proof_lines: pH 7.5, 25°C, recombinant mutant T90A/P72L/A311V/A40V/M229I/T273A/V171L/R182W/F267L


enzyme_display_name: HtrA2 peptidase

organism: Homo sapiens

source_db: oed

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

enzyme: HtrA2 peptidase

source: oed


substrate_name: beta-casein

source_db: brenda

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

mutation_type: substitution

substrate: beta-casein

source: brenda


enzyme_display_name: poly[(R)-3-hydroxyalkanoate] polymerase

organism: Caulobacter vibrioides

assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

enzyme: poly[(R)-3-hydroxyalkanoate] polymerase


enzyme_display_name: methane monooxygenase (soluble)

organism: Methylosinus trichosporium

substrate_name: NADH; H+; Furan; O2

km_display: Not reported

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

assay_conditions_summary: cofactor NAD+

enzyme: methane monooxygenase (soluble)

substrate: NADH; H+; Furan; O2


organism: Arabidopsis thaliana

substrate_name: [histone H3]-N6-methyl-L-lysine4

substrate: [histone H3]-N6-methyl-L-lysine4


substrate_name: H3K4me2 1-21 peptide

proof_lines: pH 7.5, 25°C, recombinant N-terminally truncated KDM1A

proof_lines: recombinant LSD1, initial phase, pH 7.5, 25°C

substrate: H3K4me2 1-21 peptide


organism: Aeromonas caviae

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: pH 8.0, 30°C, recombinant mutant PhaCAcN149S/D171G/S389C


proof_lines: pH 8.0, 30°C, recombinant mutant PhaCAcN149S/D171G/S389V


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


proof_lines: pH 8.0, 30°C, recombinant mutant PhaCAcN149S/D171G (PhaCAc NSDG)


proof_lines: pH 8.0, 30°C, recombinant mutant PhaCAcN149S/D171G/S389T


organism: Ectothiorhodospira shaposhnikovii

assay_conditions_summary: cofactor CoA

proof_lines: based on the assumption that 2 PhaC and 2 PhaE subunits comprise one catalytic site


enzyme_display_name: unsaturated chondroitin disaccharide hydrolase

organism: Pedobacter heparinus

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


enzyme: unsaturated chondroitin disaccharide hydrolase


organism: Streptococcus agalactiae

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


organism: Streptococcus pneumoniae


organism: Streptococcus pyogenes


proof_lines: variant lacking the N-terminal domain, pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme P148A, in the absence of activator peptide BIR2, pH and temperature not specified in the publication

proof_lines: mutant enzyme P148A, in the presence of activator peptide BIR2, pH and temperature not specified in the publication


proof_lines: mutant enzyme F131A, in the presence of activator peptide BIR2, pH and temperature not specified in the publication


proof_lines: wild type enzyme, in the presence of activator peptide BIR2, pH and temperature not specified in the publication

proof_lines: wild type enzyme, in the absence of activator peptide BIR2, pH and temperature not specified in the publication


enzyme_display_name: proteasome endopeptidase complex

organism: Trypanosoma brucei

enzyme: proteasome endopeptidase complex


organism: Mus musculus

substrate_name: N-acetyl-L-tyrosine

kcat_display: Not reported

proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y156A

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y156A

substrate: N-acetyl-L-tyrosine


proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme R67D

proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme R67D


proof_lines: mutant G230A, K0.5 value, presence of inhibitor of apoptosis protein, 37°C, pH 7.8


proof_lines: mutant comprising N-terminal and serine protease domains, pH 8.0, 37°C


mutation_signature: PDZ domain deletion mutant

mutation_type: deletion

proof_lines: PDZ domain deletion mutant, K0.5 value, Hill constant 1.7, 37°C, pH 7.8

proof_lines: PDZ domain deletion mutant, K0.5 value, Hill constant 1.5, presence of inhibitor of apoptosis protein, 37°C, pH 7.8

proof_lines: PDZ domain deletion mutant, K0.5 value, Hill constant 1.4, presence of inhibitor of apoptosis domain BIR2, 37°C, pH 7.8


proof_lines: short natural isoform lacking the N-terminal domain, pH 7.5, temperature not specified in the publication

proof_lines: protease domain, pH 7.5, temperature not specified in the publication


proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y288A

proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y288A


proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme N70A

proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme N70A


proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, wild-type enzyme

proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, wild-type enzyme


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme D235R

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme D235R


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme D114A

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme D114A


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme Y287A

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme Y287A


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E289A

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E289A


proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme R71A

proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme R71A


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E167A

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E167A


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme K290A

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme K290A


proof_lines: pH 7.5, temperature not specified in the publication, activated by Co2+, mutant enzyme E167R

proof_lines: pH 7.5, temperature not specified in the publication, without Co2+, mutant enzyme E167R


substrate_name: acrolein mercapturate; N-acetyl-S-(1,2-dichlorovinyl)-L-cysteine; 4-hydroxy-2-nonenal mercapturate; N-acetyl-L-tyrosine; N-acetyl-L-histidine; N-acetyl-S-benzyl-L-cysteine; N-acetyl-L-phenylalanine; N-acetyl-1,2-dichlorovinyl-L-cysteine

source_db: brenda; skid

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

proof_lines: pH and temperature not specified in the publication, absence of Co2+

proof_lines: pH and temperature not specified in the publication, presence of Co2+

source_databases_merged: brenda skid

source: brenda; skid


substrate_name: H3 monomethyl-K4

source_db: uniprot

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

proof_lines: kcat is 7.35 sec(-1) with H3 monomethyl-K4 as substrate when part of a complex with RCOR1 (at 25 degrees Celsius).

proof_lines: kcat is 5.47 sec(-1) with H3 monomethyl-K4 as substrate when part of a complex with RCOR1 (at 25 degrees Celsius).

proof_lines: kcat is 9.4 sec(-1) with H3 monomethyl-K4 as substrate when part of a complex with RCOR1 (at 25 degrees Celsius).

substrate: H3 monomethyl-K4

source: uniprot


substrate_name: N(6)-methyl-L-lysyl-[histone H3]

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

proof_lines: Kcat is 0.56 min(-1) for N(6)-methyl-L-lysyl(4)-[histone H3] and 1.30 min(-1) for N(6),N(6)-dimethyl-L-lysyl(4)-[histone H3] as substrates.

substrate: N(6)-methyl-L-lysyl-[histone H3]


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: CTP

substrate: CTP


organism: Streptococcus agalactiae serotype III (strain NEM316)

substrate_name: unsaturated chondroitin disaccharidee (delta0S)

mutation_signature: Δ6

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature Δ6 to reconstruct the assayed variant sequence.

proof_lines: kcat is 2.69 sec(-1) with unsaturated chondroitin (delta0S) (PubMed:21147778). kcat is 24 sec(-1) with unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue (delta6S) (PubMed:19416976). kcat is 10.2 sec(-1) with un


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

proof_lines: kcat is 1.3 sec(-1) with unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue.


organism: Streptococcus pyogenes serotype M1

proof_lines: kcat is 4 sec(-1) with unsaturated chondroitin disaccharide sulfated at C-6 position of GalNAc residue.


organism: Rhodococcus erythropolis

substrate_name: Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1 proteasome subtype)

proof_lines: The Vmax observed with the beta2-alpha1 proteasome subtype is 2.2-fold, 1.2-fold and 4-fold higher than that with the beta2-alpha2, beta1-alpha2 and beta1-alpha1 subtypes, respectively.


substrate: Suc-Leu-Leu-Val-Tyr-AMC (with the beta2-alpha1 proteasome subtype)


substrate_name: mono-methylated 'Lys-4' histone H3 N-terminal peptide


organism: Bacillus subtilis (strain 168)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: Suc-LLVY-Amc (at 55 degrees Celsius)

substrate: Suc-LLVY-Amc (at 55 degrees Celsius)


substrate_name: S-benzyl-N-acetyl-L-cysteine

substrate: S-benzyl-N-acetyl-L-cysteine


organism: Methylosinus trichosporium

substrate_name: methane

assay_conditions_summary: cofactor NADH

substrate: methane


organism: Paraburkholderia terrae

substrate_name: hexanoate

proof_lines: pH 7.4, temperature not specified in the publication

substrate: hexanoate


substrate_name: [histone H3 peptide 21mer]-N6-methyl-L-lysine4-methyl-L-arginine17

proof_lines: pH 8.0, 25°C, recombinant wild-type LSD2


organism: Allochromatium vinosum

proof_lines:
30°C, first phase of reaction
recombinant enzyme, pH 7.8, 30°C
30°C, second phase of reaction


organism: Brevundimonas sp. KH11J01

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA


organism: Cupriavidus necator

assay_conditions_summary: pH 7.2; 298.15 K; cofactor CoA

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


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

proof_lines: 25°C, pH 7.0, wild-type enzyme, based on one catalytic site in a dimeric enzyme


proof_lines: 25°C, pH 7.0, mutant enzyme G4D, based on one catalytic site in a dimeric enzyme


organism: Delftia acidovorans

assay_conditions_summary: pH 7; cofactor CoA


organism: Desmonostoc muscorum


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Halopiger aswanensis


organism: Bacillus subtilis

sequence_source: UniProtKB P27623 direct FASTA lookup; accession supported by BRENDA EC/organism page and UniProt PMID 8393871 evidence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature W74A; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature W74A to reconstruct the assayed variant sequence.


sequence_source: Canonical UniProtKB P27623 context only; row-specific D11A/R113A variant sequence not accepted from the selected evidence.

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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature D38A; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature D38A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature C106A; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature C106A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature D11E; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature D11E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature R113K; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature R113K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature T114A; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature T114A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature K103A; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature K103A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature D66E; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature D66E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature R113A; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature R113A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB P27623 using selected mutation signature D38E; accession supported by BRENDA EC/organism page and UniProt evidence. and applied mutation signature D38E to reconstruct the assayed variant sequence.


enzyme_display_name: deacetoxycephalosporin-C hydroxylase

organism: Streptomyces clavuligerus

substrate_name: Penicillin N

enzyme: deacetoxycephalosporin-C hydroxylase

substrate: Penicillin N


substrate_name: penicillin G

substrate: penicillin G


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Methylococcus capsulatus

substrate_name: propylene

assay_conditions_summary: 298.15 K; cofactor NADH

proof_lines:
25°C, purified enzyme
with methane

substrate: propylene


organism: Methylocystis sp.

substrate_name: NADH

assay_conditions_summary: cofactor NADPH

substrate: NADH


organism: Methylomonas methanica

assay_conditions_summary: pH 7.2; 309.15 K; cofactor NADH


substrate_name: glycerol 3-phosphate

substrate: glycerol 3-phosphate


enzyme_display_name: transketolase

organism: Homo sapiens

substrate_name: D-Ribose 5-phosphate; D-Xylulose 5-phosphate

enzyme: transketolase


organism: Mycobacterium tuberculosis

substrate_name: D-ribose 5-phosphate

proof_lines:
pH 7.6, 37°C
pH 7.6, 25°C
Raw SKiD Env: Temp=37°C, pH=7.6

substrate: D-ribose 5-phosphate


substrate_name: H2O; D-Fructose 6-phosphate; Hexacyanoferrate(III)


enzyme_display_name: L-lysine N(6)-monooxygenase (NADPH)

organism: Nocardia farcinica

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: pH 7.5, 25°C, cosubstrate L-lysine, wild-type enzyme, determined by by measuring oxygen consumption

enzyme: L-lysine N(6)-monooxygenase (NADPH)

substrate: NADPH


proof_lines: pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme M239R, determined by by measuring oxygen consumption


proof_lines: pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme E216Q, determined by by measuring oxygen consumption


proof_lines: pH 7.5, 25°C, cosubstrate L-lysine, mutant enzyme R301A, determined by by measuring oxygen consumption


substrate_name: Glyceraldehyde 3-phosphate; D-Sedoheptulose 7-phosphate


organism: Geobacillus stearothermophilus

substrate_name: L-glyceraldehyde

proof_lines:
Km above 300 mM, at pH 7.2 and 50°C
at pH 7.5 and 25°C
at pH 7.5 and 50°C

substrate: L-glyceraldehyde


substrate_name: D-xylulose 5-phosphate

proof_lines: His-tagged recombinant enzyme, pH 7.6, 30°C

substrate: D-xylulose 5-phosphate


substrate_name: CTP


proof_lines: E39A mutant, D11E mutant and D38E mutant


organism: Saccharomyces cerevisiae

substrate: D-Ribose 5-phosphate; D-Xylulose 5-phosphate


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-erythrose 4-phosphate

substrate: D-erythrose 4-phosphate


substrate_name: D-Xylulose 5-phosphate

substrate: D-Xylulose 5-phosphate


proof_lines: with excess D-xylose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

proof_lines: with excess D-ribose 5-phosphate as cosubstrate, at pH 7.5 and 37°C

proof_lines: with excess D-erythrose 4-phosphate as cosubstrate, at pH 7.5 and 37°C


organism: Scheffersomyces stipitis

proof_lines: mutant enzyme H27A, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C


substrate_name: sedoheptulose 7-phosphate

substrate: sedoheptulose 7-phosphate


substrate_name: D-Fructose 6-phosphate

substrate: D-Fructose 6-phosphate


proof_lines: mutant enzyme R525L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C


organism: Taxus cuspidata


proof_lines:
wild-type enzyme, pH 5.5, 37.5°
wild-type enzyme, pH 5.5, 37.5°C


organism: Taxus mairei

substrate_name: vinyl acetate

substrate: vinyl acetate


smiles: C=COC(C)=O


substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.2; 310.15 K; cofactor CoA

substrate: acetyl-CoA


proof_lines: mutant enzyme G38R/F301V, pH 5.5, 37.5°C


proof_lines: wild type enzyme, with D-erythrose 4-phosphate as cosubstrate, at pH 8.0 and 25°C

proof_lines: wild type enzyme, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Spinacia oleracea


organism: Vibrio vulnificus

substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: alpha-glucuronidase

organism: Bacteroides ovatus

substrate_name: beechwood xylan

proof_lines: recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate

enzyme: alpha-glucuronidase

substrate: beechwood xylan


organism: Paenibacillus curdlanolyticus


organism: Saccharophagus degradans

substrate_name: birchwood xylan

substrate: birchwood xylan


enzyme_display_name: protocatechuate 4,5-dioxygenase

organism: Sphingobium sp.

enzyme: protocatechuate 4,5-dioxygenase


substrate_name: protocatechuate

substrate: protocatechuate


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


organism: Medicago truncatula

substrate_name: naringenin 7-O-neohesperidoside

substrate: naringenin 7-O-neohesperidoside


substrate_name: naringenin 7-O-glucoside

substrate: naringenin 7-O-glucoside


substrate_name: malonyl-CoA

substrate: malonyl-CoA


enzyme_display_name: carnitine O-octanoyltransferase

organism: Bos taurus

substrate_name: palmitoyl-CoA

proof_lines:
mutant SAA-COT
mutant ATS-COT
mutant ATA-COT

enzyme: carnitine O-octanoyltransferase

substrate: palmitoyl-CoA


organism: Glycine max

substrate_name: daidzein 7-O-glucoside

assay_conditions_summary: pH 7.2; 303.15 K; cofactor CoA

proof_lines: cosubstrate genistein 7-O-glucoside, pH 7.2, 30°C

substrate: daidzein 7-O-glucoside


substrate_name: glycitein 7-O-glucoside

substrate: glycitein 7-O-glucoside


organism: Comamonas testosteroni


organism: Pseudarthrobacter phenanthrenivorans


substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


organism: Homo sapiens

substrate_name: propionyl-CoA

proof_lines: pH and temperature not specified in the publication

substrate: propionyl-CoA


organism: Rattus norvegicus

proof_lines: recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340A/H131


substrate_name: L-carnitine

substrate: L-carnitine


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: D-Ribose 5-phosphate

substrate: D-Ribose 5-phosphate


organism: Scheffersomyces stipitis

substrate_name: D-xylulose 5-phosphate

proof_lines: mutant enzyme R356L, with D-ribose 5-phosphate as cosubstrate, at pH 8.0 and 25°C

substrate: D-xylulose 5-phosphate


substrate_name: genistein 7-O-glucoside

substrate: genistein 7-O-glucoside


enzyme_display_name: NAD(+) ADP-ribosyltransferase

organism: Aeromonas hydrophila

substrate_name: NAD+

assay_conditions_summary: 298.15 K; cofactor NAD+

proof_lines: mutant E215A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication

proof_lines: mutant E215A, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: mutant E215A, 25°C, pH not specified in the publication

enzyme: NAD(+) ADP-ribosyltransferase

substrate: NAD+


substrate_name: (ADP-D-ribosyl)n-actin

proof_lines: mutant S178A, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: mutant S178A, 25°C, pH not specified in the publication

substrate: (ADP-D-ribosyl)n-actin


substrate_name: Unknown

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

substrate: Unknown


proof_lines: mutant Y82A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication

proof_lines: mutant Y82A, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: mutant Y82A, 25°C, pH not specified in the publication


organism: Streptomyces scabiei

assay_conditions_summary: pH 7.9; 295.15 K; cofactor NAD+


proof_lines: mutant enzyme Q158A/E160A, at pH 7.9 and 22°C


enzyme_display_name: thiamine pyridinylase

organism: Paenibacillus thiaminolyticus

substrate_name: thiamine

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.2
Raw SKiD Env: Temp=-----, pH=-----

enzyme: thiamine pyridinylase

substrate: thiamine


organism: Mus musculus

substrate_name: UDP-N-acetyl-D-glucosamine

proof_lines: mutant enzyme C217S, in 50 mM Tris (pH 7.5), at 37°C

substrate: UDP-N-acetyl-D-glucosamine


proof_lines: mutant N86A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication

proof_lines: mutant N86A, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: mutant N86A, 25°C, pH not specified in the publication


proof_lines: wild-type, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication

proof_lines: wild-type, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: wild-type, 25°C, pH not specified in the publication


proof_lines: mutant S178, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication


organism: Taxus mairei

substrate_name: vinyl acetate

substrate: vinyl acetate


substrate_name: acetyl-CoA

proof_lines: wild-type enzyme, 30°C, pH not specified in the publication

substrate: acetyl-CoA


assay_conditions_summary: 303.15 K; cofactor CoA

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


enzyme_display_name: protein geranylgeranyltransferase type I

proof_lines: pH and temperature not specified in the publication


substrate_name: dansyl-GCII

enzyme: protein geranylgeranyltransferase type I

substrate: dansyl-GCII


substrate_name: birchwood xylan

substrate: birchwood xylan


organism: Thermotoga maritima


enzyme_display_name: oxaloacetase

organism: Botrytis cinerea

substrate_name: oxaloacetate

proof_lines:
mutant S260A, trial 1
mutant S260A, trial 2
mutant S260A

enzyme: oxaloacetase

substrate: oxaloacetate


organism: Cryphonectria parasitica

proof_lines:
in presence of Ca2+, pH 7.5, 25°C
in presence of Mn2+, pH 7.5, 25°C
in presence of Mg2+, pH 7.5, 25°C


enzyme_display_name: aldehyde oxygenase (deformylating)

organism: Synechococcus elongatus

substrate_name: n-Heptanal

proof_lines: pH 7.2, 22°C, recombinant enzyme with Fd/FNR system

enzyme: aldehyde oxygenase (deformylating)

substrate: n-Heptanal


organism: Synechococcus elongatus PCC 7942 = FACHB-805

substrate_name: n-nonanal

smiles: CCCCCCCCC=O

substrate: n-nonanal


proof_lines: mutant Y77A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication

proof_lines: mutant Y77A, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: mutant Y77A, 25°C, pH not specified in the publication


proof_lines: mutant E213A, co-substrate: (ADP-D-ribosyl)n-actin, 25°C, pH not specified in the publication

proof_lines: mutant E213A, co-substrate: NAD+, 25°C, pH not specified in the publication

proof_lines: mutant E213A, 25°C, pH not specified in the publication


assay_conditions_summary: cofactor NAD+


assay_conditions_summary: buffer notes and no selected-batch kinetic fields

proof_lines:
cofactor Mg2+, buffer imidazole
cofactor Mn2+, buffer imidazole
cofactor Mg2+, buffer Hepes


proof_lines:
mutant S260P, trial 2
mutant S260P, trial 1
mutant S260P


proof_lines:
mutant S260T, trial 1
mutant S260T, trial 2


organism: Paenibacillus larvae subsp. larvae

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+


substrate_name: n-hexanal

smiles: CCCCCC=O

substrate: n-hexanal


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

proof_lines: pH 7.2, 37°C, recombinant wild-type enzyme and mutant A121F


smiles: CCCCCCC=O


organism: Synechocystis sp. PCC 6803

substrate_name: n-hexadecanal

proof_lines: recombinant mutant D49H, pH and temperature not specified in the publication

substrate: n-hexadecanal


proof_lines: recombinant mutant T146L, pH and temperature not specified in the publication


proof_lines: recombinant mutant L148R, pH and temperature not specified in the publication


proof_lines: recombinant mutant D49H/N123H, pH and temperature not specified in the publication


substrate_name: n-octanal

smiles: CCCCCCCC=O

substrate: n-octanal


proof_lines: recombinant mutant W178R, pH and temperature not specified in the publication


proof_lines: recombinant mutant Q110L, pH and temperature not specified in the publication


proof_lines: recombinant mutant Q49H/F150Y, pH and temperature not specified in the publication


proof_lines: recombinant mutant Y39F, pH and temperature not specified in the publication


proof_lines: recombinant mutant Y122F, pH and temperature not specified in the publication


proof_lines: recombinant mutant Q49H/N123H/F150Y, pH and temperature not specified in the publication


proof_lines: recombinant mutant F150Y, pH and temperature not specified in the publication


proof_lines: recombinant mutant N123H, pH and temperature not specified in the publication


proof_lines: recombinant mutant R62A, pH and temperature not specified in the publication


substrate_name: n-hexadecanal; n-Heptanal

proof_lines: recombinant mutant L146T, pH and temperature not specified in the publication

substrate: n-hexadecanal; n-Heptanal


proof_lines: recombinant mutant D143A, pH and temperature not specified in the publication


proof_lines: recombinant mutant N149A, pH and temperature not specified in the publication


proof_lines: recombinant mutant Y150F, pH and temperature not specified in the publication


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


enzyme_display_name: maltose phosphorylase

organism: Salisediminibacterium selenitireducens

substrate_name: kojibiose

proof_lines:
pH 6.5, 30°C, reverse phosphorolysis
pH 6.5, 30°C
pH 6.5, 30°C, phosphorolysis

enzyme: maltose phosphorylase

substrate: kojibiose


organism: Unknown


organism: Dianthus caryophyllus

substrate_name: (R)-citramalate (at pH 7.5 and 25 degrees Celsius)


enzyme_display_name: L-ascorbate oxidase

organism: Triticum aestivum

substrate_name: L-ascorbate

enzyme: L-ascorbate oxidase

substrate: L-ascorbate


organism: Comamonas testosteroni

substrate_name: protocatechuate

substrate: protocatechuate


organism: Rhizobium leguminosarum


organism: Escherichia coli

substrate_name: FAD

assay_conditions_summary: pH 7; 310.15 K; cofactor FAD

substrate: FAD


proof_lines: parent enzyme protein rIucD and genetically engineered forms C51A rIucD, C51A/C158A rIucD and C158A rIucD


substrate_name: NADPH

mutation_signature: with a deletion of 47 amino acids in the N-terminus recombinant enzyme form IucD398 / with a deletion of 47 amino acids in the N-terminus

proof_lines: recombinant enzyme form IucD398, with a deletion of 47 amino acids in the N-terminus

substrate: NADPH


organism: Mycolicibacterium smegmatis

substrate_name: L-lysine

proof_lines:
pH 7.5, 25°C, with NADPH
pH 7.5, 25°C
pH 7.5, 25°C, with NADH

substrate: L-lysine


organism: Nocardia farcinica

proof_lines: pH 7.5, 25°C, recombinant mutant K64A, with NADPH

proof_lines: pH 7.5, 25°C, recombinant mutant K64A, with NADH


proof_lines: pH 7.5, 25°C, recombinant mutant P238R, with NADPH

proof_lines: pH 7.5, 25°C, recombinant mutant P238R, O2 consumption

proof_lines: pH 7.5, 25°C, recombinant mutant P238R, L-lysine hydroxylation


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

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

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


organism: Bacillus methanolicus

substrate_name: D-fructose 6-phosphate

proof_lines:
isoform TKTc, at pH 7.5 and 55°C
isoform TKTp, at pH 7.7 and 55°C

substrate: D-fructose 6-phosphate


organism: Cereibacter sphaeroides

substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


proof_lines:
wild-type, pH 8.5, 25°C
wild-type, pH 6.7, 25°C
wild-type, pH 7.8, 25°C


organism: Geobacillus stearothermophilus

substrate_name: L-erythrulose (at 25 degrees Celsius)

substrate: L-erythrulose (at 25 degrees Celsius)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ribose 5-phosphate

assay_conditions_summary: pH 7

substrate: ribose 5-phosphate


organism: Staphylococcus aureus (strain N315)

substrate_name: fructose 6-phosphate (at pH 7.0 and 37 degrees Celsius)


organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)

substrate: fructose 6-phosphate (at pH 7.0 and 37 degrees Celsius)


organism: Vibrio vulnificus (strain YJ016)

substrate_name: thiamine diphosphate (at pH 7.0 and 37 degrees Celsius)


organism: Zea mays


organism: Homo sapiens

substrate_name: acetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetyl-CoA


organism: Mus musculus

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Saccharolobus solfataricus

substrate_name: NAD(+)

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

substrate: NAD(+)


organism: Arabidopsis thaliana

substrate_name: CVIM substrate and for farnesyl transferase activity


organism: Acremonium

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


organism: Acremonium sp.

substrate_name: O2; Ascorbate

verification_status: unverified

substrate: O2; Ascorbate

status: unverified


organism: Aspergillus flavus


organism: Brassica oleracea

proof_lines: enzyme from soluble fraction and cell-wall preparation


organism: Cucumis sativus

proof_lines:
spectrophotometric method
Warburg method
at 25°C


organism: Cucurbita maxima

proof_lines:
O2 consumption, polarographic method
pH 6.0, 25°C
spectrophotometric assay


organism: Cucurbita pepo condensa

proof_lines:
manometric assay
spectrometric assay
spectrophotometric method


organism: Cucurbita pepo medullosa

assay_conditions_summary: pH 6

proof_lines: commercial enzyme preparation from Sigma

proof_lines: activity in media of 10 days old cell culture


organism: Cucurbita sp.

substrate_name: chlorohydroquinone

substrate: chlorohydroquinone


substrate_name: L-ascorbate

proof_lines: pH and temperature not specified in the publication


organism: Lagenaria siceraria

proof_lines: immobilized ascorbate oxidase, at pH 6.0 and 40°C

proof_lines: free ascorbate oxidase, at pH 5.5 and 40°C


organism: Pleurotus ostreatus


enzyme_display_name: peptidoglycan glycosyltransferase

organism: Escherichia coli

enzyme: peptidoglycan glycosyltransferase


organism: Paenibacillus sp.

substrate_name: maltose

substrate: maltose


substrate_name: beta-D-glucose 1-phosphate

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

substrate: beta-D-glucose 1-phosphate


organism: Salisediminibacterium selenitireducens

substrate_name: kojibiose

substrate: kojibiose


substrate_name: sophorose

substrate: sophorose


substrate_name: glycolaldehyde

proof_lines: mutant A29E, in the presence of 50 mM hydroxypyruvate

proof_lines: mutant A29E, in the presence of 50 mM glycolaldehyde

substrate: glycolaldehyde


substrate_name: propionaldehyde

proof_lines: wild-type, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0

proof_lines: wild-type, in the presence of 50 mM glycolaldehyde

proof_lines: wild-type, in the presence of 50 mM hydroxypyruvate

substrate: propionaldehyde


substrate_name: lithium beta-hydroxypyruvate

substrate: lithium beta-hydroxypyruvate


substrate_name: 4-formylbenzoic acid

proof_lines: mutant enzyme D469T/R520Q, at pH 7.0 and 22°C

substrate: 4-formylbenzoic acid


proof_lines: mutant enzyme S385T/D469T/R520Q, at pH 7.0 and 22°C


proof_lines: mutant D469T, in the presence of 50 mM Li-hydroxypyruvate, 50 mM propionaldehyde, and 50 mM Tris-HCl, 2.4 mM thiamine diphosphate, 9 mM MgCl2, pH 7.0


proof_lines: mutant enzyme S385E/D469T/R520Q, at pH 7.0 and 22°C


substrate_name: 3-formylbenzoic acid

proof_lines: mutant enzyme S385Y/D469T/R520Q, at pH 7.0 and 22°C

substrate: 3-formylbenzoic acid


organism: Homo sapiens

substrate_name: D-ribose 5-phosphate

proof_lines: presence of 2 mM D-ribose 5-phosphate, pH 7.6, temperature not specified in the publication

substrate: D-ribose 5-phosphate


organism: Mus musculus

substrate_name: thiamine diphosphate

proof_lines:
cosubstrate D-xylulose 5-phosphate
(+ D-ribose 5-phosphate)

substrate: thiamine diphosphate


organism: Oryctolagus cuniculus


enzyme_display_name: mitochondrial processing peptidase

enzyme: mitochondrial processing peptidase


organism: Saccharomyces cerevisiae

substrate_name: MLSALARPVGAALRRSFSTSA; H2O

substrate: MLSALARPVGAALRRSFSTSA; H2O


enzyme_display_name: chitin synthase

organism: Phytophthora sojae

substrate_name: Unknown

enzyme: chitin synthase

substrate: Unknown


enzyme_display_name: lysophospholipase

enzyme: lysophospholipase


substrate_name: 1-palmitoyl lysophosphatidylcholine

proof_lines:
for lysophospholipase activity
for acylprotein thioesterase activity

substrate: 1-palmitoyl lysophosphatidylcholine


organism: Plasmodium falciparum

substrate_name: lysophosphatidylcholine

assay_conditions_summary: pH 8

proof_lines: pH 8, temperature not specified in the publication

substrate: lysophosphatidylcholine


organism: Unknown

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


enzyme_display_name: D-Ala-D-Ala dipeptidase

substrate_name: D-Ala-D-Ala

enzyme: D-Ala-D-Ala dipeptidase

substrate: D-Ala-D-Ala


enzyme_display_name: phosphate butyryltransferase

organism: Clostridium acetobutylicum

substrate_name: Phosphate; Butanoyl-CoA

enzyme: phosphate butyryltransferase

substrate: Phosphate; Butanoyl-CoA


organism: Thermococcus kodakarensis

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


enzyme_display_name: cyclic-di-AMP phosphodiesterase

organism: Bacillus subtilis

substrate_name: cyclic di-3',5'-adenylate

proof_lines: pH 8.3, temperature not specified in the publication

enzyme: cyclic-di-AMP phosphodiesterase

substrate: cyclic di-3',5'-adenylate


organism: Mycolicibacterium smegmatis

proof_lines:
pH 7.8, 37°C
Raw SKiD Env: Temp=37°C, pH=7.8


organism: Staphylococcus aureus

proof_lines: pH 8.0, 37°C, presence of 0.02 mM 5-O-phosphonoadenylyl-(3->5)-adenosine


organism: Streptococcus pneumoniae D39


organism: Streptococcus suis

substrate_name: ADP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: ADP


enzyme_display_name: transketolase

organism: Escherichia coli (strain K12)

substrate_name: D-xylulose 5-phosphate

proof_lines: kcat is 51.3 sec(-1) with thiamine diphosphate as a cofactor, D-xylulose 5-phosphate as donor substrate and D-ribose 5-phosphate as the acceptor substrate (PubMed:32839604). kcat is 1.9 sec(-1) with 2'-methoxy thiamine diphosphate as a cofa

enzyme: transketolase

substrate: D-xylulose 5-phosphate


substrate_name: D-xylulose 5-phosphate (recombinant enzyme with C-terminal hexahistidine tag at pH 7.6 and 30 degrees Celsius)

proof_lines: kcat is 3.1 sec(-1) with D-xylulose 5-phosphate as substrate (recombinant enzyme with C-terminal hexahistidine tag at pH 7.6 and 30 degrees Celsius) (PubMed:20667822). kcat is 6.3 sec(-1) with D-xylulose 5-phosphate as substrate (recombinan


organism: Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545)

substrate_name: xylulose 5-phosphate with ribose 5-phosphate as the aldose acceptor (at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 25.3 sec(-1) with xylulose 5-phosphate and ribose 5-phosphate as substrates (at pH 8.0 and 25 degrees Celsius) (PubMed:27578891). kcat is 18.0 sec(-1) with xylulose 5-phosphate and erythrose 4-phosphate as substrates (at pH 8.0 and


substrate_name: NAD(+)

substrate: NAD(+)


organism: Streptococcus pneumoniae (strain ATCC BAA-255 / R6)

substrate_name: dansylated lipid II

proof_lines: kcat is greater than 0.0005 sec(-1) with dansylated lipid II as substrate (PubMed:22487093). kcat/KM is 0.001 M(-1)sec(-1) with dansylated lipid II as substrate (PubMed:12867450).

substrate: dansylated lipid II


organism: Paenibacillus thiaminolyticus

substrate_name: thiamine

substrate: thiamine


organism: Arabidopsis thaliana

substrate_name: CVIM substrate

proof_lines: kcat is 0.5 h(-1), 0.08 h(-1), 0.008 h(-1) and 0.012 h(-1) for CVIL, CVII, CVIQ and CVIM substrates, respectively.

substrate: CVIM substrate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: geranylgeranyl diphosphate

proof_lines: kcat is 0.34 sec(-1) with dansyl-GCIIL as substrate (PubMed:9109664). kcat is 4.8 sec(-1) with GST-CAIL as substrate (PubMed:10491163).

substrate: geranylgeranyl diphosphate


proof_lines: kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as


organism: Homo sapiens

substrate_name: Unknown

proof_lines: The specific activity is 0.8 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphoethanolamine as substrate. The specific activity is 0.3 nmol/min/ug enzyme with 1-hexadecanoyl-2-(9Z,12Z-octadecadien

proof_lines: The specific activity is 2.1 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine as substrate. The specific activity is 0.6 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetr


organism: Mus musculus

proof_lines: The specific activity is 394 nmol/min/ug enzyme with 1-hexadecanoyl-sn-glycero-3-phosphocholine. The specific PLA2 activity is 11 nmol/min/ug enzyme with 1-hexadecanoyl-2-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphocholine (in the


organism: Bacillus subtilis (strain 168)

substrate_name: c-di-AMP

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 0.55 sec(-1) for the phosphodiesterase activity with c-di-AMP as substrate. kcat is 0.23 sec(-1) for the phosphodiesterase activity with c-di-GMP as substrate. kcat is 0.59 min(-1) for the ATPase activity.

substrate: c-di-AMP


organism: Plasmodium falciparum


organism: Rattus norvegicus

proof_lines:
(+ D-ribose 5-phosphate)
cosubstrate D-xylulose 5-phosphate


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


organism: Saccharomyces cerevisiae

proof_lines: mutant E418A, cofactor thiamine diphosphate, 25°C, pH 7.6

proof_lines: mutant E418A, cofactor N1’-methyl-thiamine diphosphate, 25°C, pH 7.6


proof_lines: and second value 0.773 mM, pH 7.6, presence of 0.1 mM Ca2+, temperature not specified in the publication

proof_lines: pH 7.6, 25°C, affinity to the first active center when the second center is unoccupied


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Enterococcus faecium


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

organism: Ensifer adhaerens

substrate_name: N-carbamoyl-D-p-hydroxyphenylglycine

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

substrate: N-carbamoyl-D-p-hydroxyphenylglycine


organism: Nitratireductor indicus

substrate_name: N-carbamoyl-D-Trp

substrate: N-carbamoyl-D-Trp


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

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

data_origin: experimental

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Rhizopus delemar (strain RA 99-880 / ATCC MYA-4621 / FGSC 9543 / NRRL 43880)


substrate: Unknown


enzyme_display_name: dynamin GTPase

organism: Bos taurus

substrate_name: GTP

enzyme: dynamin GTPase

substrate: GTP


substrate_name: GTP (for basal GTPase activity)

substrate: GTP (for basal GTPase activity)


enzyme_display_name: scopoletin glucosyltransferase

substrate_name: scopoletin

proof_lines: wild type, 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30°C

enzyme: scopoletin glucosyltransferase

substrate: scopoletin


proof_lines: 71C1/71C3 chimera including N-terminus of 71C1 (position 1-261) and C-terminus of 71C3 (position 256-476), 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30°C


proof_lines: 71C1 double mutant, 50 mM Tris-HCl, pH 7.0, 14 mM 2-mercaptoethanol, 30°C


organism: Canis lupus familiaris


organism: Cricetulus griseus

substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


organism: Gallus gallus


proof_lines: CaCo-2, colonic adenocarcinoma, cells differentiated to enterocytes


proof_lines:
pH 6.7, 37°C, mutant enzyme C217S
mutant enzyme C217S


proof_lines:
pH 6.7, 37°C, wild-type enzyme
wild-type enzyme


organism: Sus scrofa


organism: Catharanthus roseus

substrate_name: UDP-glucose

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

substrate: UDP-glucose


enzyme_display_name: carnitine O-octanoyltransferase

substrate_name: octanoyl-CoA

enzyme: carnitine O-octanoyltransferase

substrate: octanoyl-CoA


substrate_name: acyl-CoA

proof_lines: mutant strain expressed in Saccharomyces cerevisiae COT A238D

substrate: acyl-CoA


substrate_name: decanoyl-CoA

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: recombinant enzyme expressed in Saccharomyces cerevisiae pYESCOTH340A/H131

substrate: decanoyl-CoA


organism: Taxus baccata

substrate_name: 10-deacetylbaccatin III

proof_lines: recombinant enzyme with a hexahistidine fusion tag

substrate: 10-deacetylbaccatin III


organism: Taxus cuspidata


organism: Cuphea wrightii

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

proof_lines: pH 7.6, 30°C, recombinant His-tagged wild-type enzyme

substrate: acetyl-CoA


organism: Escherichia coli

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

proof_lines: pH 7.0, 25°C, recombinant enzyme from Brassica napus seeds


organism: Staphylococcus aureus

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines:
pH 7.0, 30°C, recombinant enzyme
pH 7.2, 30°C, recombinant enzyme


organism: Streptomyces glaucescens

substrate_name: isobutyryl-CoA

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

substrate: isobutyryl-CoA


organism: Clostridium acetobutylicum

substrate_name: Butanoylphosphate

substrate: Butanoylphosphate


organism: Clostridium beijerinckii

substrate_name: butanoyl-CoA

proof_lines:
cosubstrate butyryl-CoA
cosubstrate acetoacetyl-CoA

substrate: butanoyl-CoA


organism: Listeria monocytogenes

substrate_name: hexanoyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: hexanoyl-CoA


organism: Lathyrus oleraceus

substrate_name: malonyl-[acyl-carrier protein]

substrate: malonyl-[acyl-carrier protein]


substrate_name: isovaleryl-CoA

assay_conditions_summary: 283.15 K; cofactor CoA

substrate: isovaleryl-CoA


organism: Streptococcus pneumoniae

assay_conditions_summary: pH 7; cofactor CoA


organism: Streptomyces antibioticus

substrate_name: cyclohexonyl-N-acetylcysteamine

substrate: cyclohexonyl-N-acetylcysteamine


organism: Escherichia coli (strain K12)


organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)


enzyme_display_name: 3-oxoacid CoA-transferase

substrate_name: acetoacetyl-CoA

enzyme: 3-oxoacid CoA-transferase

substrate: acetoacetyl-CoA


substrate_name: grouped: acetoacetate; acetoacetyl-CoA; succinyl-CoA; succinate


substrate_name: grouped: acetoacetyl-CoA; acetoacetate; succinyl-CoA; succinate


substrate_name: grouped: acetoacetate; acetoacetyl-CoA; succinate; succinyl-CoA


organism: Nicotiana benthamiana

substrate_name: N-4-trans-coumaroyl tyramine

substrate: N-4-trans-coumaroyl tyramine


organism: Amylomyces rouxii

substrate_name: Unknown

substrate: Unknown


organism: Aspergillus flavus

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


organism: Aspergillus nidulans


organism: Botrytis cinerea


organism: Candida tropicalis

substrate_name: UDP-N-acetyl-alpha-D-glucosamine

substrate: UDP-N-acetyl-alpha-D-glucosamine


organism: Choanephora cucurbitarum


organism: Coprinopsis cinerea


organism: Kluyveromyces bulgaricus

substrate_name: 6-O-dansyl N-acetylglucosamine

proof_lines:
chitin synthetase II
chitin synthetase III
chitin synthetase I

substrate: 6-O-dansyl N-acetylglucosamine


organism: Mortierella candelabrum


organism: Mortierella pusilla


organism: Neocallimastix frontalis


organism: Listeria monocytogenes serotype 1/2a (strain 10403S)

substrate_name: 2-methylbutanoyl-CoA (at 30 degrees Celsius)

proof_lines: kcat is 27.5 min(-1) (at 30 degrees Celsius) and 2.8 min(-1) (at 10 degrees Celsius) with 2-methylbutanoyl-CoA as substrate. kcat is 19.0 min(-1) (at 30 degrees Celsius) and 6.1 min(-1) (at 10 degrees Celsius) with 2-methylpropanoyl-CoA as


organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)

substrate_name: 2-methylpropanoyl-CoA (in the presence of malonyl-FabC)

proof_lines: kcat is 17.17 min(-1) with 2-methylpropanoyl-CoA as substrate (in the presence of malonyl-FabC) (PubMed:22136753). kcat is 1.72 min(-1) with acetyl-CoA as substrate (in the presence of malonyl-FabC) (PubMed:22136753). kcat is 0.66 min(-1) w


substrate_name: acetyl-CoA

proof_lines: kcat is 1.52 min(-1) with acetyl-CoA as substrate (PubMed:22136753). kcat is 0.92 min(-1) with malonyl-RedQ as substrate (PubMed:22136753).


organism: Streptomyces lividans

substrate_name: propanoyl-CoA

proof_lines: kcat is 74 min(-1) with propanoyl-CoA as substrate. kcat is 113 min(-1) with butanoyl-CoA as substrate. kcat is 58 min(-1) with acetyl-CoA as substrate.

substrate: propanoyl-CoA


organism: Enterococcus faecium

substrate_name: D-Ala-D-Ala (in the absence of divalent cations)

proof_lines: kcat is 4.7 sec(-1) with D-Ala-D-Ala. kcat is 1.8 sec(-1) with D-Ala-D-Ser. kcat is 0.35 sec(-1) with D-Ser-D-Ala. kcat is 0.005 sec(-1) with D-Ala-D-lactate.


organism: Enterococcus gallinarum

proof_lines: kcat is 131.7 min(-1) with D-Ala-D-Ala as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:24711382). kcat is 27.7 min(-1) with UDP-MurNAc-L-Ala-D-Glu-L-Lys-D-Ala-D-Ala as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:24711382).


organism: Escherichia coli (strain K12)

substrate_name: D-Ala-D-Ala

proof_lines: kcat is 170 sec(-1) with D-Ala-D-Ala. kcat is 70 sec(-1) with L-Ala-D-Ala.

substrate: D-Ala-D-Ala


organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

proof_lines: kcat is 310 sec(-1) with D-Ala-D-Ala. kcat is 110 sec(-1) with L-Ala-D-Ala.


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

organism: Paenarthrobacter aurescens

proof_lines: kcat is 5.1 sec(-1) with L-carbamoyl-L-tryptophan as substrate. kcat is 6.5 sec(-1) with N-carbamoyl-L-tyrosine as substrate. kcat is 5.0 sec(-1) with N-carbamoyl-D,L-phenylalanine as substrate. kcat is 16.1 sec(-1) with N-carbamoyl-L-thien

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


organism: Rhizobium meliloti

substrate_name: N-carbamoyl-L-tryptophan (at 40 degrees Celsius and pH 8.0)

proof_lines: kcat is 91.66 sec(-1) with N-formyl-L-methionine as substrate (at 40 degrees Celsius and pH 8.0). kcat is 66.84 sec(-1) with N-acetyl-L-methionine as substrate (at 40 degrees Celsius and pH 8.0). kcat is 16.9 sec(-1) with N-carbamoyl-L-vali


organism: Nostoc punctiforme (strain ATCC 29133 / PCC 73102)

substrate_name: GTP

substrate: GTP


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.43 min(-1) with GTP substrate.


organism: Saccharomyces cerevisiae

substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


substrate_name: D-ribose 5-phosphate

substrate: D-ribose 5-phosphate


substrate_name: 2-deoxy-D-ribose 5-phosphate

proof_lines: wild-type, cofactor 4’-methylamino-thiamine diphosphate, 25°C, pH 7.6

proof_lines: wild-type, cofactor N1’-methyl-thiamine diphosphate, 25°C, pH 7.6

substrate: 2-deoxy-D-ribose 5-phosphate


organism: Thermotoga maritima

substrate_name: lithium hydroxypyruvate

substrate: lithium hydroxypyruvate


organism: Trypanosoma brucei


organism: Cicer arietinum

substrate_name: apigenin 7-O-glucoside

substrate: apigenin 7-O-glucoside


organism: Petroselinum crispum

substrate_name: luteolin 7-O-glucoside

substrate: luteolin 7-O-glucoside


organism: Bos taurus

substrate_name: decanoyl-CoA

substrate: decanoyl-CoA


enzyme_display_name: thiamine pyridinylase

organism: Pteridium esculentum

substrate_name: nicotinic acid

enzyme: thiamine pyridinylase

substrate: nicotinic acid


organism: Velesunio ambiguus

substrate_name: aniline

proof_lines: lower maximal activity than pyridine and nicotinic acid

substrate: aniline


enzyme_display_name: protein geranylgeranyltransferase type I

proof_lines: prenyl donor: geranylgeranyl diphosphate


organism: Escherichia coli

substrate_name: Thr-Lys-Cys-Val-Ile-Ile

proof_lines: in 50 mM Tris-HCl, 5 mM dithiothreitol, 5 mM MgCl2, and 0.01 mM ZnCl2

enzyme: protein geranylgeranyltransferase type I

substrate: Thr-Lys-Cys-Val-Ile-Ile


organism: Homo sapiens

substrate_name: GST-RhoA

proof_lines:
at 30°C
pH 7.5, 37°C

substrate: GST-RhoA


organism: Rattus norvegicus

substrate_name: geranylgeranyl diphosphate

proof_lines:
pH 7.6, 30°C
pH 7.7, 30°C
with respect to Ras-Cys-Val-Leu-Leu

substrate: geranylgeranyl diphosphate


proof_lines: with respect to geranylgeranyl diphosphate


enzyme_display_name: phosphoglycerate kinase (GTP)

organism: Entamoeba histolytica

proof_lines: recombinant purified mutant Y239F/E309M, at 37°C, pH 7.0

enzyme: phosphoglycerate kinase (GTP)


substrate_name: GDP

proof_lines: recombinant purified mutant Y239F, at 37°C, pH 7.0

substrate: GDP


proof_lines: wild-type, in cytosolic-enriched cellular extracts, at 37°C, pH 7.0

proof_lines: recombinant purified wild-type, at 37°C, pH 7.0


proof_lines: recombinant purified mutant E309Q, at 37°C, pH 7.0


proof_lines: recombinant purified mutant E309M, at 37°C, pH 7.0


proof_lines: recombinant purified mutant V311L, at 37°C, pH 7.0


substrate_name: Glycerate 1,3-bisphosphate; GDP

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

substrate: Glycerate 1,3-bisphosphate; GDP


organism: Bacillus subtilis

substrate_name: CTP

substrate: CTP


organism: Staphylococcus aureus

substrate_name: CDPglycerol

proof_lines:
pH 8, reverse reaction
pH 8, forward reaction
pH 8

substrate: CDPglycerol


substrate_name: acetoacetate

assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA

proof_lines:
brain, pH 8.1, 25°C
pH 8.1, 25°C
kidney, skeletal muscle, pH 8.1, 25°C

substrate: acetoacetate


organism: Sus scrofa

assay_conditions_summary: pH 8.1; 295.15 K; cofactor CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: succinyl-CoA

proof_lines: pH 8.1, 25°C, presence of sodium sulfate

substrate: succinyl-CoA


organism: Acanthamoeba castellanii

substrate_name: lysophosphatidylcholine

proof_lines:
at low substrate concentrations
at high substrate concentrations

substrate: lysophosphatidylcholine


substrate_name: lysolecithin

substrate: lysolecithin


enzyme_display_name: NAD(+) ADP-ribosyltransferase

organism: Clostridium botulinum

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

enzyme: NAD(+) ADP-ribosyltransferase

substrate: NAD+


organism: Dictyostelium discoideum

proof_lines:
116000 Da protein
90000 Da protein


organism: Helix pomatia


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


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


organism: Neurospora crassa

substrate_name: Unknown

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: Rattus norvegicus


organism: Saccharolobus solfataricus


enzyme_display_name: peptidoglycan glycosyltransferase

organism: Escherichia coli

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


organism: Cheilanthes sieberi

substrate_name: nicotinic acid

proof_lines: lower maximal activity than pyridine and nicotinic acid

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


organism: Zobellia sp. M-2


organism: Pseudoalteromonas carrageenovora


substrate_name: kappa-carrageenan

proof_lines: pH and temperature not specified in the publication

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


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)


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


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

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

substrate: GDP-fucose


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

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