organism: Campylobacter jejuni subsp. jejuni serotype O:2


enzyme_display_name: acyl-lysine deacylase

organism: Thermus thermophilus

enzyme: acyl-lysine deacylase


substrate_name: H2O; N2-Acetyl-L-ornithine

substrate: H2O; N2-Acetyl-L-ornithine


enzyme_display_name: cAMP deaminase

organism: Leptospira interrogans serovar Copenhageni str. Fiocruz L1-130

substrate_name: 3',5'-cyclic AMP

enzyme: cAMP deaminase

substrate: 3',5'-cyclic AMP


enzyme_display_name: 2,5-dihydroxypyridine 5,6-dioxygenase

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

verification_status: unverified

enzyme: 2,5-dihydroxypyridine 5,6-dioxygenase

status: unverified


enzyme_display_name: glutarate dioxygenase

organism: Escherichia coli (strain K12)

substrate_name: glutarate

enzyme: glutarate dioxygenase

substrate: glutarate


organism: Oryza sativa subsp. japonica


substrate_name: monacolin L acid

substrate: monacolin L acid


organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)


substrate_name: tryptophan

substrate: tryptophan


enzyme_display_name: (S)-nandinine synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: sulfite reductase (coenzyme F420)

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

substrate_name: sulfite


enzyme_display_name: columbamine O-methyltransferase

organism: Coptis japonica

substrate_name: columbamine

enzyme: columbamine O-methyltransferase

substrate: columbamine


enzyme_display_name: jasmonate O-methyltransferase

organism: Arabidopsis thaliana

substrate_name: methyl jasmonate

substrate: methyl jasmonate


enzyme_display_name: 3-oxoadipate CoA-transferase

organism: Pseudomonas knackmussii (strain DSM 6978 / CCUG 54928 / LMG 23759 / B13)

enzyme: 3-oxoadipate CoA-transferase


enzyme_display_name: 3-O-acetylpapaveroxine carboxylesterase

organism: Papaver somniferum

enzyme: 3-O-acetylpapaveroxine carboxylesterase


organism: Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)

substrate_name: cAMP

substrate: cAMP


organism: Pseudomonas knackmussii

substrate_name: succinyl-CoA

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

substrate: succinyl-CoA


organism: Pseudomonas sp.

substrate_name: Succinyl-CoA; 3-Oxoadipate

substrate: Succinyl-CoA; 3-Oxoadipate


substrate_name: 3-O-Acetylpapaveroxine; H2O

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

substrate: 3-O-Acetylpapaveroxine; H2O


enzyme_display_name: [phosphatase 2A protein]-leucine-carboxy methyltransferase

organism: Homo sapiens


enzyme_display_name: [methyl-Co(III) methanol-specific corrinoid protein]:coenzyme M

organism: Methanosarcina barkeri


organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

substrate_name: dimethylamine

substrate: dimethylamine


enzyme_display_name: 3-oxoadipyl-CoA thiolase

enzyme: 3-oxoadipyl-CoA thiolase


organism: Gentiana triflora

substrate_name: delphinidin 3,5-di-O-glucoside

substrate: delphinidin 3,5-di-O-glucoside


enzyme_display_name: pyridinium-3,5-biscarboxylic acid mononucleotide synthase

organism: Lactiplantibacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)

substrate_name: nicotinic acid adenine dinucleotide

substrate: nicotinic acid adenine dinucleotide


enzyme_display_name: cysteine transaminase

organism: Rattus norvegicus

substrate_name: L-cysteine

enzyme: cysteine transaminase

substrate: L-cysteine


enzyme_display_name: 2-phospho-L-lactate guanylyltransferase

enzyme: 2-phospho-L-lactate guanylyltransferase


enzyme_display_name: molybdopterin adenylyltransferase

substrate_name: ATP for domain G

assay_conditions_summary: cofactor ATP

enzyme: molybdopterin adenylyltransferase

substrate: ATP for domain G


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

substrate_name: ATP

substrate: ATP


enzyme_display_name: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate

organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: uridine 5'-diphosphobacillosamine

substrate: uridine 5'-diphosphobacillosamine


organism: Pseudomonas putida

proof_lines: pH 8.0, 25°C, strict substrate specificity


enzyme_display_name: tryptophan N-monooxygenase

substrate_name: L-tryptophan

proof_lines: CYP79B2, pH and temperature not specified in the publication

substrate: L-tryptophan


organism: Sinapis alba


organism: Berberis wilsoniae

substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Eutrema japonicum

substrate_name: jasmonate

enzyme: jasmonate O-methyltransferase

substrate: jasmonate


organism: Fragaria x ananassa


organism: Sus scrofa

substrate_name: S-Adenosyl-L-methionine; [phosphatase 2A protein]-leucine

enzyme: [phosphatase 2A protein]-leucine-carboxy methyltransferase


substrate_name: Unknown

substrate: Unknown


substrate_name: CoA

substrate: CoA


enzyme_display_name: putrescine--2-oxoglutarate transaminase

organism: Escherichia coli

substrate_name: putrescine

enzyme: putrescine--2-oxoglutarate transaminase

substrate: putrescine


organism: Campylobacter jejuni

substrate_name: UDP-bacillosamine

enzyme: undecaprenyl phosphate N,N'-diacetylbacillosamine 1-phosphate

substrate: UDP-bacillosamine


enzyme_display_name: beta-galactosidase

organism: Thermomyces lanuginosus

substrate_name: beta-lactose

enzyme: beta-galactosidase

substrate: beta-lactose


organism: Thermotoga maritima

substrate_name: o-nitrophenyl-beta-D-galactoside

substrate: o-nitrophenyl-beta-D-galactoside


organism: Thermus aquaticus

substrate_name: lactose

proof_lines: calculated from glucose liberated from lactose

proof_lines: calculated from disappearance from lactose

substrate: lactose


organism: Thermus sp.

proof_lines: at 70°C and pH 6.5, using 4-nitrophenyl-beta-D-galactopyranoside as substrate


organism: Torulopsis sphaerica


organism: Trametes cinnabarina


organism: Treponema phagedenis

substrate_name: p-nitrophenyl-beta-D-galactoside

substrate: p-nitrophenyl-beta-D-galactoside


organism: uncultured soil bacterium

substrate_name: 2-nitrophenyl beta-D-galactopyranoside

proof_lines:
pH 7, 20°C
pH 7, 10°C
pH 7, 5°C

substrate: 2-nitrophenyl beta-D-galactopyranoside


organism: Vigna radiata

proof_lines:
beta-galactosidase I
beta-galactosidase II
beta-galactosidase III


organism: Wickerhamiella versatilis


organism: Xanthomonas phaseoli pv. manihotis

proof_lines: pH 7.0, 30°C, mutant E184A, glycohydrolase activity


enzyme_display_name: 7,8-dihydroneopterin oxygenase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 7,8-dihydroneopterin in the aldolase reaction

proof_lines: kcat is 0.0054 sec(-1) for the aldolase reaction with 7,8-dihydroneopterin as substrate. kcat is 0.006 sec(-1) for the aldolase reaction with 7,8-dihydromonapterin as substrate. kcat is 0.0015 sec(-1) for the epimerization of 7,8-dihydroneo

enzyme: 7,8-dihydroneopterin oxygenase


organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: 1-deoxypentalenic acid

proof_lines: kcat is 4.2 sec(-1) with 1-deoxypentalenic acid.

substrate: 1-deoxypentalenic acid


enzyme_display_name: ent-cassa-12,15-diene 11-hydroxylase

organism: Oryza sativa subsp. japonica

substrate_name: ent-cassadiene

proof_lines: kcat is 0.011 sec(-1) with ent-sandaracopimaradien as substrate. kcat is 0.009 sec(-1) with ent-pimaradiene as substrate. kcat is 0.015 sec(-1) with ent-isokaurene as substrate. kcat is 0.006 sec(-1) with ent-cassadiene as substrate. kcat i

enzyme: ent-cassa-12,15-diene 11-hydroxylase

substrate: ent-cassadiene


enzyme_display_name: (S)-nandinine synthase

organism: Argemone mexicana

proof_lines: kcat is 13.8 min(-1) for (S)-cheilanthifoline.

enzyme: (S)-nandinine synthase


substrate_name: a hybrid RNA/DNA substrate

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

substrate: a hybrid RNA/DNA substrate


organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

substrate_name: CDP-L-glutamine

substrate: CDP-L-glutamine


sequence_source: UniProtKB:P48982 direct lookup from the PMID 16844121 BgaX organism/enzyme anchor

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


enzyme_display_name: acyl-lysine deacylase

organism: Achromobacter pestifer

enzyme: acyl-lysine deacylase


organism: Papaver somniferum

substrate_name: (S)-1-Hydroxy-N-methylcanadine; O2; NADPH; H+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

substrate: (S)-1-Hydroxy-N-methylcanadine; O2; NADPH; H+


enzyme_display_name: emodin O-methyltransferase

organism: Aspergillus terreus

substrate_name: Emodin; S-Adenosyl-L-methionine

enzyme: emodin O-methyltransferase

substrate: Emodin; S-Adenosyl-L-methionine


organism: Aspergillus terreus (strain NIH 2624 / FGSC A1156)

substrate_name: emodin

assay_conditions_summary: pH 7

substrate: emodin


enzyme_display_name: sulfopyruvate decarboxylase

organism: Methanocaldococcus jannaschii

substrate_name: sulfopyruvate

enzyme: sulfopyruvate decarboxylase

substrate: sulfopyruvate


enzyme_display_name: deoxynucleotide 3'-phosphatase

organism: Rattus norvegicus

substrate_name: deoxythymidine 5'-phosphate

enzyme: deoxynucleotide 3'-phosphatase

substrate: deoxythymidine 5'-phosphate


organism: Paenarthrobacter nicotinovorans

sequence_source: UniProtKB/Swiss-Prot Q93NG6 FASTA; reviewed entry DHPON_PAENI; PMID 16321959 evidence

assay_conditions_summary: pH 7.5; buffer 75 mM phosphate

proof_lines: in 75 mM phosphate buffer, pH 7.5, temperature not specified in the publication


enzyme_display_name: maleamate amidohydrolase

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

substrate_name: Unknown

enzyme: maleamate amidohydrolase

substrate: Unknown


organism: Bacteriophage T4

substrate_name: Deoxythymidine 3'-phosphate; H2O

substrate: Deoxythymidine 3'-phosphate; H2O


organism: Bordetella bronchiseptica

substrate_name: Maleamate

substrate: Maleamate


organism: Pseudomonas putida

substrate_name: H2O; Maleamate

substrate: H2O; Maleamate


organism: Arthrobacter nicotinovorans

substrate_name: 2,6-Dihydroxypseudooxynicotine; H2O

substrate: 2,6-Dihydroxypseudooxynicotine; H2O


enzyme_display_name: linoleate 10R-lipoxygenase

organism: Aspergillus fumigatus

substrate_name: O2; Linoleate

proof_lines: pH and temperature not specified in the publication

enzyme: linoleate 10R-lipoxygenase

substrate: O2; Linoleate


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


enzyme_display_name: glycine betaine--corrinoid protein Co-methyltransferase

organism: Desulfitobacterium hafniense

substrate_name: glycine betaine

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

substrate: glycine betaine


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

substrate_name: linoleic acid

smiles: CCCCC/C=C\C/C=C\CCCCCCCC(=O)O

substrate: linoleic acid


organism: Desulfitobacterium hafniense (strain Y51)

enzyme: glycine betaine--corrinoid protein Co-methyltransferase


organism: Escherichia coli (strain K12)

substrate_name: UDP-glucose (for hydrolysis reaction)

proof_lines: kcat is 0.013 sec(-1) for UDP-glucose hydrolysis.

substrate: UDP-glucose (for hydrolysis reaction)


organism: Escherichia coli

substrate_name: UDPglucose; Lipopolysaccharide

substrate: UDPglucose; Lipopolysaccharide


enzyme_display_name: homogentisate geranylgeranyltransferase

organism: Hordeum vulgare

enzyme: homogentisate geranylgeranyltransferase


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: glucosinolate gamma-glutamyl hydrolase

organism: Arabidopsis thaliana

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

enzyme: glucosinolate gamma-glutamyl hydrolase


substrate_name: phenylacetohydroximoyl-glutathione

substrate: phenylacetohydroximoyl-glutathione


enzyme_display_name: coagulation factor IXa

organism: Homo sapiens

substrate_name: Factor X

enzyme: coagulation factor IXa

substrate: Factor X


organism: Bos taurus

proof_lines: factor IXabeta, 0.1 mg/ml phospholipids, factor VIIIa in activating mixture

proof_lines: factor IXabeta, 0.1 mg/ml phospholipids in activating mixture

proof_lines: Gla-domainless factor IXabeta in activating mixture


proof_lines: pH 7.4, 22°C, recombinant mutant N129A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant N129A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: mutant enzyme N129A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutants N129A and K132A, each in the intrinsic tenase complex, in absence of ethylene glycol


proof_lines: pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant R165A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: mutant enzyme R165A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant N178A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: mutant enzyme N178A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant K132A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: mutant enzyme K132A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in presence of 30% ethylene glycol

proof_lines: pH 7.4, 22°C, recombinant mutant K126A the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: mutant enzyme K126A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: mutant Y94F/K98T/Y177F/I213V/E219, FX activation in presence of FVIIIa

proof_lines: mutant Y94F/K98T/Y177F/I213V/E219, FX activation in absence of FVIIIa


proof_lines: mutant Y94F/K98T, FX activation in presence of FVIIIa

proof_lines: mutant Y94F/K98T, FX activation in absence of FVIIIa


proof_lines: mutant Y94F/K98T/Y177F, FX activation in absence of FVIIIa

proof_lines: mutant Y94F/K98T/Y177F, FX activation in presence of FVIIIa


substrate_name: Factor X; H2O

proof_lines: in the presence of 0.1 mM phospholipid and 5 mM Ca2+

proof_lines: plasma-derived FIXa, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

proof_lines: plasma-derived FIXa, 5 units/ml FVIIIa and extruded phosphatidylcholine-phosphatidylserine phospholipid vesicles supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

substrate: Factor X; H2O


proof_lines: mutant enzyme rFIXa107A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

proof_lines: mutant enzyme rFIXa105A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C

proof_lines: mutant enzyme rFIXa91A, 5 units/ml FVIIIa and SFLLRN-activated platelets supplemented with bovine serum albumine (2 mg/ml) and 5 mM CaCl2, at 37 °C


proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, in presence of 0.2 M NaCl

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, in absence of NaCl

proof_lines: wild type enzyme FIXa, in presence of 200 mM Na+


proof_lines: mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in presence of FVIIIa

proof_lines: mutant Y94F/A95aK/K98T/Y177F/I213V/E219G, FX activation in absence of FVIIIa


assay_conditions_summary: pH 7.5; 295.15 K; buffer containing 0

proof_lines: wild type enzyme, in 0.02 M Tris-HCl (pH 7.5) buffer containing 0.1 M NaCl, 0.1 mg/ml bovine serum albumin, 33% ethylene glycol, and 5 mM Ca2+, at 22°C

proof_lines: pH 7.4, 22°C, recombinant wild-type enzyme the intrinsic tenase complex, in absence of ethylene glycol

proof_lines: wild type FIXa, FX activation in presence of FVIIIa


proof_lines: FIXa/FXa chimera in which the 39-loop of the protease is replaced with the corresponding loop of FXa, in TBS containing 0.1 mg/ml bovine serum albumin, 0.1% polyethylene glycol (PEG) 8000, and 5 mM Ca2+, at 22°C, pH not specified in the pub

proof_lines: in the presence of factor VIIIa, pH and temperature not specified in the publication

proof_lines: chimera enzyme FIXaN, in the presence of SFLLRN-activated platelets


proof_lines: mutant enzyme R233A, using factor X as substrate, at pH 7.4, 22°C


proof_lines: mutant enzyme R170A, using factor X as substrate, at pH 7.4, 22°C


proof_lines:
variant protein factor IXaCH
variant protein factor IXaAL


proof_lines: mutant enzyme E410A, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410A, in the presence of factor VIIIa, at pH 7.4 and 37°C


proof_lines: mutant enzyme E410L, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410L, in the presence of factor VIIIa, at pH 7.4 and 37°C


proof_lines: mutant enzyme E410N, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410N, in the presence of factor VIIIa, at pH 7.4 and 37°C


proof_lines: mutant enzyme E410H, in the absence of factor VIIIa, at pH 7.4 and 37°C

proof_lines: mutant enzyme E410H, in the presence of factor VIIIa, at pH 7.4 and 37°C


enzyme_display_name: plasmepsin II

organism: Unknown

enzyme: plasmepsin II


organism: Plasmodium falciparum

proof_lines: pH 4.5, temperature not specified in the publication


proof_lines:
pH 4.4, 37°C
autoactivated enzyme
pH 4.7


proof_lines: F244E mutant enzyme expressed by a system that bypasses the need for autoactivation


proof_lines: delF241 mutant enzyme expressed by a system that bypasses the need for autoactivation


proof_lines: F244A mutant enzyme expressed by a system that bypasses the need for autoactivation


proof_lines: F244K mutant enzyme expressed by a system that bypasses the need for autoactivation


assay_conditions_summary: pH 5

proof_lines: wild-type PMII, pH 5, temperature not specified in the publication


enzyme_display_name: matriptase

proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant L785S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant L785S

enzyme: matriptase


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant A757S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S


proof_lines: above, pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant E712Y/A757S/L785S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y/A757S/L785S


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant A757S/L785S

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant A757S/L785S


substrate_name: RQLRVVGG

assay_conditions_summary: pH 8; 310.15 K; buffer Tris saline

proof_lines: matriptase-2 in conditioned medium of HEK-MT2 cells, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

proof_lines: purified matriptase-2, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

proof_lines: recombinant human matriptase, in Tris saline buffer (50 mM Tris, 150 mM NaCl, pH 8.0) at 37°C

substrate: RQLRVVGG


organism: Mus musculus

substrate_name: Suc-Ala-Ala-Pro-Arg-p-nitroanilide

substrate: Suc-Ala-Ala-Pro-Arg-p-nitroanilide


organism: Rattus norvegicus

substrate_name: single-chain urokinase-type plasminogen activator

proof_lines: catalytic domain, Asp603 - Val855, after treatment with enteropeptidase

proof_lines: full-length rat matriptase with Myc-epitope-hexahistidine tag at its carboxyl-terminus

proof_lines: pseudozymogen His6t-S-CD consisting of a spacer and the catalytical domain with an N-terminal His6-tag and a cleavage site for activation by enterokinase is used


proof_lines: construct consisting of the catalytic domain of matriptase bearing a N772Q mutation fused to Myc-epitope-hexahistidine tag at its carboxyl-terminus treated with recombinant enterokinase


proof_lines: engineered L-matriptase (secreted variant of matriptase activated by recombinant enterokinase)


substrate_name: Ile-Pro-Arg-p-nitroanilide

substrate: Ile-Pro-Arg-p-nitroanilide


proof_lines: at pH 8.0, temperature not specified in the publication


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

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


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant H665F

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant H665F


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged wild-type enzyme

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged wild-type enzyme


proof_lines: pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant


proof_lines: above, pH and temperature not specified in the publication, recombinant c-Myc-tagged mutant E712Y

proof_lines: pH 8.0, 37°C, recombinant c-Myc-tagged mutant E712Y


enzyme_display_name: thrombin

substrate_name: GLVPRGVNL

assay_conditions_summary: pH 7.4; 298.15 K; buffer 10 mM imidazole

proof_lines:
pH 7.4, 25°C
alpha-thrombin
beta-thrombin

enzyme: thrombin

substrate: GLVPRGVNL


substrate_name: H2O; Sar-Pro-Arg p-nitroanilide dihydrochloride

assay_conditions_summary: pH 7.5; 298.15 K; buffer and 0

proof_lines:
pH 7.5, 25°C
pH 8.0, 25°C, absence of Na+
0.15 M KCl


proof_lines: mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C

proof_lines: mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C

proof_lines: mutant enzyme E217C/K224C, in Tris-HCl (pH 7.5) with 1.0 M NaCl and dithiothreitol, at 22°C


proof_lines: mutant enzyme R67C/I82C, in Tris-HCl (pH 7.5) with 0.2 M NaCl, at 22°C

proof_lines: mutant enzyme R67C/I82C, in Tris-HCl (pH 7.5) with 0.2 M choline chloride, at 22°C


proof_lines: mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride

proof_lines: mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl

proof_lines: mutant enzyme N143P, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mN NaCl


proof_lines: wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM choline chloride

proof_lines: wild type enzyme, in 5 mM Tris, 0.1% (w/v) PEG 8000, pH 8.0, 25°C, 200 mM NaCl


substrate_name: fibrinogen

proof_lines: pH 7.0, 25°C, Kcat/KM values for diverse recombinant thrombin mutants, overview

substrate: fibrinogen


substrate_name: protein C

substrate: protein C


substrate_name: spectrozyme-TH

proof_lines: mutant K222D, pH 8.0, 25°C, absence of Na+

proof_lines: mutant K222D, pH 8.0, 25°C, presence of 0.2 M Na+

substrate: spectrozyme-TH


proof_lines: wild-type, pH 8.0, 25°C, presence of 0.2 M Na+


substrate_name: p-Tosyl-L-arginine methyl ester; H2O

substrate: p-Tosyl-L-arginine methyl ester; H2O


substrate_name: Coagulation Factor XIII; H2O

proof_lines: 37°C, pH not specified in the publication, plasma-derived human thrombin FII

proof_lines: 37°C, pH not specified in the publication, recombinant human thrombin FII

substrate: Coagulation Factor XIII; H2O


substrate_name: Fibrinopeptide A

mutation_type: deletion

substrate: Fibrinopeptide A


substrate_name: PAR1 peptide

substrate: PAR1 peptide


enzyme_display_name: aspartate kinase

substrate_name: ATP; L-Aspartate

enzyme: aspartate kinase

substrate: ATP; L-Aspartate


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


substrate_name: L-Aspartate

substrate: L-Aspartate


substrate_name: L-Malate

substrate: L-Malate


proof_lines: AK2, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana


organism: Daucus carota


proof_lines: 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana


proof_lines: AK3, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana


organism: Pseudomonas stutzeri


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Methanocaldococcus jannaschii

substrate_name: L-aspartate

proof_lines:
at 37°C
at 70°C
Raw SKiD Env: Temp=37°C, pH=-----

substrate: L-aspartate


organism: Thermus thermophilus


assay_conditions_summary: pH 7.5; 333.15 K; cofactor ATP


substrate_name: L-Aspartate; ATP

substrate: L-Aspartate; ATP


organism: Streptomyces noursei

proof_lines: mutant M68V, recombinant enzyme purified to homogeneity


proof_lines: wild-type, recombinant enzyme purified to homogeneity


organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 328.15 K; cofactor ATP


enzyme_display_name: trypanothione-disulfide reductase

organism: Leishmania donovani

substrate_name: trypanothione disulfide

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

enzyme: trypanothione-disulfide reductase

substrate: trypanothione disulfide


organism: Leishmania infantum

proof_lines: in the presence of 0.01 mM 4-((1-(4-ethylphenyl)-2-methyl-5-(4-(methylthio)phenyl)-1H-pyrrol-3-yl)methyl)thiomorpholine, at 20°C, pH not specified in the publication

proof_lines: in the absence of 4-((1-(4-ethylphenyl)-2-methyl-5-(4-(methylthio)phenyl)-1H-pyrrol-3-yl)methyl)thiomorpholine, at 20°C, pH not specified in the publication

proof_lines: in the presence of 0.03 mM 4-((1-(4-ethylphenyl)-2-methyl-5-(4-(methylthio)phenyl)-1H-pyrrol-3-yl)methyl)thiomorpholine, at 20°C, pH not specified in the publication


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


proof_lines: mutant enzyme W81A, pH and temperature not specified in the publication


organism: Aspergillus japonicus

substrate_name: myo-inositol hexakisphosphate

proof_lines:
phytic acid sodium salt
phytic acid dipotassium salt

substrate: myo-inositol hexakisphosphate


organism: Aspergillus niger


organism: Bacillus sp. (in: firmicutes)


organism: Bacillus subtilis


proof_lines: mutant enzyme E436A, pH and temperature not specified in the publication


proof_lines: mutant enzyme Q439A, pH and temperature not specified in the publication


organism: Trypanosoma brucei

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines:
in 40 mM HEPES, pH 7.4, 1 mM EDTA
Raw SKiD Env: Temp=-----, pH=7.4


organism: Trypanosoma congolense

substrate_name: H+; NADPH; Oxidized trypanothione

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; Oxidized trypanothione


organism: Burkholderia sp. a13(2014)


organism: Citrobacter amalonaticus

assay_conditions_summary: pH 4.5; 310.15 K; buffer sodium acetate

proof_lines: recombinant enzyme, in 0.1 M sodium acetate buffer (pH 4.5) at 37°C


organism: Debaryomyces castellii

proof_lines:
native protein
recombinant protein
Raw SKiD Env: Temp=-----, pH=-----


organism: Trypanosoma cruzi

substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: ADP-specific phosphofructokinase

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 6.5; 313.15 K; cofactor ADP

proof_lines:
pH 6.5, 40°C
pH 6.5, 50°C
Raw SKiD Env: Temp=40°C, pH=6.5

enzyme: ADP-specific phosphofructokinase

substrate: D-fructose 6-phosphate


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


organism: Methanosarcina mazei

substrate_name: ADP

substrate: ADP


proof_lines:
pH 6.5, 40°C
MgADP, pH 6.5, 40°C


organism: Pyrococcus horikoshii

assay_conditions_summary: 323.15 K; cofactor ADP


organism: Methanococcus maripaludis

assay_conditions_summary: pH 6.5; 303.15 K; cofactor ADP


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


substrate_name: D-glucose

substrate: D-glucose


proof_lines: pH 6.5, 30°C, phosphopfructokinase activity

proof_lines: pH 7.8, 30°C, reverse glucokinase reaction


organism: Methanococcoides burtonii

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ADP


substrate_name: D-fructose 1,6-bisphosphate

substrate: D-fructose 1,6-bisphosphate


organism: Methanohalobium evestigatum

substrate_name: ADP; D-fructose 6-phosphate

substrate: ADP; D-fructose 6-phosphate


enzyme_display_name: D-xylose reductase (NADPH)

organism: Saccharomyces cerevisiae

substrate_name: D-xylose

assay_conditions_summary: pH 5; 303.15 K; cofactor NADPH

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

enzyme: D-xylose reductase (NADPH)

substrate: D-xylose


organism: Scheffersomyces stipitis

substrate_name: D-Xylose

substrate: D-Xylose


assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

proof_lines: with NADH, with 150 mM NaCl, pH 8.0, 30°C


organism: Yamadazyma tenuis

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme N309D, 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 N309D, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the proportion of open-chain free aldehyde in aqueous solution of xylose

proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme D50A, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose

substrate: NADPH


proof_lines: pH 7.0, 25°C, cofactor: NADH, mutant enzyme W23Y, kcat/Km value is corrected for the 0.02% of open-chain free aldehyde in aqueous solution of xylose


organism: Zymomonas mobilis subsp. mobilis

substrate_name: benzaldehyde

proof_lines: pH 7.2, temperature not specified in the publication

substrate: benzaldehyde


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


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


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


organism: Thermococcus kodakarensis

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

assay_conditions_summary: pH 7.5; 323.15 K; cofactor 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


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

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


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


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


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


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

substrate_name: Unknown

substrate: Unknown


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

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

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

substrate: recombinant bikunin


organism: Alteromonas sp

substrate_name: diisopropylfluorophosphate

substrate: diisopropylfluorophosphate


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


organism: Unknown

substrate_name: trypanothione disulfide

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


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


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

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


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


enzyme_display_name: trypanothione-disulfide reductase

organism: Lunaria biennis

substrate_name: Unknown

enzyme: trypanothione-disulfide reductase

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

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.


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


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

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