organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 6; 303.15 K; cofactor NAD+

proof_lines:
recombinant full-length enzyme
pH 6.0, 30°C, in presence of exosin
pH 6.0, 30°C, in absence of exosin


enzyme_display_name: NAD(+) ADP-ribosyltransferase

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: deletion

enzyme: NAD(+) ADP-ribosyltransferase

source: brenda


kcat_display: Not reported

mutation_type: substitution


organism: Rattus norvegicus

substrate_name: NAD+

km_display: Not reported

assay_conditions_summary: cofactor NAD+

substrate: NAD+


mutation_signature: Unknown

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


proof_lines: hydrolysis of NAD+, mutant enzyme Q187A/189A


enzyme_display_name: chitin synthase

organism: Neurospora crassa

substrate_name: Unknown

ki_unit: mM

enzyme: chitin synthase

substrate: Unknown


organism: Phascolomyces articulosus


organism: Phycomyces blakesleeanus

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Rhizopus arrhizus

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Saccharomyces cerevisiae


organism: Umbelopsis vinacea


enzyme_display_name: maltose phosphorylase

organism: Bacillus sp. AHU2001

substrate_name: D-glucose

enzyme: maltose phosphorylase

substrate: D-glucose


organism: Emticicia oligotrophica

substrate_name: maltose

proof_lines: pH 7.5, temperature not specified in the publication

substrate: maltose


organism: Levilactobacillus brevis

substrate_name: arsenate

substrate: arsenate


organism: Propionibacterium freudenreichii


organism: Bacillus cereus

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NAD+

proof_lines:
pH 7.3, 37°C, cosubstrate RhoA
pH 7.3, 37°C, cosubstrate RhoC
pH 7.3, 37°C, cosubstrate RhoB


organism: Saccharolobus solfataricus


enzyme_display_name: peptidoglycan glycosyltransferase

organism: Escherichia coli

protein_accession_database: UniProt

sequence_source: UniProtKB:P02919 reconstructed K287A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed K287A and applied mutation signature K287A to reconstruct the assayed variant sequence.

enzyme: peptidoglycan glycosyltransferase


sequence_source: UniProtKB:P02919 reconstructed N312A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed N312A and applied mutation signature N312A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P02919 reconstructed D234N

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed D234N and applied mutation signature D234N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P02919 reconstructed R372A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed R372A and applied mutation signature R372A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P02919 reconstructed G242A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed G242A and applied mutation signature G242A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P02919 reconstructed S266A

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed S266A and applied mutation signature S266A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P02919 reconstructed E290Q

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed E290Q and applied mutation signature E290Q to reconstruct the assayed variant sequence.


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


sequence_source: UniProtKB:P02919 reconstructed H240Q

sequence_variant_note: Resolved canonical sequence from UniProtKB:P02919 reconstructed H240Q and applied mutation signature H240Q to reconstruct the assayed variant sequence.


substrate_name: lipid I-meso-DAP

sequence_source: UniProtKB:P02919 protein identity context only

proof_lines:
at pH 8.5 and 30°C
lipid II, pH 7.5, 25°C

substrate: lipid I-meso-DAP


organism: Staphylococcus aureus


enzyme_display_name: thiamine pyridinylase

organism: Cheilanthes sieberi

substrate_name: nicotinic acid

proof_lines: lower maximal activity than pyridine and nicotinic acid

enzyme: thiamine pyridinylase

substrate: nicotinic acid


organism: Clostridium botulinum

substrate_name: thiamine

substrate: thiamine


substrate_name: pyridoxine

substrate: pyridoxine


organism: Corallococcus sp. EGB

proof_lines: pH 7.2, 37°C, cosubstrate: 4-nitrothiophenol


organism: Marsilea drummondii

substrate_name: beta-picoline

proof_lines: measured in Pi-Tris and Pi-diphosphate, the same as for thiamine diphosphate

substrate: beta-picoline


organism: Paenibacillus thiaminolyticus

proof_lines: pH 7.2, temperature not specified in the publication

proof_lines: pH 5.8, 25°C, the enzyme does not follow strict Michaelis-Menten kinetics


enzyme_display_name: kappa-carrageenase

organism: Zobellia galactanivorans

substrate_name: kappa-carrageen

enzyme: kappa-carrageenase

substrate: kappa-carrageen


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Zobellia sp. M-2


organism: Pseudoalteromonas carrageenovora


substrate_name: kappa-carrageenan

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

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda skid

substrate: kappa-carrageenan


organism: Pseudoalteromonas tetraodonis


organism: Wenyingzhuangia aestuarii


organism: Wenyingzhuangia fucanilytica

substrate_name: furcellaran

substrate: furcellaran


enzyme_display_name: alpha-glucuronidase

organism: Aspergillus niger

proof_lines:
enzyme form CM-I
enzyme form CM-II

enzyme: alpha-glucuronidase


organism: Aspergillus tubingensis


organism: Aureobasidium pullulans


organism: Bacteroides sp.


organism: Cellvibrio japonicus

substrate_name: aldotriouronic acid

substrate: aldotriouronic acid


enzyme_display_name: NAD(+) glycohydrolase

organism: Sus scrofa

enzyme: NAD(+) glycohydrolase


enzyme_display_name: D-Ala-D-Ala dipeptidase

organism: Enterococcus faecalis

substrate_name: D-Ala-D-Ala

enzyme: D-Ala-D-Ala dipeptidase

substrate: D-Ala-D-Ala


organism: Enterococcus faecium

proof_lines: maltose-binding protein fusion enzyme, Co2+-form, pH 8.0, 37°C


organism: Enterococcus gallinarum


organism: Enterococcus sp.


proof_lines: pH 8.0, 37°C, recombinant mutant C78S/C157S


proof_lines: pH 8.0, 37°C, recombinant mutant D145A/E146A


proof_lines: pH 8.0, 37°C, recombinant mutant H149A/H150A


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


enzyme_display_name: lysophospholipase

organism: Caldibacillus thermoamylovorans

substrate_name: 4-nitrophenyl palmitate

enzyme: lysophospholipase

substrate: 4-nitrophenyl palmitate


organism: Candida albicans


organism: Cryptococcus neoformans


organism: Hordeum vulgare


organism: Mus musculus

substrate_name: lysophosphatidylcholine

proof_lines: substrate concentration between 0.015-0.2 mM

substrate: lysophosphatidylcholine


organism: Mycobacterium lepraemurium


organism: Penicillium chrysogenum


organism: Pseudomonas aeruginosa


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


proof_lines:
Vmax: 90.9 micromol/h/mg protein
Vmax: 0.113 micromol/h/mg protein
Vmax: 122.7 micromol/h/mg protein


enzyme_display_name: cyclic-di-AMP phosphodiesterase

organism: Staphylococcus aureus

substrate_name: Unknown

proof_lines: pH 8.5, temperature not specified in the publication

enzyme: cyclic-di-AMP phosphodiesterase

substrate: Unknown


enzyme_display_name: unsaturated chondroitin disaccharide hydrolase

organism: Streptococcus agalactiae


enzyme: unsaturated chondroitin disaccharide hydrolase


organism: Bacteria


organism: Cytophaga sp.


organism: Streptococcus pyogenes

substrate_name: NAD+

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

proof_lines: enzyme variant SPNJ4 mutant R289K/D330G, pH 7.4, 37°C

substrate: NAD+


proof_lines: enzyme variant SPNJ4 mutant D330G/I374V, pH 7.4, 37°C


proof_lines: enzyme variant SPNJ4 mutant R289N/D330G, pH 7.4, 37°C


proof_lines: enzyme variant SPNJ4 mutant D330G, pH 7.4, 37°C


proof_lines: enzyme variant SPNJ4 mutant R289K, pH 7.4, 37°C


enzyme_display_name: HtrA2 peptidase

substrate_name: SPMFKGV-para-nitroaniline

enzyme: HtrA2 peptidase

substrate: SPMFKGV-para-nitroaniline


substrate_name: oligomeric alpha-synuclein

substrate: oligomeric alpha-synuclein


enzyme_display_name: mitochondrial processing peptidase

organism: Bos taurus

substrate_name: ARAARAARAFTSSA

enzyme: mitochondrial processing peptidase

substrate: ARAARAARAFTSSA


enzyme_display_name: proteasome endopeptidase complex

organism: Struthio camelus

enzyme: proteasome endopeptidase complex


enzyme_display_name: N-carbamoyl-D-amino-acid hydrolase

organism: Agrobacterium sp.

substrate_name: N-carbamoyl-D-p-hydroxyphenylglycine

enzyme: N-carbamoyl-D-amino-acid hydrolase

substrate: N-carbamoyl-D-p-hydroxyphenylglycine


organism: Agrobacterium tumefaciens

substrate_name: N-Carbamoyl-D-phenylglycine

substrate: N-Carbamoyl-D-phenylglycine


proof_lines: pH 7.0, 40°C, mutant enzyme M184L, T262A


proof_lines: pH 7.0, 40°C, mutant enzyme Q23L/V40A/H58Y/G75S/M184L/T262A

proof_lines: pH 7.0, 40°C,mutant enzyme Q23L/V40A/H58Y/G75S/M184L/T262A


proof_lines:
65°C, pH 7.0, wild-type enzyme
37°C, pH 7.0, wild-type enzyme
pH 7.0, 40°C, wild-type enzyme


proof_lines:
65°C, pH 7.0, mutant enzyme P295C/F304C
37°C, pH 7.0, mutant enzyme P295C/F304C
55°C, pH 7.0, mutant enzyme P295C/F304C


proof_lines:
37°C, pH 7.0, mutant enzyme A302C
55°C, pH 7.0, mutant enzyme A302C
65°C, pH 7.0, mutant enzyme A302C


organism: Cellvibrio japonicus


organism: Geobacillus stearothermophilus

substrate_name: aldotetraouronic acid

substrate: aldotetraouronic acid


organism: Helix pomatia


organism: Scheffersomyces stipitis


organism: Thermoanaerobacterium saccharolyticum


organism: Thermoascus aurantiacus


organism: Thermotoga maritima


organism: Trichoderma reesei


organism: Clostridium perfringens


organism: Streptococcus agalactiae


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


enzyme_display_name: 2-oxoaldehyde dehydrogenase (NAD(+))

organism: Unknown

enzyme: 2-oxoaldehyde dehydrogenase (NAD(+))


enzyme_display_name: heptaprenyl diphosphate synthase

organism: Bacillus subtilis

substrate_name: isopentenyl diphosphate

enzyme: heptaprenyl diphosphate synthase

substrate: isopentenyl diphosphate


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

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


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


organism: Staphylococcus aureus

proof_lines: pH and temperature not specified in the publication


substrate_name: Isopentenyl diphosphate; trans,trans-Farnesyl diphosphate

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


proof_lines: pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-II(A79F)

proof_lines: pH 8.5, 37°C, mutant enzyme subunit-I(wild-type)/subunit-B(A79F)


organism: Candida albicans

substrate_name: pyruvate

substrate: pyruvate


organism: Arabidopsis thaliana

substrate_name: GDP-beta-L-fucose

proof_lines: mutant enzyme S253A, 10 mM MnCl2, 50 mM MES buffer, pH 6.5, at 30°C

substrate: GDP-beta-L-fucose


substrate_name: GDP-L-Fuc

substrate: GDP-L-Fuc


organism: Helicobacter pylori

substrate_name: LacNAc

proof_lines: deletion mutant FTdelta28 with 28 residues deleted from the C-terminus

substrate: LacNAc


proof_lines: deletion mutant FTdelta66 with 66 residues deleted from the C-terminus


substrate_name: GDP-fucose (at pH 6.0 and 30 degrees Celsius)

source_db: uniprot

source: uniprot


organism: Caenorhabditis elegans

substrate_name: GDP-fucose (at pH 7.5 and 23 degrees Celsius)


proof_lines: mutant enzyme Y243A, 10 mM MnCl2, 50 mM MES buffer, pH 6.5, at 30°C


proof_lines: wild type enzyme, 10 mM MnCl2, 50 mM MES buffer, pH 6.5, at 30°C


proof_lines: mutant enzyme N219A, 10 mM MnCl2, 50 mM MES buffer, pH 6.5, at 30°C


proof_lines: mutant enzyme T339A, 10 mM MnCl2, 50 mM MES buffer, pH 6.5, at 30°C


enzyme_display_name: phosphoribosyl 1,2-cyclic phosphate phosphodiesterase

organism: Escherichia coli

source_db: oed

source: oed


enzyme: phosphoribosyl 1,2-cyclic phosphate phosphodiesterase


substrate_name: bis(p-nitrophenyl)phosphate

proof_lines: mutant D164A, pH 7.1, 25°C, presence of Mn2+

substrate: bis(p-nitrophenyl)phosphate


proof_lines: deletion mutant FTdelta115 with 115 residues deleted from the C-terminus


proof_lines: deletion mutant FTdelta38 with 38 residues deleted from the C-terminus


proof_lines: deletion mutant FTdelta23 with 23 residues deleted from the C-terminus


proof_lines: deletion mutant FTdelta45 with 45 residues deleted from the C-terminus


substrate_name: NAD+


organism: Capra hircus

substrate_name: H2O; NAD+; Methylglyoxal

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

substrate: H2O; NAD+; Methylglyoxal


organism: Homo sapiens

substrate_name: 3-Deoxy-D-glucosone; NAD+; H2O

substrate: 3-Deoxy-D-glucosone; NAD+; H2O


organism: Oryctolagus cuniculus


organism: Ovis aries

assay_conditions_summary: pH 9.3; 298.15 K; cofactor NAD+

proof_lines: assay mixture containing 40 mM L-2-aminopropan-1-ol, 5 mM methylglyoxal and 10 mM potassium phosphate

proof_lines: assay mixture containing 40 mM L-2-aminopropan-1-ol, 5 mM methylglyoxal, no potassium phosphate

proof_lines: amine as activator in aldehyde oxidation


organism: Pseudomonas putida

substrate: NAD+


organism: Apis mellifera

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


substrate_name: dansyl-GnGn

sequence_source: UniProtKB reviewed Q9LJK1/FUT11_ARATH fetched by exact PMID 11420147 lookup

substrate: dansyl-GnGn


organism: Drosophila melanogaster

sequence_source: UniProtKB reviewed Q9VUL9/FUTA_DROME fetched by exact PMID 11382750 lookup

proof_lines: glycopeptide derived from IgG, FucTA gene


substrate_name: GDP-fucose

verification_status: unverified

substrate: GDP-fucose

status: unverified


substrate_name: N-acetyllactosamine

substrate: N-acetyllactosamine


proof_lines: deletion mutant FTdelta80 with 80 residues deleted from the C-terminus


enzyme_display_name: xylan alpha-1,2-glucuronosidase

organism: Amphibacillus xylanus

enzyme: xylan alpha-1,2-glucuronosidase


organism: Cellvibrio japonicus


organism: Paenibacillus curdlanolyticus

substrate_name: aldouronic acid

substrate: aldouronic acid


organism: Pseudothermotoga thermarum

proof_lines:
pH 6.5, 80°C
at pH 6.0 and 80°C


proof_lines: mutant H222A, pH 7.1, 25°C, presence of Mn2+


proof_lines: wild-type, pH 7.1, 25°C, presence of Mn2+


proof_lines: mutant D80A, pH 7.1, 25°C, presence of Mn2+


proof_lines: mutant H200A, pH 7.1, 25°C, presence of Mn2+


organism: Saccharophagus degradans

substrate_name: birchwood xylan

substrate: birchwood xylan


organism: Thermotoga maritima

proof_lines: pH 7.5, 85°C, recombinant His-tagged wild-type enzyme


proof_lines: mutant D187A, pH 7.1, 25°C, presence of Mn2+


proof_lines: mutant H78A, pH 7.1, 25°C, presence of Mn2+


proof_lines: mutant T75A, pH 7.1, 25°C, presence of Mn2+


proof_lines:
pH 7.2, 25°C, presence of Mn2+
pH 7.2, 25°C, presence of Zn2+
pH 7.2, 25°C, presence of Ni2+


substrate_name: thymidine 5'-monophosphate p-nitrophenyl ester


proof_lines: mutant D54A, pH 7.1, 25°C, presence of Mn2+


proof_lines: kcat is 1.92 min(-1) and 2.71 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.


proof_lines: kcat is 1.9 min(-1) and 2.0 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.


proof_lines: kcat is 2.1 min(-1) and 1.9 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.


proof_lines: kcat is 2.6 min(-1) and 3.0 min(-1) for 2-oxoglutarate and histone H3K4me3, respectively.


organism: Bos taurus

proof_lines:
enzyme from pituitary
enzyme from thymus
enzyme from spleen


proof_lines:
pH 7.8, 25°C
20S proteasome, pH 8.2, 37°C
pH 7.5, 25°C


organism: Patiria pectinifera


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae

substrate_name: Unknown

substrate: Unknown


organism: Blastobacter sp.

substrate_name: N-carbamoyl-D-Val

substrate: N-carbamoyl-D-Val


organism: Comamonas sp.


organism: Ralstonia pickettii

substrate_name: N-carbamoyl-D-p-hydroxyphenylglycine

substrate: N-carbamoyl-D-p-hydroxyphenylglycine


assay_conditions_summary: pH 7; 313.15 K; buffer 100 mM potassium phosphate

proof_lines: mutant enzyme Q12L/Q23L/Q207E/N242G/H248Q/T262A/T263S/E266D/T271I/A273P, in 100 mM potassium phosphate buffer (pH 7.0), at 40°C


proof_lines: CDase-M3, in 100 mM potassium phosphate buffer (pH 7.0), at 40°C


enzyme_display_name: N-carbamoyl-L-amino-acid hydrolase

organism: Achromobacter xylosoxidans

substrate_name: N-carbamoyl-L-isoleucine

enzyme: N-carbamoyl-L-amino-acid hydrolase

substrate: N-carbamoyl-L-isoleucine


organism: Homo sapiens

substrate_name: [histone H3 N-terminal 21mer mutant T6V] N6,N6,N6-trimethyl-L-lysine4

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


proof_lines: pH 8.5, 75°C, recombinant His-tagged mutant fusion enzyme


organism: Brevibacillus reuszeri

substrate_name: N-carbamoyl-L-methionine

substrate: N-carbamoyl-L-methionine


organism: Geobacillus stearothermophilus

substrate_name: N-acetyl-L-phenylalanine

substrate: N-acetyl-L-phenylalanine


organism: Paenarthrobacter aurescens


organism: Pseudomonas sp. ON4a


organism: Sinorhizobium meliloti

substrate_name: N-carbamoyl-L-tryptophan

proof_lines: determined at 40°C for 20 min at pH 8.0 after preincubation with 2 mM Ni2+

substrate: N-carbamoyl-L-tryptophan


enzyme_display_name: dynamin GTPase

substrate_name: GTP

enzyme: dynamin GTPase

substrate: GTP


enzyme_display_name: ubiquinol oxidase (non-electrogenic)

organism: Trypanosoma brucei brucei

proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme R118K

enzyme: ubiquinol oxidase (non-electrogenic)


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme T219A


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme L122A


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme E215N


organism: Sauromatum venosum

proof_lines: mutant Y299F, pH and temperature not specified in the publication


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


proof_lines: mutant Y253F, pH and temperature not specified in the publication


proof_lines: mutant T179A, pH and temperature not specified in the publication


proof_lines: mutant C172A, pH and temperature not specified in the publication


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme T219S


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme D100E


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme D100A


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme E215D


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme R96K


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


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme L212A


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme E215A


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme R96A


proof_lines: pH 7.4, temperature not specified in the publication, mutant enzyme R118A


enzyme_display_name: rosmarinate synthase

organism: Lavandula angustifolia

substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: with 3-(4-hydroxyphenyl)lactate, pH 7.5, 30°C, recombinant AAT1

proof_lines: with shikimate, pH 7.5, 30°C, recombinant AAT1

proof_lines: with caffeoyl-CoA, pH 7.5, 30°C, recombinant AAT1

enzyme: rosmarinate synthase

substrate: caffeoyl-CoA


enzyme_display_name: ribonuclease E

organism: Escherichia coli

substrate_name: 5'-triphosphorylated 9S RNA

mutation_signature: truncated RNase E

mutation_type: truncation

proof_lines: truncated RNase E, residues 1-517, in complex with RhlB, enolase, and PNPase, pH 7.5, 30°C

enzyme: ribonuclease E

substrate: 5'-triphosphorylated 9S RNA


proof_lines: N-terminal domain, residues 1-517, pH 7.5, 30°C

proof_lines: full-length RNase E in complex with RhlB, enolase, and PNPase, pH 7.5, 30°C


proof_lines: N-terminal domain, residues 1-517, with mutations D26N/D28N/D338N, pH 7.5, 30°C


enzyme_display_name: ribosylpyrimidine nucleosidase

organism: Arabidopsis thaliana

substrate_name: isopentenyladenine-riboside

proof_lines: recombinant enzyme expressed in Escherichia coli, in 50 mM Tris-HCl, pH 7.5, at 30°C

proof_lines: recombinant enzyme expressed in Saccharomyces cerevisiae, in 50 mM Tris-HCl, pH 7.5, at 30°C

enzyme: ribosylpyrimidine nucleosidase

substrate: isopentenyladenine-riboside


substrate_name: Inosine

assay_conditions_summary: pH 7.3; 310.15 K; buffer 50 mM HEPES

proof_lines: mutant enzyme Q227F, in 50 mM HEPES buffer (pH 7.3), at 37°C

substrate: Inosine


proof_lines: mutant enzyme T223F/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C


enzyme_display_name: formate dehydrogenase (NADP(+))

organism: Burkholderia stabilis

substrate_name: NAD+

assay_conditions_summary: pH 7; 303.15 K; buffer 1 M potassium phosphate; cofactor NADP+

proof_lines: wild type enzyme, in 1 M potassium phosphate buffer (pH 7.0), at 30°C

enzyme: formate dehydrogenase (NADP(+))

substrate: NAD+


substrate_name: NADP+

proof_lines: mutant enzyme Q223E, in 1 M potassium phosphate buffer (pH 7.0), at 30°C

substrate: NADP+


organism: Granulicella mallensis

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

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

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


enzyme_display_name: flavanone 7-O-beta-glucosyltransferase

organism: Astragalus membranaceus

substrate_name: Calycosin

enzyme: flavanone 7-O-beta-glucosyltransferase

substrate: Calycosin


organism: Unknown

substrate_name: formate

substrate: formate


organism: Glycine max

substrate_name: O(2) (in the presence of 0.025% N,N',N'-polyoxyethylene(l0)-N-tallow-1,3- diamino-propane)


organism: Neomoorella thermoacetica

substrate_name: formate (at 55 degrees Celsius and pH 7.5, with NADP as electron acceptor)


organism: Coleus scutellarioides

substrate_name: 4-coumaroyl-CoA (in the presence of 4-Hydroxyphenyllactate)

assay_conditions_summary: cofactor CoA


organism: Melissa officinalis

substrate_name: 4-coumaroyl-CoA (with 4-hydroxyphenyllactate as acceptor substrate)


enzyme_display_name: galactoside O-acetyltransferase

organism: Escherichia coli (strain K12)

substrate_name: acetyl-CoA

enzyme: galactoside O-acetyltransferase

substrate: acetyl-CoA


organism: Homo sapiens

substrate_name: 4-methylumbelliferone when assayed with UDP-glucose as the sugar donor


organism: Malus domestica

substrate_name: phloretin

substrate: phloretin


enzyme_display_name: kallikrein 8

substrate_name: Pro-Phe-Arg-MCA

enzyme: kallikrein 8

substrate: Pro-Phe-Arg-MCA


organism: Mus musculus

substrate_name: Boc-Val-Pro-Arg-MCA

substrate: Boc-Val-Pro-Arg-MCA


organism: Zea mays

substrate_name: apigenin

substrate: apigenin


substrate_name: uridine

assay_conditions_summary: pH 7.3; 310.15 K; buffer Q227Y in 50 mM HEPES

proof_lines: mutant enzyme Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C

substrate: uridine


assay_conditions_summary: pH 7.3; 310.15 K; buffer uridine/Inosine in 50 mM HEPES

proof_lines: wild type enzyme, in 50 mM HEPES buffer (pH 7.3), at 37°C


assay_conditions_summary: pH 7.3; 310.15 K; buffer Q227A in 50 mM HEPES

proof_lines: mutant enzyme Q227A, in 50 mM HEPES buffer (pH 7.3), at 37°C


substrate_name: 5'-phosphorylated fluorogenic substrate

proof_lines: kcat is 0.83 min(-1) for 5'-PO(4) substrate and 0.088 min(-1) for 5-OH substrate.

substrate: 5'-phosphorylated fluorogenic substrate


organism: Caenorhabditis elegans

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

assay_conditions_summary: pH 7

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


organism: Lycium barbarum

substrate_name: naringenin

substrate: naringenin


organism: Plagiochasma appendiculatum

substrate_name: quercetin

substrate: quercetin


substrate_name: luteolin

substrate: luteolin


organism: Escherichia coli

proof_lines: mutant enzyme T223Y, in 50 mM HEPES buffer (pH 7.3), at 37°C


substrate_name: Inosine

proof_lines: mutant enzyme T223A, in 50 mM HEPES buffer (pH 7.3), at 37°C


proof_lines: mutant enzyme T223F, in 50 mM HEPES buffer (pH 7.3), at 37°C


proof_lines: mutant enzyme T223Y/Q227Y, in 50 mM HEPES buffer (pH 7.3), at 37°C


organism: Escherichia coli K-12

substrate_name: cytidine

substrate: cytidine


organism: Leishmania braziliensis

substrate_name: adenosine

proof_lines: positive homotropic cooperativity, Hill coefficient value of 2.4, pH 7.5, 25°C

substrate: adenosine


organism: Saccharolobus solfataricus

proof_lines:
pH 7.4, 80°C
Raw SKiD Env: Temp=80°C, pH=7.4


organism: Arum italicum

proof_lines: in the presence of EDT-20 (0.025%) and pyruvate, 0.3 M succinate, 25 mM TES, 10 mM potassium phosphate, and 2 mM magnesium sulfate, pH 7.0, at 25°C


substrate_name: Unknown

substrate: Unknown


organism: Gluconobacter oxydans

proof_lines: at 25°C in 50 mM potassium phosphate (pH 6.5)


organism: Glycine max


organism: Moniliophthora perniciosa

proof_lines: pH 7.4, temperature not specified in the publication


organism: Arabidopsis thaliana

substrate_name: [histone H3]-N6,N6-dimethyl-L-lysine4

proof_lines: in 10% (v/v) glycerol, at pH 8.0 and 25°C

substrate: [histone H3]-N6,N6-dimethyl-L-lysine4


substrate_name: [acetylated histone H3 21mer]-N6,N6,N6-trimethyl-L-lysine4

proof_lines: in the absence of unmodified histone H3 10mer peptide, at pH 7.5 and 25°C

proof_lines: in the presence of 0.038 mM unmodified histone H3 10mer peptide, at pH 7.5 and 25°C


substrate_name: NADP+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

substrate: NADP+


organism: [Candida] boidinii


organism: Mycolicibacterium vaccae

assay_conditions_summary: pH 7; 295.15 K; cofactor NADP+

proof_lines: mutant C145S/A198G/D221Q/C255V, at pH 7.0 and 22°C


proof_lines: mutant C145S/D221Q/C255V, at pH 7.0 and 22°C


organism: Melissa officinalis

substrate_name: caffeoyl-CoA

sequence_source: NCBI protein CBW35684.1 / UniProt G0LD36 linked to PMID 21354582

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines: with 3-(3,4-dihydroxyphenyl)lactate, pH 7.0, 30°C, crude recombinant His-tagged enzyme

proof_lines: with 3-(4-hydroxyphenyl)lactate, pH 7.0, 30°C, crude recombinant His-tagged enzyme

proof_lines: with 3-(4-hydroxyphenyl)lactate, pH 7.0, 30°C, native crude enzyme

substrate: caffeoyl-CoA


proof_lines:
25°C, mutant Y83F
hexahistidine-tagged Y83F mutant


substrate_name: isopropyl-thio-beta-D-galactopyranoside

proof_lines:
hexahistidine-tagged Y83L mutant
25°C, mutant Y83L

substrate: isopropyl-thio-beta-D-galactopyranoside


substrate_name: p-nitrophenyl-beta-D-galactopyranoside

substrate: p-nitrophenyl-beta-D-galactopyranoside


proof_lines:
25°C, wild-type enzyme
hexahistidine-tagged wild type enzyme
wild type enzyme


proof_lines:
25°C, mutant Y83V
hexahistidine-tagged Y83V mutant


proof_lines:
acetyl donor: propionyl-CoA
acetyl donor: acetyl-CoA
acetyl donor: butyryl-CoA


organism: Citrus sinensis

substrate_name: diosmetin

proof_lines: pH 7.5, 30°C, with UDP-glucose, recombinant enzyme

substrate: diosmetin


organism: Citrus x paradisi


organism: Petunia x hybrida

proof_lines:
peak III
peak II
peak I


organism: Helicobacter pylori

substrate_name: N-acetyllactosamine

proof_lines:
FucT 45
FucT 115

substrate: N-acetyllactosamine


substrate_name: GDP-fucose

substrate: GDP-fucose


proof_lines: mutant C145S/D221A/C255V, at pH 7.0 and 22°C


proof_lines: mutant C145S/D221G/C255V, at pH 7.0 and 22°C


organism: Neomoorella thermoacetica

substrate_name: formate

assay_conditions_summary: cofactor NADP+

proof_lines:
cosubstrate methyl viologen
cosubstrate NADP+

substrate: formate


organism: Pseudomonas sp.


organism: Solanum tuberosum


organism: Coleus scutellarioides

proof_lines: pH 7.0, 30°C, with cinnamoyl-CoA, recombinant RAS

proof_lines: pH 7.0, 30°C, with feroyl-CoA, recombinant RAS


organism: Homo sapiens


organism: Mus musculus

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


proof_lines:
native enzyme, pH 8.0, 37°C
recombinant enzyme, pH 8.0, 37°C
complex formation, pH 7.4, 37°C


substrate_name: GTP

assay_conditions_summary: 295.15 K; cofactor ATP

proof_lines: 22°C, wild-type dynamin, lipid tubule stimulated GTPase activity

proof_lines: 37°C, wild-type dynamin, lipid tubule stimulated GTPase activity

proof_lines: 37°C, wild-type dynamin, basal GTPase activity

substrate: GTP


assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines: 37°C, S61D and T141A mutant dynamin, lipid tubule stimulated GTPase activity


proof_lines: 37°C, S61A mutant dynamin: lipid tubule stimulated GTPase activity, T65D mutant dynamin: basal GTPase activity


proof_lines: 37°C, T65H mutant dynamin, basal GTPase activity

proof_lines: 37°C, T65H mutant dynamin, lipid tubule stimulated GTPase activity


proof_lines: 37°C, T65D mutant dynamin, lipid tubule stimulated GTPase activity


proof_lines: 37°C, S61D mutant dynamin, lipid tubule stimulated GTPase activity

proof_lines: 37°C, S61D mutant dynamin, basal GTPase activity


proof_lines: 37°C, T141D mutant dynamin, lipid tubule stimulated GTPase activity

proof_lines: 37°C, T141D mutant dynamin, basal GTPase activity


proof_lines: 37°C, T65D and T65H mutant dynamin, basal GTPase activity

proof_lines: 37°C, T65D and T65H mutant dynamin, lipid tubule stimulated GTPase activity


proof_lines: 37°C, S61A mutant dynamin, lipid tubule stimulated GTPase activity

proof_lines: 37°C, S61A mutant dynamin, basal GTPase activity


assay_conditions_summary: 303.15 K; cofactor ATP

proof_lines: in 10 mM Tris-HCl, 10 mM NaCl, 2 mM Mg2+, at 30°C


organism: Rattus norvegicus

assay_conditions_summary: cofactor ATP

proof_lines:
in presence of microtubules
in absence of microtubules


enzyme_display_name: oxaloacetase

organism: Dianthus caryophyllus

enzyme: oxaloacetase


substrate_name: oxaloacetate

proof_lines:
mutant S257T, trial 1
mutant S257T, trial 2

substrate: oxaloacetate


organism: Streptantibioticus cattleyicolor


enzyme_display_name: aldehyde oxygenase (deformylating)

organism: Botryococcus braunii

substrate_name: octadecanal

enzyme: aldehyde oxygenase (deformylating)

substrate: octadecanal


organism: Lathyrus oleraceus


organism: Nostoc punctiforme


organism: Podiceps nigricollis


organism: Prochlorococcus marinus

substrate_name: n-octanal

proof_lines: pH and temperature not specified in the publication

substrate: n-octanal


enzyme_display_name: xylose isomerase

organism: Thermus aquaticus

substrate_name: D-arabinose

proof_lines: D-ribose D-glucose

enzyme: xylose isomerase

substrate: D-arabinose


organism: Geobacillus stearothermophilus

substrate_name: aldotetraouronic acid

substrate: aldotetraouronic acid


organism: uncultured bacterium

substrate_name: aldouronic acid

assay_conditions_summary: pH 6

proof_lines:
pH 6, 37Â°C
presence of Mg2+, pH 6, 37Â°C

substrate: aldouronic acid


organism: Arabidopsis thaliana

substrate_name: methyluridine

proof_lines: isoform NSH1, pH not specified in the publication, at 30°C

proof_lines: recombinant enzyme expressed in Escherichia coli

substrate: methyluridine


organism: Escherichia coli

substrate_name: uridine

substrate: uridine


organism: Leishmania donovani

substrate_name: purine ribonucleoside

substrate: purine ribonucleoside


organism: Pseudomonas fluorescens


organism: Homo sapiens

assay_conditions_summary: pH 8.5; 310.15 K; buffer note

proof_lines: in 100 mM sodium phosphate, 0.01% (v/v) Tween 20, pH 8.5, at 37°C


enzyme_display_name: mitochondrial processing peptidase

enzyme: mitochondrial processing peptidase


proof_lines:
pH 7.5, 25°C, mutant E75D
pH 7.5, 25°C, mutant E139Aand E75D


substrate_name: fetuin

substrate: fetuin


substrate_name: GDP-L-fucose

proof_lines: pH 6.5, recombinant FucT VI mutant L244A

substrate: GDP-L-fucose


proof_lines: pH 6.5, recombinant FucT VI mutant Y240A


proof_lines: pH 6.5, recombinant FucT VI mutants Y240A and L244A


proof_lines: pH 6.5, recombinant FucT VI mutant S249A


proof_lines: pH 6.5, recombinant FucT VI mutant F246A


organism: Lymnaea stagnalis


organism: Vigna radiata


proof_lines: in 25 mM bis-Tris-propane (pH 8.3), 15 mM MgCl2, 100 mM NaCl, 0.1% (v/v) Triton X-100, and 1 mM dithiothreitol

proof_lines: recombinant enzyme N-terminal half, pH 7.5, 30°C

proof_lines: pH 7.5, 25°C, recombinant N-terminal domain


organism: Bacteroides ovatus

substrate_name: birchwood xylan

assay_conditions_summary: pH 6.5; 310.15 K; buffer context but no UniProt id

proof_lines: in 50 mM sodium phosphate, 12 mM citrate buffer, pH 6.5, at 37°C

substrate: birchwood xylan


organism: Cellvibrio japonicus

substrate_name: aldotriouronic acid

substrate: aldotriouronic acid


organism: Rattus norvegicus

proof_lines:
37°C, wild-type enzyme
wild-type dynamin, high salt
wild-type dynamin, low salt


proof_lines:
I690K mutant, high salt
I690K mutant, low salt
I690K mutant, + GAP


proof_lines:
K694A mutant, low salt
K694A mutant, + GAP
K694A mutant, high salt


organism: Aspergillus niger


proof_lines: wild type enzyme, in 50 mM K+-HEPES (pH 7.5 and 25°C)

proof_lines: wild type enzyme, in 0.1 M imidazole (pH 7.6 and 25°C)

proof_lines: wild type enzyme, in 50 mM K+-HEPES (pH7.5 and 25°C)


proof_lines: mutant enzyme P240T, in 50 mM K+-HEPES (pH 7.5 and 25°C)


proof_lines: mutant enzyme C124S, in 50 mM K+-HEPES (pH 7.5 and 25°C)


proof_lines: mutant enzyme P240S, in 50 mM K+-HEPES (pH 7.5 and 25°C)


proof_lines: mutant enzyme C124A, in 50 mM K+-HEPES (pH 7.5 and 25°C)


proof_lines: mutant enzyme Y44F, in 50 mM K+-HEPES (pH 7.5 and 25°C)


organism: Dianthus caryophyllus


enzyme_display_name: choline-sulfatase

organism: Sinorhizobium meliloti

substrate_name: choline O-sulfate

enzyme: choline-sulfatase

substrate: choline O-sulfate


substrate_name: phosphoryl choline

substrate: phosphoryl choline


enzyme_display_name: aspartate N-acetyltransferase

substrate_name: L-aspartate

assay_conditions_summary: pH 7.1; 303.15 K; cofactor CoA

enzyme: aspartate N-acetyltransferase

substrate: L-aspartate


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: 4-nitrophenyl methylphosphonate

substrate: 4-nitrophenyl methylphosphonate


proof_lines:
at pH 6.0 and 25°C
at pH 7.6 and 25°C
pH 7.5, 25°C


substrate_name: 4-nitrophenyl methylphosphate

substrate: 4-nitrophenyl methylphosphate


proof_lines:
wild-type, pH 6.0, 25°C
wild-type, pH 7.6, 25°C


substrate_name: 4-Methylumbelliferyl sulfate

substrate: 4-Methylumbelliferyl sulfate


substrate_name: Choline sulfate

substrate: Choline sulfate


substrate_name: 4-Nitrophenyl sulfate

substrate: 4-Nitrophenyl sulfate


assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, temperature not specified in the publication

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


enzyme_display_name: phosphoribulokinase

organism: Spinacia oleracea

substrate_name: ATP; D-Ribulose 5-phosphate

enzyme: phosphoribulokinase

substrate: ATP; D-Ribulose 5-phosphate


organism: Trieres chinensis

substrate_name: D-ribulose 5-phosphate

assay_conditions_summary: pH 8; cofactor ATP

substrate: D-ribulose 5-phosphate


organism: Mus musculus

assay_conditions_summary: cofactor CoA

proof_lines:
in presence of 1 mM CHAPS
in presence of 0.5 mM CHAPS


assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

proof_lines: pH 7.0, 37°C, slightly varying Km depending on source organelle


organism: Anabaena cylindrica

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


organism: Brassica sp.

substrate_name: ATP

substrate: ATP


organism: Cereibacter sphaeroides

substrate_name: Unknown

substrate: Unknown


substrate_name: aspartate

data_origin: experimental

substrate: aspartate


sequence_source: UniProtKB:P12033; RCSB PDB:1A7J; PRK I/prkA structural paper context

assay_conditions_summary: pH 8.2; 303.15 K; cofactor NADH

proof_lines: wild type enzyme, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-phos

proof_lines: wild-type enzyme and S19A mutant, pH 8, 30°C


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation H100Q; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature H100Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H100Q, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-p


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation Y98L; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature Y98L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y98L, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-ph


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation H100N; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature H100N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H100N, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-p


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation H100A; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature H100A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H100A, at 30°C, in 100 mM Tris-HCl (pH 8.2) containing 10 mM MgCl2, 0.5 mM dithiothreitol, 5 mM ATP, 0.2 mM phosphoenolpyruvate, 0.2 mM NADH, 2 units of pyruvate kinase, 2 units of lactic dehydrogenase, and 1 mM D-ribulose 5-p


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation R168Q; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature R168Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation R186Q; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature R186Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation R173Q; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature R173Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P12033 using selected mutation R187Q; P12033 is PRK I/prkA with PDB 1A7J. and applied mutation signature R187Q to reconstruct the assayed variant sequence.


organism: Chlamydomonas reinhardtii

sequence_source: UniProtKB:P19824; reviewed entry cites PMID 16667433 / DOI 10.1104/pp.93.1.188

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


organism: Halothiobacillus neapolitanus

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


organism: Heterosigma akashiwo

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


organism: Unknown


organism: Escherichia coli (strain K12)

substrate_name: imido-di-P (with magnesium ions as cofactor and at pH 9)

assay_conditions_summary: pH 7

proof_lines: kcat is 10.2 sec(-1) with alpha-Glc-1-P as substrate. kcat is 1.26 sec(-1) with alpha-Man-1-P as substrate. kcat is 0.98 sec(-1) with alpha-Gal-1-P as substrate. kcat is 0.09 sec(-1) with Glc-6-P as substrate (at pH 7.0 and 37 degrees Celsi


assay_conditions_summary: pH 7.9; 293.15 K; cofactor ATP


organism: Synechococcus sp.

proof_lines:
pH 8, 25°C
pH 7, 25°C


organism: Triticum aestivum


organism: Enterobacter cloacae

substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


organism: Escherichia coli


organism: Lathyrus oleraceus


organism: Pholiota microspora

substrate_name: ADP

assay_conditions_summary: cofactor ADP

substrate: ADP


organism: Aspergillus nidulans


organism: Penicillium chrysogenum


organism: Pseudomonas aeruginosa


organism: Pseudomonas nitroreducens


enzyme_display_name: anthrax lethal factor endopeptidase

organism: Bacillus anthracis

proof_lines:
in 20 mM HEPES, pH 7.4, at 25°C
in 0.1 M HEPES, pH 7.4 at 37°C

enzyme: anthrax lethal factor endopeptidase


enzyme_display_name: taurocyamine kinase

organism: Arenicola brasiliensis

substrate_name: Taurocyamine

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

proof_lines: mutant enzyme K69R/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C

enzyme: taurocyamine kinase

substrate: Taurocyamine


proof_lines: mutant enzyme T70A, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K95E, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K69A, in 100 mM Tris-HCl, at pH 8.0 and 25°C


organism: Citrobacter braakii

substrate_name: D-glucose 6-phosphate

proof_lines:
Vmax: 0.8 micromol/min/mg
Vmax: 2.2 micromol/min/mg
Vmax: 2.6 micromol/min/mg

substrate: D-glucose 6-phosphate


organism: Pantoea agglomerans

substrate_name: myo-inositol hexakisphosphate

proof_lines: entrapped enzyme, pH 4.5, dropped as a consequence of entrapment

substrate: myo-inositol hexakisphosphate


organism: Pantoea sp. 3.5.1

substrate_name: alpha-D-glucose 1-phosphate

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

substrate: alpha-D-glucose 1-phosphate


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


proof_lines: mutant enzyme H67A, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K95I, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K95R, in 100 mM Tris-HCl, at pH 8.0 and 25°C


organism: Riftia pachyptila


proof_lines: mutant enzyme V71A, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K95A, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K69R, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme T68A, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme T68A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K95H, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme H67A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme T70A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C


organism: Paragonimus westermani


organism: Phytophthora sojae


substrate_name: glycocyamine

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

substrate: glycocyamine


assay_conditions_summary: pH 9; 303.15 K; cofactor ATP

proof_lines: recombinant enzyme, pH 9.0, 30°C, with glycocyamine

proof_lines: recombinant enzyme, pH 9.0, 30°C, with taurocyamine


proof_lines: mutant enzyme K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme V71A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C


proof_lines: mutant enzyme K69A/K95Y, in 100 mM Tris-HCl, at pH 8.0 and 25°C


organism: Clonorchis sinensis

proof_lines: recombinant full-length enzyme, pH 8.0, 25°C


enzyme_display_name: dynamin GTPase

organism: Homo sapiens

substrate_name: GTP

proof_lines: 37°C, T65A mutant dynamin, lipid tubule stimulated GTPase activity

proof_lines: 37°C, T65A mutant dynamin, basal GTPase activity

enzyme: dynamin GTPase

substrate: GTP


proof_lines: 37°C, T141A mutant dynamin, basal GTPase activity

proof_lines: 37°C, T141A mutant dynamin, lipid tubule stimulated GTPase activity


enzyme_display_name: alpha-N-acetylglucosaminidase

organism: Unknown

enzyme: alpha-N-acetylglucosaminidase


organism: Bos taurus

proof_lines: R66A mutant of the GTPase domain of dynamin


proof_lines: S45N mutant of the GTPase domain of dynamin


proof_lines: K142A mutant of the GTPase domain of dynamin


proof_lines: Km is in the range of 0.005-0.05 mM depending on salt and temperature conditions


organism: Bacteroides thetaiotaomicron


organism: Clostridium perfringens


mutation_signature: C-terminal deletion mutant

proof_lines: C-terminal deletion mutant, pH 7.4, 37°C


enzyme_display_name: rhomboid protease

organism: Providencia stuartii

substrate_name: FL-casein

proof_lines: K0.5 value, Hill coefficient 1.8, pH 6.0, 3°C

proof_lines: K0.5 value, Hill coefficient 1.7, pH 6.0, 3°C

enzyme: rhomboid protease

substrate: FL-casein


enzyme_display_name: ferredoxin--nitrate reductase

organism: Haloferax volcanii

substrate_name: nitrate

proof_lines: 120 mM Na2CO3 pH 9, 1 M NaCl, 4 mM methyl viologen, 35 mM KNO3, 17 mM Na2S2O4 (freshly prepared in 0.1 M NaHCO3) and 0.7 mU of enzyme preparations. The samples are incubated for 20 min at 60°C

enzyme: ferredoxin--nitrate reductase

substrate: nitrate


enzyme_display_name: L-iduronidase

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

proof_lines:
Aldurazyme, at pH 3.5 and 37°C
recombinant enzyme, at pH 3.5 and 37°C
at pH 2.8 and 37°C

source_databases_merged: sabio_rk brenda skid

enzyme: L-iduronidase


substrate_name: 4-methylumbelliferyl alpha-L-iduronide

proof_lines: pH 4.2, 32°C, recombinant wild-type enzyme

substrate: 4-methylumbelliferyl alpha-L-iduronide


organism: Escherichia coli

substrate_name: BODIPY FL casein

substrate: BODIPY FL casein


enzyme_display_name: levanase

organism: Dyadobacter fermentans

substrate_name: low molecular weight levan

proof_lines: S0.5 value, Hill coefficient 0.98, pH 6, 37°C

enzyme: levanase

substrate: low molecular weight levan


organism: Paenarthrobacter aurescens

proof_lines: S0.5 value, Hill coefficient 1.48, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 1.44, pH 6, 37°C


organism: Shouchella lehensis G1

substrate_name: levan

substrate: levan


proof_lines: dialdehyde starch-tapioca/bovine serum albumine cross-linked aggregate, pH 8, 30°C

proof_lines: glutaraldehyde cross-linked aggregate, pH 8, 30°C


organism: Haemophilus influenzae

substrate_name: TatA

proof_lines: K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C

substrate: TatA


organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)


enzyme_display_name: phosphoketolase

organism: Pseudomonas aeruginosa

substrate_name: D-Fructose 6-phosphate

enzyme: phosphoketolase

substrate: D-Fructose 6-phosphate


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


enzyme_display_name: hydrogenase (acceptor)

organism: Methanosarcina barkeri

substrate_name: oxidized ferredoxin

enzyme: hydrogenase (acceptor)

substrate: oxidized ferredoxin


organism: Nitratidesulfovibrio vulgaris


organism: Pyrococcus furiosus

assay_conditions_summary: cofactor NAD+

proof_lines: with methyl viologen as electron acceptor

proof_lines: with methylene blue as electron acceptor


organism: Solidesulfovibrio fructosivorans


organism: Streptomyces sp.

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


organism: Trichormus variabilis

substrate_name: oxidized methyl viologen

proof_lines:
cell free extract
cell-free extract, at pH 8.0 and 30°C
purified enzyme

substrate: oxidized methyl viologen


organism: Haloferax denitrificans


organism: Hydrogenobacter thermophilus

substrate_name: reduced ferredoxin 1

substrate: reduced ferredoxin 1


organism: Leptolyngbya boryana

substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


organism: Synechococcus elongatus PCC 7942 = FACHB-805

proof_lines: mutant enzyme R46K, pH and temperature not specified in the publication


organism: Vibrio natriegens

proof_lines: S0.5 value, Hill coefficient 1.08, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 0.77, pH 6, 37°C


organism: Bifidobacterium adolescentis

substrate_name: D-sedoheptulose 7-phosphate

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

substrate: D-sedoheptulose 7-phosphate


organism: Bifidobacterium animalis subsp. lactis

substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


organism: Lactiplantibacillus plantarum

substrate_name: D-fructose 6-phosphate

proof_lines:
apparent Km value, Ca2+
apparent Km value, Mg2+
apparent Km value, Mn2+

substrate: D-fructose 6-phosphate


organism: Allochromatium vinosum

substrate_name: Abz-VAA

proof_lines: NiFe hydrogenase attached to a pyrolytic graphite electrode

substrate: Abz-VAA


organism: Azotobacter vinelandii

substrate_name: oxidized methylene blue

proof_lines:
membrane-associated enzyme
purified enzyme

substrate: oxidized methylene blue


organism: Cupriavidus necator

proof_lines:
at pH 5.5, 20°C
at pH 5.0, 30°C
at pH 6.0, 30°C


organism: Desulfomicrobium norvegicum


organism: Desulfovibrio desulfuricans

substrate_name: Unknown

substrate: Unknown


organism: Desulfovibrio multispirans


organism: Desulfovibrio vulgaris

substrate_name: Hydrogen

substrate: Hydrogen


organism: Escherichia coli


substrate_name: methionaquinone

substrate: methionaquinone


organism: Hydrogenophaga sp.

substrate_name: methyl viologen

substrate: methyl viologen


organism: Lamprobacter modestohalophilus


organism: Methanocaldococcus jannaschii

substrate_name: methylenetetrahydromethanopterin

substrate: methylenetetrahydromethanopterin


organism: Lactococcus lactis subsp. lactis


organism: Pseudomonas aeruginosa


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

substrate_name: levan

sequence_source: source_record and UniProtKB Q8A6W6

assay_conditions_summary: pH 8

proof_lines: kcat is 32987 min(-1) with levan as substrate (PubMed:20603004). kcat is 466 sec(-1) with levan synthesized by wild-type Lsc3 from sucrose as substrate (PubMed:28103254). kcat is 366 sec(-1) with levan synthesized by wild-type Lsc3 from raf

substrate: levan


organism: Synechococcus elongatus PCC 7942 = FACHB-805

substrate_name: nitrate

proof_lines: mutant enzyme K201R, pH and temperature not specified in the publication

substrate: nitrate


proof_lines: mutant enzyme R197Q, pH and temperature not specified in the publication


proof_lines: mutant enzyme E219QR, pH and temperature not specified in the publication


proof_lines: mutant enzyme K614R, pH and temperature not specified in the publication


proof_lines: mutant enzyme R43K, pH and temperature not specified in the publication


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


proof_lines: mutant enzyme R46Q, pH and temperature not specified in the publication


proof_lines: dithionite-reduced methyl viologen as electron donor


organism: Synechococcus sp.

proof_lines: 25°C, pH 8.0, electron donor methylviologen

proof_lines: reduced methyl viologen as electron donor, recombinant enzyme expressed in Escherichia coli


organism: Synechocystis sp. PCC 6803


organism: Rattus norvegicus


organism: Pyrococcus furiosus


organism: Azotobacter chroococcum


organism: Belliella baltica

substrate_name: low molecular weight levan

proof_lines: S0.5 value, Hill coefficient 1.00, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 1.34, pH 6, 37°C

substrate: low molecular weight levan


organism: Capnocytophaga ochracea

proof_lines: S0.5 value, Hill coefficient 2.09, pH 6, 37°C

proof_lines: S0.5 value, Hill coefficient 0.82, pH 6, 37°C


organism: Homo sapiens


organism: Bos taurus

substrate_name: phenyl-alpha-N-acetylglucosaminide

proof_lines:
form I 0.32, form II 0.29
form I 0.067, form II 0.043

substrate: phenyl-alpha-N-acetylglucosaminide


proof_lines: 0.58 in the presence of 0.025% bovine serum albumin

proof_lines: pH 4.5, 37°C, without bovine serum albumin


organism: Sus scrofa

proof_lines:
partially purified enzyme
0.08 partially purified enzyme


organism: Arthrobacter sp.


organism: Bacillus subtilis


organism: Rhodotorula sp.


proof_lines:
pH 4.5, 37°C
pH 2.8
pH 5.8, 37°C, recombinant enzyme


substrate_name: phenyl alpha-L-iduronide

substrate: phenyl alpha-L-iduronide


organism: Escherichia coli

substrate_name: FL-casein

proof_lines: K0.5 value, Hill coefficient 1.2, pH 6.0, 3°C

substrate: FL-casein


organism: Bacillus anthracis

substrate_name: fluorescein-QRRKKVYPYPME

substrate: fluorescein-QRRKKVYPYPME


substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


organism: Arenicola brasiliensis

substrate_name: Taurocyamine

substrate: Taurocyamine


organism: Arenicola marina

substrate_name: N-taurocyamine

substrate: N-taurocyamine


organism: Phytophthora infestans

proof_lines: isoform PK1, in 100 mM Tris-HCl, at pH 8.0 and 25°C

proof_lines: isoform PK2, in 100 mM Tris-HCl, at pH 8.0 and 25°C


organism: Bitis arietans

substrate_name: methylumbelliferyl-N-acetylglucosamine

substrate: methylumbelliferyl-N-acetylglucosamine


organism: Oenococcus oeni

substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


organism: Rhodotorula graminis


proof_lines:
10°C, pH 7.4
fetal and adult enzyme


organism: Rattus norvegicus


organism: Pseudomonas aeruginosa


enzyme_display_name: thymine dioxygenase

organism: Rhodotorula glutinis

substrate_name: thymine

enzyme: thymine dioxygenase

substrate: thymine


organism: Neurospora crassa

sequence_source: UniProtKB:Q7RYZ9 active accession; sequence present in UniProt but not emitted by this exact-accession verdict

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


organism: Ignavibacterium album

substrate_name: ethyl-alpha-D-glucose

proof_lines: glucosyl transferase activity, pH 5.0, 37°C

substrate: ethyl-alpha-D-glucose


organism: Ignavibacterium album (strain DSM 19864 / JCM 16511 / NBRC 101810 / Mat9-16)

substrate_name: sophorose (with pNP-alpha-glucose as an acceptor)

proof_lines: kcat is 70 sec(-1) with sophorose as substrate. kcat is 12 sec(-1) with beta-(1->2)-glucotriose as substrate. kcat is 1.0 sec(-1) with methyl-alpha-glucose as substrate. kcat is 0.55 sec(-1) with ethyl-alpha-glucose as substrate. kcat is 1.


enzyme_display_name: ananain

organism: Ananas comosus

substrate_name: synthetic 7-amino-4-methylcoumarin (AMC) substrate Z-Phe-Val-Arg-AMC (at pH 5.0 and 37 degrees Celsius)

proof_lines: kcat is 13.9 sec(-1) for Z-Phe-Val-Arg-AMC. kcat is 1.58 sec(-1) for Z-Phe-Arg-AMC. kcat is 0.16 sec(-1) for Z-Arg-Arg-AMC. kcat is 9.80 sec(-1) for Pro-Leu-Gln. kcat is 7.13 sec(-1) for Val-Leu-Arg. kcat is 5.62 sec(-1) for Pro-Leu-Arg. kc

enzyme: ananain


enzyme_display_name: peptidyltransferase

substrate_name: N-Formylmethionyl-tRNA(fMet); Puromycin

proof_lines:
at 37°C and pH 7.5
when NH4Cl ribosomal wash is present
when NH4Cl ribosomal wash is absent

enzyme: peptidyltransferase

substrate: N-Formylmethionyl-tRNA(fMet); Puromycin


organism: Oryctolagus cuniculus

substrate_name: AcPhe-tRNA

proof_lines: from the competitive phase of the inhibition

substrate: AcPhe-tRNA


substrate_name: acetylphenylalanyl-tRNA

substrate: acetylphenylalanyl-tRNA


organism: Saccharomyces cerevisiae

proof_lines: strain 2A-J809 lacking the two genes encoding L24

proof_lines: strain L1729 lacking the single gene encoding L39

proof_lines: strain YKS99-2C missing the protein L41, the two genes RPL41A and RPL41B


proof_lines: triple mutant strain L1725 lacking the proteins L24 and L39


proof_lines:
wild type strain YKS99-2A
wild type strain 2D-J809


substrate_name: PLK

substrate: PLK


organism: Bos taurus

substrate_name: GTP

proof_lines: T65A mutant of the GTPase domain of dynamin

substrate: GTP


proof_lines: T141Q mutant of the GTPase domain of dynamin


organism: Ancylobacter novellus


organism: Bifidobacterium adolescentis

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


organism: Debaryomyces hansenii


organism: Leuconostoc mesenteroides


organism: Leuconostoc mesenteroides subsp. mesenteroides


enzyme_display_name: acetyl-CoA C-acetyltransferase

organism: Escherichia coli

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines:
pH 7.8, 30°C
Raw SKiD Env: Temp=30°C, pH=7.8

enzyme: acetyl-CoA C-acetyltransferase

substrate: acetyl-CoA


organism: Homo sapiens

substrate_name: H2O; Oleoyl-CoA

substrate: H2O; Oleoyl-CoA


assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA


substrate_name: Coenzyme A

substrate: Coenzyme A


organism: Clostridium acetobutylicum

substrate_name: Coenzyme A; Acetoacetyl-CoA

substrate: Coenzyme A; Acetoacetyl-CoA


organism: Cupriavidus necator

substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 8.3; 303.15 K; cofactor CoA

substrate: acetoacetyl-CoA


organism: Enterococcus faecalis

substrate_name: Acetyl-CoA

substrate: Acetyl-CoA


organism: Arabidopsis thaliana


organism: Aspergillus fumigatus

substrate_name: acetyl-CoA; acetoacetyl-CoA; CoA

source_db: brenda; skid

assay_conditions_summary: pH 8.1; 303.15 K; cofactor CoA

proof_lines:
pH 8.1, 30°C
Raw SKiD Env: Temp=30°C, pH=8.1

substrate: acetyl-CoA; acetoacetyl-CoA; CoA

source: brenda; skid


organism: Bacopa monnieri

substrate_name: acetoacetyl-CoA; acetyl-CoA

assay_conditions_summary: pH 8.9; 298.15 K; cofactor CoA

substrate: acetoacetyl-CoA; acetyl-CoA


organism: Candida tropicalis

assay_conditions_summary: cofactor CoA


organism: Zoogloea ramigera

substrate_name: Acetoacetyl-10-bis-demethylpantetheine 11-pivaloate; Coenzyme A


substrate_name: CTP

substrate: CTP


organism: Plasmodium falciparum

substrate_name: Ethanolamine phosphate

substrate: Ethanolamine phosphate


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


organism: Ricinus communis

substrate_name: CTP; Ethanolamine phosphate

substrate: CTP; Ethanolamine phosphate


organism: Trypanosoma brucei


assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


organism: Metallosphaera sedula

assay_conditions_summary: pH 7.5; 343.15 K; cofactor CoA


organism: Mus musculus

proof_lines:
isozyme Pcyt2alpha, at 37°C
isozyme Pcyt2beta, at 37°C


proof_lines: pH 8.0, 37°C, recombinant His-tagged mutant H146A enzyme


proof_lines: pH 8.0, 37°C, recombinant His-tagged mutant H422A enzyme


enzyme_display_name: phosphatidate phosphatase

substrate_name: H2O; Dioctanoyl phosphatidic acid

enzyme: phosphatidate phosphatase

substrate: H2O; Dioctanoyl phosphatidic acid


enzyme_display_name: protein-glutamine glutaminase

organism: Chryseobacterium proteolyticum

substrate_name: CBz-Gln-Gly

proof_lines: pH 6.5, 37°C, recombinant wild-type enzyme

enzyme: protein-glutamine glutaminase

substrate: CBz-Gln-Gly


proof_lines: pH 6.5, 37°C, recombinant mutant T211V/I271V enzyme


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: (S)-norcoclaurine synthase

organism: Thalictrum flavum

proof_lines: mutant E110A, 37°C, 0.1 M phosphate buffer pH 7.5

enzyme: (S)-norcoclaurine synthase


proof_lines: mutant Y108F, 37°C, 0.1 M phosphate buffer pH 7.5


proof_lines: wild-type, 37°C, 0.1 M phosphate buffer pH 7.5


organism: Pyrobaculum neutrophilum

assay_conditions_summary: pH 7.8; 358.15 K; cofactor CoA


organism: Rattus norvegicus


organism: Sus scrofa


enzyme_display_name: coenzyme-B sulfoethylthiotransferase

organism: Methanothermobacter marburgensis

substrate_name: Unknown

enzyme: coenzyme-B sulfoethylthiotransferase

substrate: Unknown


proof_lines: mutant enzyme L68T/M97V, at pH 7.5 and 30Â°C


enzyme_display_name: 3-hexulose-6-phosphate synthase

organism: Methylomonas aminofaciens

substrate_name: formaldehyde

enzyme: 3-hexulose-6-phosphate synthase

substrate: formaldehyde


organism: Mycobacterium gastri

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Bos taurus

proof_lines:
isoenzyme A, thiolysis
enzyme B
isoenzyme B, thiolysis


substrate_name: acetyl-CoA

proof_lines: isoenzyme A, in the presence of 3.5 mM NH4+


organism: Unknown


organism: Methanothermobacter thermautotrophicus

substrate_name: coenzyme B

proof_lines:
isoenzyme I
isoenzyme II
below

substrate: coenzyme B


organism: Arabidopsis thaliana

substrate: acetyl-CoA


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

substrate_name: acetoacetyl-CoA (in law salt conditions)

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


organism: Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10)

substrate_name: CoA

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

substrate: CoA


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


substrate_name: acetoacetyl-CoA


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Methanosarcina thermophila

substrate_name: methyl-coenzyme M

sequence: AADIFAKFKTSMEVK

wild_type_sequence: AADIFAKFKTSMEVK

substrate: methyl-coenzyme M


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)


organism: Escherichia coli (strain K12)

substrate_name: undecaprenyl pyrophosphate

substrate: undecaprenyl pyrophosphate


organism: Homo sapiens


substrate_name: phosphatidate (isoform 1)

substrate: phosphatidate (isoform 1)


organism: Mus musculus


organism: Rattus norvegicus

substrate_name: 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phosphate (at pH 6.5 and 37 degrees Celsius)


organism: Cavia cutleri

substrate_name: serotonin (for protein-glutamine serotonyltransferase activity)


organism: Thalictrum flavum subsp. glaucum


organism: Bacillus subtilis

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

substrate: acetoacetyl-CoA


organism: Bradyrhizobium japonicum


organism: Candida tropicalis

proof_lines: recombinant peroxisomal thiolase I, thiolysis

proof_lines: recombinant cytosolic thiolase I, thiolysis


organism: Clostridium acetobutylicum


organism: Enterococcus faecalis

proof_lines: synthesis thiolysis


organism: Escherichia coli


organism: Gallus gallus


organism: Helianthus annuus

substrate_name: Coenzyme A; Acetoacetyl-CoA

substrate: Coenzyme A; Acetoacetyl-CoA


proof_lines:
E252del mutant enzyme
mutant enzyme E252del


organism: Rhizobium sp.

proof_lines:
thiolysis
enzyme from bacteroids
synthesis


organism: Streptomyces collinus

proof_lines:
native thiolase
recombinant thiolase


proof_lines: kcat is 21 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM KCl) (PubMed:17371050). kcat is 8 sec(-1) for the degradation of acetoacetyl-CoA (at 25 degrees Celsius in the presence of 40 mM NaCl)


proof_lines: kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1) for octanoyl-CoA hydrolysis (PubMed:254


organism: Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 / Marburg)

proof_lines: kcat is 18 sec(-1) (at 25 degrees Celsius, under conditions in which the heterodisulfide product is recycled via reduction by hydroxocobalamin). kcat is 0.96 sec(-1) (at 25 degrees Celsius, under conditions in which the heterodisulfide prod


organism: Chryseobacterium proteolyticum

substrate_name: casein

proof_lines: kcat is 323.8 min(-1) with casein as substrate. kcat is 974.5 min(-1) with oxidized insulin B chain as substrate. kcat is 525.9 min(-1) with Cbz-Gln-Gly as substrate. kcat is 342.8 min(-1) with Cbz-Gln-O-methyl as substrate. kcat is 410.8 m

substrate: casein


organism: Homo sapiens

substrate_name: benzyloxycarbonyl-Gln-Gly (for protein-glutamine deamidase activity)

proof_lines: kcat is 11.2 min(-1) with benzyloxycarbonyl-Gln-Gly substrate for protein-glutamine deamidase activity.


organism: Papaver somniferum

proof_lines: Sigmoidal saturation kinetics suggesting positive cooperativity in the binding of dopamine.


organism: Unknown


organism: Sus scrofa


organism: Thermus thermophilus

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 8; 338.15 K; cofactor CoA

substrate: Acetyl-CoA


organism: Zoogloea ramigera


organism: Rattus norvegicus

substrate_name: CTP

proof_lines:
pH 7.8, 37°C
approximate value, pH 7.8, 37°C
pH 5.5

substrate: CTP


organism: Methanosarcina thermophila

substrate_name: methyl coenzyme M

substrate: methyl coenzyme M


organism: Methanothermobacter marburgensis

substrate_name: CoB

proof_lines: with SH-CoB6 as cosubstrate, pH not specified in the publication, at 25°C

proof_lines: with SH-CoB5 as cosubstrate, pH not specified in the publication, at 25°C

substrate: CoB


organism: Methanothrix soehngenii


substrate_name: H2O; Sphinganine 1-phosphate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: phosphatidate dispersed in sonicated microsomal lipid

proof_lines: phosphatidate bound to microsomal membrane

substrate: H2O; Sphinganine 1-phosphate


organism: Chryseobacterium cucumeris

substrate_name: CBz-Gln-Gly

substrate: CBz-Gln-Gly


organism: Niallia circulans

substrate_name: benzyloxycarbonyl-L-Gln-L-Pro

substrate: benzyloxycarbonyl-L-Gln-L-Pro


enzyme_display_name: maleimide hydrolase

organism: Agrobacterium tumefaciens

substrate_name: Phthalimide

enzyme: maleimide hydrolase

substrate: Phthalimide


organism: Pseudomonas putida

substrate_name: hydantoin

substrate: hydantoin


organism: Methylococcus capsulatus

substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


substrate_name: D-Ribulose 5-phosphate; Formaldehyde

substrate: D-Ribulose 5-phosphate; Formaldehyde


organism: Blastobacter sp.

substrate_name: H2O; Succinimide

substrate: H2O; Succinimide


organism: Blastobacter sp. A17p-4

substrate_name: Maleimide

substrate: Maleimide


organism: Oreochromis niloticus


substrate_name: H2O; Phthalimide

substrate: H2O; Phthalimide


proof_lines: pH 7, 60°C, KM increases about 20-30fold when the reaction temperature increases from 25 to 60°C


organism: Corydalis chinensis

substrate_name: dopamine

substrate: dopamine


organism: Eschscholtzia tenuifolia


organism: Eschscholzia californica

proof_lines: pH 7.0, 37°C, hyperbolic saturation kinetics


organism: Nandina domestica


organism: Papaver somniferum


organism: Thalictrum flavum


organism: Thalictrum flavum ssp. glaucum

proof_lines: pH 7.5, 37°C, hyperbolic saturation kinetics


organism: Bacillus sp. (in: firmicutes)

substrate_name: D-ribulose 5-phosphate; formaldehyde

proof_lines: D-ribulose 5-phosphate generated from ribose 5-phosphate, at 50°C

proof_lines: commercial D-ribulose 5-phosphate, at 50°C

substrate: D-ribulose 5-phosphate; formaldehyde


substrate_name: D-arabino-hex-3-ulose 6-phosphate; D-ribulose 5-phosphate; formaldehyde

assay_conditions_summary: pH 7; 303.15 K; buffer 50 mM sodium potassium phosphate

proof_lines: in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 30°C

proof_lines: in 50 mM sodium potassium phosphate buffer, 5 mM MgCl2, at pH 7.0, at 37°C


organism: Methylomonas aminofaciens

substrate_name: formaldehyde; D-ribulose 5-phosphate

assay_conditions_summary: pH 7.4; buffer 50 mM potassium phosphate

proof_lines: in 50 mM potassium phosphate buffer (pH 7.4), 5 mM MgCl2

substrate: formaldehyde; D-ribulose 5-phosphate


organism: Methylomonas sp.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 300 mM Tris-HCI

proof_lines: in 300 mM Tris-HCI buffer (pH 7.5), at 30°C


organism: Methylophilus methylotrophus


organism: Methylotuvimicrobium alcaliphilum


organism: Mycobacterium gastri

assay_conditions_summary: pH 7.5; 303.15 K; buffer 500 mM potassium phosphate

proof_lines: apparent value, in 50 mM potassium phosphate, pH 7.5, with 5 mM MgCl2, at 30°C

proof_lines: in 500 mM potassium phosphate buffer, at pH 7.5, at 30°C


organism: Pseudomonas sp.


organism: Pyrococcus horikoshii

substrate_name: formaldehyde

proof_lines:
recombinant HPS, at 60°C
recombinant HPS, at 80°C

substrate: formaldehyde


enzyme_display_name: coenzyme A diphosphatase

organism: Mus musculus

substrate_name: CoA

enzyme: coenzyme A diphosphatase

substrate: CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: coenzyme A

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: coenzyme A


organism: Mycolicibacterium smegmatis

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Saccharomyces cerevisiae

substrate_name: oxidized CoA disulfide

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: oxidized CoA disulfide


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 4.6 sec(-1) with CoA as substrate (PubMed:10922370). kcat is 5.0 sec(-1) with CoASSCoA as substrate (PubMed:10922370). kcat is 0.133 sec(-1) with 8-oxo-dGTP as substrate using a GST-fused enzyme (PubMed:15475388).


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R34M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R189A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature D53A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R39A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature L41A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature R189M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature F40A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P11930, checked directly through UniProt REST during this review. and applied mutation signature E115A to reconstruct the assayed variant sequence.


organism: Mycobacterium tuberculosis


enzyme_display_name: D-arabinose 1-dehydrogenase (NADP(+))

organism: Saccharolobus solfataricus

substrate_name: D-arabinose

assay_conditions_summary: pH 7.5; 353.15 K; cofactor NADP+

proof_lines: pH 7.5, 70°C, determined with 10 mM D-arabinose

proof_lines: pH 7.5, 70°C, determined with 0.4 mM NADP+

enzyme: D-arabinose 1-dehydrogenase (NADP(+))

substrate: D-arabinose


enzyme_display_name: hydroquinone 1,2-dioxygenase

organism: Sphingobium chlorophenolicum

proof_lines: cosubstrate 2-chloro-6-methylhydroquinone, 1,2-cleavage, pH 7.0, 23°C

proof_lines: cosubstrate 2,6-dibromohydroquinone, pH 7.0, 23°C

enzyme: hydroquinone 1,2-dioxygenase


smiles: O=O


organism: Sphingomonas sp.

substrate_name: hydroquinone

proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7

substrate: hydroquinone


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

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

proof_lines: kcat is 23.8 sec(-1) with D-arabinose as substrate. kcat is 26.8 sec(-1) with L-fucose as substrate. kcat is 17.7 sec(-1) with L-galactose or D-ribose as substrate.


organism: Cupriavidus necator

proof_lines: pH 7.4, temperature not specified in the publication


organism: Lactococcus lactis

sequence_source: UniProt Q9CJC0 (yaiA, Lactococcus lactis subsp. lactis strain IL1403); PMID 25430846 abstract names YaiA as the hydroquinone dioxygenase.


organism: Pseudomonas fluorescens


enzyme_display_name: pestivirus NS3 polyprotein peptidase

organism: Classical swine fever virus (strain Alfort/Tuebingen)

substrate_name: Sub-UpU

enzyme: pestivirus NS3 polyprotein peptidase

substrate: Sub-UpU


organism: Candida albicans

substrate_name: L-fucose

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: with D-arabinose as cosubstrate, at pH 8.0 and 30°C

substrate: L-fucose


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines: recombinant subunit ARA1p, at pH 8.2 and 25°C

substrate: NADPH


organism: Hepacivirus hominis

substrate_name: Unknown

proof_lines: S-isomer R-isomer SCH446211

substrate: Unknown


organism: West Nile virus

proof_lines: pH and temperature not specified in the publication

proof_lines: at pH 8.0 in Tris-HCl (10 mM), CHAPS (1 mM) and glycerol (20% v/v), at 25°C


enzyme_display_name: endopeptidase Clp

organism: Escherichia coli (strain K12)

substrate_name: N-succinyl-Leu-Tyr-AMC

enzyme: endopeptidase Clp

substrate: N-succinyl-Leu-Tyr-AMC


organism: Escherichia coli

substrate_name: fEGFP-ssrA

assay_conditions_summary: pH 7.6; 303.15 K; cofactor ATP

proof_lines: presence of adaptor protein SspB, pH 7.6, 30°C

proof_lines: absence of adaptor protein SspB, pH 7.6, 30°C

substrate: fEGFP-ssrA


organism: Plasmodium falciparum

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: 30°C, pH 7.0, PfClpP is a very weak peptidase on its own


substrate_name: Arc-ssrA

proof_lines:
AKH mutant in the presence of SspB
AKH mutant

substrate: Arc-ssrA


proof_lines: wild-type, reducing conditions, 4°C, pH not specified in the publication

proof_lines: wild-type, non-reducing conditions, 4°C, pH not specified in the publication


proof_lines: mutant A153C, reducing conditions, 4°C, pH not specified in the publication


substrate_name: glucagon

proof_lines:
value below
ClpPDELTAN
ATPase activity

substrate: glucagon


organism: Staphylococcus aureus


proof_lines: mutant L144M, pH and temperature not specified in the publication


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


enzyme_display_name: 1,4-alpha-glucan branching enzyme

organism: Parageobacillus thermoglucosidasius

substrate_name: amylose

enzyme: 1,4-alpha-glucan branching enzyme

substrate: amylose


enzyme_display_name: lipoyl-dependent peroxiredoxin

organism: Xylella fastidiosa

substrate_name: [dihydrolipoamide acyltransferase, subunit E2 from pyruvate dehydrogenase complexlipoyl-carrier protein]-N6-[(R)-dihydrolipoyl]-L-lysine

proof_lines:
pH 7.4, 37°C
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: lipoyl-dependent peroxiredoxin


substrate_name: Lipoamide

substrate: Lipoamide


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide


organism: Mycobacterium tuberculosis


substrate_name: trans-pinocarveylhydroperoxide

substrate: trans-pinocarveylhydroperoxide


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


smiles: OO


enzyme_display_name: aminomethyltransferase

organism: Pisum sativum

substrate_name: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate

assay_conditions_summary: cofactor NAD+

enzyme: aminomethyltransferase

substrate: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate


organism: Rattus norvegicus


organism: Zea mays

proof_lines: amylose AS-320, pH 7.0, 30°C, chimeric enzyme form BE II-I BspHI

proof_lines: reduced amylose of an average chain-length 405, enzyme isoenzyme BE IIa


enzyme_display_name: heterotrimeric G-protein GTPase

substrate_name: H2O; GTP

enzyme: heterotrimeric G-protein GTPase

substrate: H2O; GTP


enzyme_display_name: bacterial tyrosine kinase

organism: Gallus gallus

substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

enzyme: bacterial tyrosine kinase

substrate: ATP


organism: Myxococcus xanthus

substrate_name: L-tyrosine in poly(Glu,Tyr)

substrate: L-tyrosine in poly(Glu,Tyr)


proof_lines: cytoplasmic fragment of BtkB (Ser444-Ser710), pH 7, 37°C


organism: Burkholderia cepacia

substrate_name: L-tyrosyl-[AAVHEYLSA]

substrate: L-tyrosyl-[AAVHEYLSA]


enzyme_display_name: triphosphatase

organism: Sulfolobus acidocaldarius

substrate_name: Triphosphate

enzyme: triphosphatase

substrate: Triphosphate


substrate_name: tripolyphosphate

substrate: tripolyphosphate


organism: Bos taurus

substrate_name: GTP

proof_lines: illuminated uROS is used as source of photoexited rhodopsin required for transducin activation

proof_lines: illuminated V8-uROS is used as source of photoexited rhodopsin required for transducin activation

substrate: GTP


organism: Homo sapiens

proof_lines: G36 protein phosphorylated by protein kinase M-like kinase


organism: Mus musculus


organism: Oryza sativa

proof_lines:
30°C, pH 6, presence of CaCl2, 2 mM
30°C, pH 6, presence of MgCl2, 2 mM
30°C, pH 5, presence of CuCl2, 2 mM


organism: Saccharolobus solfataricus


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 0.6 sec(-1) with tert-butyl hydroperoxide as substrate and AhpD as reductant and 0.1 sec(-1) with tert-butyl hydroperoxide as substrate and TrxC as reductant.


organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)

assay_conditions_summary: cofactor ATP


substrate_name: cAMP

proof_lines: kcat is 13 sec(-1) with triphosphate as substrate and Mg(2+) as cofactor. kcat is 35 sec(-1) with triphosphate as substrate and Co(2+) as cofactor. kcat is 3.4 sec(-1) with tetraphosphate as substrate and Mg(2+) as cofactor. kcat is 7.1 sec

substrate: cAMP


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

substrate_name: PPPi (at pH 9.7 and 37 degrees Celsius)

assay_conditions_summary: pH 9.7; cofactor ATP

proof_lines: kcat is 288 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 50 degrees Celsius). kcat is 76 sec(-1) for hydrolysis of PPPi (at pH 9.7 and 37 degrees Celsius). kcat is 19 sec(-1) for hydrolysis of PPPi (at pH 7.1 and 37 degrees Celsius). kcat

substrate: PPPi (at pH 9.7 and 37 degrees Celsius)


proof_lines: pH 7.5, 30°C, reduced amylose AS-320, wild-type enzyme


proof_lines: pH 7.5, 30°C, reduced amylose AS-320, mutant enzyme R384K


enzyme_display_name: lipoamidase

substrate_name: lipoyl-4-aminobenzoate; lipoyl 4-aminobenzoate; lipoyl-4-aminobenzoic acid; biotinyl-4-aminobenzoic acid; lipoyl-6-aminoquinoline

proof_lines: enzyme from serum, at pH 6.0, temperature not specified in the publication

enzyme: lipoamidase


organism: Sus scrofa

substrate_name: lipoylmethyl ester; reduced lipoyl-4-aminobenzoate; lipoyl n-butyl ester; lipoyl isopropyl ester; L-Tyr-Arg

proof_lines: pH and temperature not specified in the publication


organism: Nitrosomonas europaea

substrate_name: tripolyphosphate; ATP

assay_conditions_summary: pH 9.7; 310.15 K; cofactor ATP

proof_lines: His-tagged mutant enzyme K8A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged mutant enzyme K8A, at pH 10.1 and 50°C, in the presence of 10 mM Mn2+

proof_lines: His-tagged mutant enzyme K8A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+

substrate: tripolyphosphate; ATP


proof_lines: His-tagged mutant enzyme K85A, at pH 9.7 and 50°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged mutant enzyme K85A, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+


proof_lines: His-tagged mutant enzyme K52R, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+


proof_lines: His-tagged wild type enzyme, at pH 9.7 and 37°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged wild type enzyme, at pH 7.1 and 37°C, in the presence of 5 mM Mg2+

proof_lines: His-tagged wild type enzyme, at pH 8.1 and 50°C, in the presence of 10 mM Mn2+


proof_lines: R265H mutant, 2 mM substrate in the presence of 5 mM ATP

proof_lines: R265H mutant, 2 mM substrate in the presence of 5 mM diphosphate


organism: Enterococcus faecalis

substrate_name: octanoylated domain

substrate: octanoylated domain


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)

substrate_name: inorganic triphosphate

substrate: inorganic triphosphate


enzyme_display_name: dimethylallyltranstransferase

organism: Haematococcus lacustris

substrate_name: geranyl diphosphate

enzyme: dimethylallyltranstransferase

substrate: geranyl diphosphate


substrate_name: Isopentenyl diphosphate; Geranyl diphosphate


organism: Picea abies

substrate_name: dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


organism: Rattus norvegicus

substrate_name: Dimethylallyl diphosphate; Isopentenyl diphosphate


organism: Artemisia spiciformis


organism: Hevea brasiliensis

substrate_name: DMAPP

substrate: DMAPP


organism: Homo sapiens

substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Abies grandis

substrate: Dimethylallyl diphosphate; Isopentenyl diphosphate


organism: Corynebacterium glutamicum


organism: Micrococcus luteus


organism: Mycobacterium tuberculosis

proof_lines: in 50 mM sodium phosphate (pH 7.0), at 37°C


organism: Phaedon cochleariae

proof_lines: fixed substrate dimethylallyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Co2+

proof_lines: fixed substrate dimethylallyl diphosphate (0.05 mM), pH and temperature not specified in the publication, metal cofactor: Mg2+

proof_lines: fixed substrate isopentenyl diphosphate (0.015 mM), pH and temperature not specified in the publication, metal cofactor: Co2+


organism: Vitis vinifera


organism: Escherichia coli


mutation_signature: N-terminal deletion mutant


substrate_name: reduced H-protein

substrate: reduced H-protein


substrate_name: amylose

proof_lines: amylose AS-320, pH 7.0, 30°C, wild-type enzyme

substrate: amylose


proof_lines: amylose AS-320, pH 7.0, 30°C, mutant enzyme Y300F


organism: Oryctolagus cuniculus

substrate_name: amylopectin

substrate: amylopectin


organism: Oryza sativa

proof_lines: amylose AS-1160, degree of polymerization of approximately 6,510, isoform BEI, pH 7.5, 30°C


organism: Solanum tuberosum


organism: Bos taurus

substrate_name: cholesterol

proof_lines:
in the presence of 0.45% cyclodextrin
in the presence of 4.5% cyclodextrin
by large unilamellar vesicles

substrate: cholesterol


enzyme_display_name: [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase

substrate_name: ATP

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines:
pH 7.5, 30°C
ATP in form of MgATP2-

substrate: ATP


substrate_name: Coenzyme A; NAD+; alpha-Ketovaline

enzyme: [3-methyl-2-oxobutanoate dehydrogenase (acetyl-transferring)] kinase

substrate: Coenzyme A; NAD+; alpha-Ketovaline


substrate_name: ATP; [3-Methyl-2-oxobutanoate dehydrogenase (lipoamide)]


substrate_name: phosphate

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: 25°C, reconstituted with lipoylated recombinant E2

substrate: phosphate


substrate_name: O2; Cholesterol; Reduced adrenal ferredoxin

unit: mol/(mol*min)


substrate_name: Cholesterol; Reduced adrenal ferredoxin; O2


substrate_name: Cholest-5-ene-3beta,25-diol; Reduced ferredoxin; O2


substrate_name: BCKDH; ATP

substrate: BCKDH; ATP


enzyme_display_name: proprotein convertase 1

organism: Mus musculus

substrate_name: Unknown

enzyme: proprotein convertase 1

substrate: Unknown


proof_lines:
pH 7.0, 25°C,mixed inhibition
pH 7.0, 25°C
pH 6.5, 37°C


enzyme_display_name: steroid 15beta-monooxygenase

organism: Priestia megaterium

substrate_name: progesterone

proof_lines: pH 7.4, 30°C, for determination of Km-value the formation of the product 15beta-hydroxy-progesterone is determined

enzyme: steroid 15beta-monooxygenase

substrate: progesterone


substrate_name: deoxycorticosterone

substrate: deoxycorticosterone


enzyme_display_name: (S)-coclaurine-N-methyltransferase

organism: Coptis japonica

substrate_name: (S)-Coclaurine

enzyme: (S)-coclaurine-N-methyltransferase

substrate: (S)-Coclaurine


enzyme_display_name: sulfite dehydrogenase (cytochrome)

organism: Ancylobacter novellus

substrate_name: sulfite

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.0, mutant H57A

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.5, mutant H57A

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 7.0, mutant H57A

enzyme: sulfite dehydrogenase (cytochrome)

substrate: sulfite


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 9.0, mutant Y236F

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 7.5, mutant Y236F

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236F


organism: Chlorobaculum tepidum

substrate_name: ferricytochrome c

substrate: ferricytochrome c


organism: Starkeya novella

substrate_name: H2O; Ferricytochrome c; Sulfite

substrate: H2O; Ferricytochrome c; Sulfite


substrate_name: (RS)-coclaurine

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

substrate: (RS)-coclaurine


proof_lines: mutant F332A, pH not specified in the publication, temperature not specified in the publication


substrate_name: heliamine

proof_lines: mutant Y328A, pH not specified in the publication, temperature not specified in the publication

substrate: heliamine


proof_lines: mutant W329A, pH not specified in the publication, temperature not specified in the publication


substrate_name: reduced ferredoxin

proof_lines: pH 7.4, 30°C, wild-type ferredoxin from the cyanobacterium Anabaena PCC 7119

proof_lines: pH 7.4, 30°C, wild-type flavodoxin from the cyanobacterium Anabaena PCC 7119

substrate: reduced ferredoxin


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 10.0, wild-type enzyme

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 9.0, wild-type enzyme

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 9.5, wild-type enzyme


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.2, mutant R55M

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 6.6, mutant R55M

proof_lines: 25°C, 20 mM Tris acetate buffer, pH 7.5, mutant R55M


proof_lines: 25°C, 20 mM Tris acetate buffer, pH 8.5, mutant Y236Fyme


organism: Unknown

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


enzyme_display_name: flavone 3'-O-methyltransferase

organism: Oryza sativa Japonica Group

substrate_name: S-adenosyl-L-methionine; luteolin

enzyme: flavone 3'-O-methyltransferase

substrate: S-adenosyl-L-methionine; luteolin


enzyme_display_name: clostripain

organism: Hathewaya histolytica

proof_lines: commercial enzyme preparation, in 50 mM Tris-HCl, 5 mM dithiothreitol, and 5 mM CaCl2, at pH 7.5 and 25°C

proof_lines: purified recombinant enzyme, in 50 mM Tris-HCl, 5 mM dithiothreitol, and 5 mM CaCl2, at pH 7.5 and 25°C

enzyme: clostripain


enzyme_display_name: geraniol dehydrogenase (NAD(+))

organism: Castellaniella defragrans

substrate_name: nerol

proof_lines: native enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C

proof_lines: recombinant enzyme, in 100 mM glycine-NaOH, pH 9.4, at 21°C

enzyme: geraniol dehydrogenase (NAD(+))

substrate: nerol


organism: Arabidopsis thaliana

proof_lines: i.e. quercetin, 30°C, pH not specified in the publication

proof_lines: i.e. mycricetin, 30°C, pH not specified in the publication


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


organism: Carpoglyphus lactis

substrate_name: geraniol

sequence_source: UniProtKB reviewed accession B2NI93, found by lit_pubmed:18422649 and fetched from UniProt FASTA.

assay_conditions_summary: pH 8.5; 295.15 K; cofactor NAD+

substrate: geraniol


organism: Acidithiobacillus ferrooxidans

substrate_name: ferricyanide

proof_lines: reaction with ferricyanide or cytochrome c

substrate: ferricyanide


organism: Acidithiobacillus thiooxidans


proof_lines:
recombinant enzyme
at pH 7.7 and 360 mV
at pH 8.0 and 264 mV


assay_conditions_summary: pH 6; buffer pH 6

proof_lines: mutant enzyme Y236F, in 20 mM bis-Tris-acetate buffer pH 6.0

proof_lines: mutant enzyme Y236F, in 20 mM Tris-acetate buffer pH 8.0


assay_conditions_summary: pH 8; buffer pH 8

proof_lines: wild type enzyme, in 20 mM Tris-acetate buffer pH 8.0

proof_lines: wild type enzyme, in 20 mM bis-Tris-acetate buffer pH 6.0


organism: Homo sapiens

proof_lines: mutant enzyme G473A, pH 8.5, using ferricyanide as the electron acceptor

proof_lines: mutant enzyme G473A, pH 7.0, using ferricyanide as the electron acceptor


proof_lines: mutant enzyme G473W, pH 8.5, using ferricyanide as the electron acceptor

proof_lines: mutant enzyme G473W, pH 7.0, using ferricyanide as the electron acceptor


assay_conditions_summary: pH 7

proof_lines: mutant enzyme G473D, pH 7.0, using ferricyanide as the electron acceptor

proof_lines: mutant enzyme G473D, pH 8.5, using ferricyanide as the electron acceptor


proof_lines: tether deletion mutant enzyme DELTAKVATV, in 20 mM Tris acetate, pH 8.0, at 25°C


mutation_signature: tether deletion mutant enzyme DELTAKVAT

proof_lines: tether deletion mutant enzyme DELTAKVAT, in 20 mM Tris acetate, pH 8.0, at 25°C


mutation_signature: tether deletion mutant enzyme DELTAKVA

proof_lines: tether deletion mutant enzyme DELTAKVA, in 20 mM Tris acetate, pH 8.0, at 25°C


proof_lines: mutant enzyme P105A/P111A, in 20 mM Tris acetate, pH 8.0, at 25°C


proof_lines: wild type enzyme, in 20 mM Tris acetate, pH 8.0, at 25°C

proof_lines: wild type enzyme, pH 8.6, using ferricyanide as the electron acceptor

proof_lines: wild type enzyme, pH 7.0, using ferricyanide as the electron acceptor


proof_lines: mutant enzyme P105A, in 20 mM Tris acetate, pH 8.0, at 25°C


proof_lines: mutant enzyme P111A, in 20 mM Tris acetate, pH 8.0, at 25°C


organism: Paracoccus pantotrophus


organism: Paracoccus versutus


organism: Rhodotorula sp.

proof_lines:
reaction with cytochrome c
reaction with ferricyanide


substrate_name: H2O; Cytochrome c; Sulfite

substrate: H2O; Cytochrome c; Sulfite


organism: Thiobacillus thioparus


organism: Coptis japonica

substrate_name: (R,S)-norreticuline

substrate: (R,S)-norreticuline


organism: Liriodendron chinense

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


organism: Priestia megaterium

substrate_name: progesterone for the 15-beta hydroxylation

proof_lines: With deoxycorticosterone as substrate only 15-beta hydroxylation is observed.


organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

proof_lines: The values given here are for the native GeDH, the values for the recombinant protein can be found in another article (PubMed:22286981).


organism: Tanacetum cinerariifolium

substrate_name: trans-chrysanthemol

proof_lines: kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemol) (PubMed:29122986).

substrate: trans-chrysanthemol


organism: Oryza sativa subsp. japonica

substrate_name: quercetin

proof_lines: Measured at pH 7.5 and 37 degrees Celsius for all experiments.

substrate: quercetin


substrate_name: serotonin

substrate: serotonin


substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: GlcNAc

substrate: GlcNAc


organism: Hathewaya histolytica

substrate_name: Nalpha-benzoyl-L-Lys methyl ester

sequence_source: UniProtKB reviewed P09870; BRENDA EC 3.4.22.8 organism/accession page

proof_lines:
depending on assay method
pH 7.4, 25°C

substrate: Nalpha-benzoyl-L-Lys methyl ester


organism: Tinospora cordifolia

substrate_name: (S)-norcoclaurine

proof_lines: probably allosteric enzyme, Hill coeffizient 2.6

substrate: (S)-norcoclaurine


organism: Glycine max

substrate_name: 5,7,3'-trihydroxyflavone 7-O-glucoside

substrate: 5,7,3'-trihydroxyflavone 7-O-glucoside


organism: Hordeum vulgare


organism: Oryza sativa

substrate_name: luteolin

assay_conditions_summary: pH 7.5; 310.15 K; buffer 10 mM Tris-HCl

proof_lines: OMT-15, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C

proof_lines: OMT-17, in 10 mM Tris-HCl buffer (pH 7.5), at 37°C

substrate: luteolin


organism: Petroselinum crispum


organism: Zea mays


organism: Homo sapiens

substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


proof_lines:
Hep3B cell, pH 7.0, 37°C
with UDP-glucose
with UDP-N-acetylglucosamine


organism: Mesocricetus auratus

proof_lines: cosubstrate: N-acetyl-D-glucosaminyl-1,2-alpha-6-deoxy- (or-4-O-methyl-) mannosyl-1,6-beta-D-glucosyl-O-(CH2)7-CH3


organism: Rattus norvegicus


organism: Clostridium perfringens


organism: Cupriavidus pinatubonensis

substrate_name: NADH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn1, via UV/VIS-NAD(P)H consumption determination, with NADPH

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHCn1, via product determination per HPLC, with NADPH


organism: Rhodococcus opacus

substrate_name: NADPH

substrate: NADPH


organism: Sinomonas cyclohexanicum

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: Km increases as pH rises from 7.0 to 8.4


enzyme_display_name: oryzin

organism: Aspergillus heteromorphus

substrate_name: azocasein

enzyme: oryzin

substrate: azocasein


organism: Aspergillus melleus

substrate_name: Acetyl-Ala methyl ester

substrate: Acetyl-Ala methyl ester


organism: Aspergillus oryzae

substrate_name: acetyl-L-tyrosine ethyl ester

substrate: acetyl-L-tyrosine ethyl ester


organism: Aspergillus sojae

proof_lines: acetyl-(Ala)2-Phe methyl ester, Aspergillus sojae


organism: Bacillus licheniformis

substrate_name: casein

substrate: casein


proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHRo1CP, UV/VIS-NAD(P)H consumption determination

proof_lines: pH 7.5, 30°C, recombinant enzyme PHBHRo1CP, via UV/VIS-NAD(P)H consumption determination, with NADPH


enzyme_display_name: glutathione peroxidase

substrate_name: Cumene hydroperoxide; Reduced glutathione

enzyme: glutathione peroxidase


substrate_name: glutathione

proof_lines: mutant C2S/C78S/C115S/C156S/C202S, presence of 0.03 mM H2O2, pH 7.4, 37°C

proof_lines: mutant C2S/C78S/C115S/C156S/C202S, presence of 0.10 mM H2O2, pH 7.4, 37°C

proof_lines: mutant C2S/C78S/C115S/C156S/C202S, presence of 3 mM GSH, pH 7.4, 37°C

substrate: glutathione


enzyme_display_name: glutathione oxidase

substrate_name: dithiothreitol

enzyme: glutathione oxidase

substrate: dithiothreitol


substrate_name: L-Cys

substrate: L-Cys


organism: Mus musculus


substrate_name: t-Butylhydroperoxide

substrate: t-Butylhydroperoxide


organism: Pseudoalteromonas sp. ANT506


substrate_name: H2O2; Reduced glutathione

substrate: H2O2; Reduced glutathione


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Chlamydomonas reinhardtii

proof_lines: kcat is 7.4 sec(-1) for the reduction of hydrogen peroxide (with cytosolic thioredoxin) (at 30 degrees Celsius and pH 7.9) (PubMed:19690965). kcat is 7.4 sec(-1) for the reduction of tert-butyl hydroperoxide (with cytosolic thioredoxin) (at


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


substrate_name: bis-(2-hydroxyethyl) disulfide (HEDS)

proof_lines: kcat is 1.2 sec(-1) with bis-(2-hydroxyethyl) disulfide (HEDS) as substrate.

substrate: bis-(2-hydroxyethyl) disulfide (HEDS)


organism: Escherichia coli (strain K12)

substrate_name: phosphoadenosine 5'-phosphosulfate

substrate: phosphoadenosine 5'-phosphosulfate


organism: Aloe vera

substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


organism: Brugia pahangi

substrate_name: linolenic acid hydroperoxide

substrate: linolenic acid hydroperoxide


organism: Haemophilus influenzae


organism: Homo sapiens

substrate_name: GSH

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM PIPES

proof_lines: apparent value, imprinted GSH-selenosubtilisin in the presence of 1 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C

proof_lines: apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM H2O2, in 50 mM PIPES buffer, pH 7.0 at 37°C

proof_lines: apparent value, imprinted GSH-selenosubtilisin in the presence of 2 mM GSH, in 50 mM PIPES buffer, pH 7.0 at 37°C

substrate: GSH


proof_lines: wild type enzyme, in the presence of 2 mM GSH, at 37°C and pH 7.0

proof_lines: wild type enzyme, in the presence of 1 mM GSH, at 37°C and pH 7.0

proof_lines: wild type enzyme, in the presence of 0.2 mM H2O2, at 37°C and pH 7.0


organism: Hyalomma dromedarii

proof_lines:
isoform Gpx2, pH 7.0, 25°C
isoform Gpx1, pH 7.0, 25°C


organism: Lateolabrax japonicus


organism: Lucilia cuprina

substrate_name: cumene peroxide

proof_lines: 27°C, pH 7.0, activity of seleno-glutathione transferase

proof_lines: 27°C, pH 7.0, reaction with H2O2, activity of seleno-glutathione transferase

proof_lines: 27°C, pH 7.0, reaction with cumene peroxide, activity of seleno-glutathione transferase

substrate: cumene peroxide


organism: Oryza sativa

substrate_name: tert-butyl hydroperoxide

substrate: tert-butyl hydroperoxide