organism: Rattus norvegicus

substrate_name: ADP

substrate: ADP


enzyme_display_name: apyrase

substrate_name: ATP (with Ca2(+) as cofactor and 1900 pM enzyme)

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor ATP

enzyme: apyrase

source: uniprot


enzyme_display_name: geranylgeranyl diphosphate synthase

organism: Arabidopsis thaliana

substrate_name: farnesyl diphosphate (in the presence of 500 uM of isopentenyl diphosphate)

proof_lines: kcat is 29.7 sec(-1) with farnesyl diphosphate as substrate (in the presence of 500 uM of isopentenyl diphosphate). kcat is 21.0 sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of 100 uM of isopentenyl diphosphate). kc

enzyme: geranylgeranyl diphosphate synthase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP

proof_lines: kcat is 0.3 min(-1) with GPP as substrate. kcat is 0.7 min(-1) with FPP as substrate. kcat is 0.17 min(-1) with DMAPP as substrate.

substrate: IPP


enzyme_display_name: ribonuclease Z

substrate_name: bpNPP

proof_lines: kcat is 7.4 sec(-1) with bpNPP as substrate.

enzyme: ribonuclease Z

substrate: bpNPP


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

organism: Dictyostelium discoideum

substrate_name: cAMP

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

substrate: cAMP


proof_lines: Vmax values for isoforms 2, 3 and 4 relative to isoform 1 are 3.8, 1.6 and 2.1.


enzyme_display_name: assemblin

organism: Human cytomegalovirus (strain AD169)

proof_lines: KM is 10.7 uM according to PubMed:12549906.

enzyme: assemblin


organism: Glossina morsitans morsitans

substrate_name: ATP

proof_lines: kcat is 48.9 min(-1) with ATP as substrate. kcat is 12.7 min(-1) with ADP as substrate.

substrate: ATP


organism: Bacillus subtilis

substrate_name: trnI-Thr-TCAATG-trailer

source_db: brenda

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

proof_lines: the first cytosine is the primary anti-determinant for RNaseZ

substrate: trnI-Thr-TCAATG-trailer

source: brenda


organism: Drosophila melanogaster


organism: Homo sapiens

proof_lines: 25 mM K-MOPS, pH 6.75, 2.5 mM CaCl2, 1 mM dithiothreitol, 5% glycerol, 4 U/ml RNasin, 100 microg/ml bovine serum albumin

proof_lines: 25 mM K-MOPS, 2 mM MgCl2, at pH 6.8 and 37°C

proof_lines: 25 mM K-MOPS, pH 6.75, 1 mM MnCl2, 1 mM dithiothreitol, 5% glycerol, 4 U/ml RNasin, 100 microg/ml bovine serum albumin


organism: Sus scrofa

proof_lines:
at 37°C
at 28°C
CC is added to the 3-end of tRNA


organism: Synechocystis sp.

proof_lines: 40 mM Tris-HCl pH 7.5, 2 mM dithiothreitol


enzyme_display_name: ribonuclease H

substrate_name: RNA-DNA heteroduplex

mutation_type: substitution

enzyme: ribonuclease H

substrate: RNA-DNA heteroduplex


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


substrate_name: DNA/RNA hybrid

proof_lines: obtained by transcription of calf thymus DNA

substrate: DNA/RNA hybrid


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 8

proof_lines:
pH 8.0, 50 mM NaCl, wild-type enzyme
pH 8.0, 500 mM NaCl, wild-type enzyme


organism: Mus musculus

substrate_name: poly(rAdT)

substrate: poly(rAdT)


organism: Pyrococcus abyssi

substrate_name: RNA-DNA/DNA hybrid

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

substrate: RNA-DNA/DNA hybrid


organism: Thermococcus kodakarensis

substrate_name: RNA*DNA hybrid

substrate: RNA*DNA hybrid


enzyme_display_name: 1-phosphatidylinositol 4-kinase

organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
pH 8.0, 30°C
pH 7.5, 34°C
ATP in form of MgATP2-

enzyme: 1-phosphatidylinositol 4-kinase


organism: Spinacia oleracea

substrate_name: phosphatidylinositol

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5, enzyme form QII
pH 7.5, enzyme form QI

substrate: phosphatidylinositol


assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP


substrate_name: bis(p-nitrophenyl)phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature R252G to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-R252G, mutant, bis(p-nitrophenyl)phosphate catalysis

substrate: bis(p-nitrophenyl)phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature F51L to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-F51L, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature C40G to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-C40G, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature P178A to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-P178A, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature E208A to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-E208A, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature P64A to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-P64A, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_source: UniProtKB reviewed Q8LGU7 canonical sequence

proof_lines: AthTRZ1 wild-type, hydrolysis of phosphodiester bonds of bpNPP, KM value for AthTRZ1 two-fold increased relative to that of the tRNase Z of Escherichia coli


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature G62V to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-G62V, mutant, bis(p-nitrophenyl)phosphate catalysis


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q8LGU7; single-substitution reconstruction from selected AthTRZ1 mutation signature and applied mutation signature C25G to reconstruct the assayed variant sequence.

proof_lines: AthTRZ1-C25G, mutant, bis(p-nitrophenyl)phosphate catalysis


enzyme_display_name: polynucleotide 3'-phosphatase

organism: Acetivibrio thermocellus

substrate_name: bis-p-nitrophenyl phosphate

proof_lines: mutant enzyme D392N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme D392N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

enzyme: polynucleotide 3'-phosphatase

substrate: bis-p-nitrophenyl phosphate


proof_lines: mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 8.0),0.5 mM MnCl2

proof_lines: mutant enzyme H376N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H376N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


substrate_name: p-nitrophenyl phosphate

proof_lines: mutant enzyme D236E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2

proof_lines: mutant enzyme D236E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

substrate: p-nitrophenyl phosphate


proof_lines: mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2

proof_lines: mutant enzyme H264N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


proof_lines: mutant enzyme H323A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme H189A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme H189A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2


proof_lines: mutant enzyme D392A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme H189E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H189E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


proof_lines: mutant enzyme R237A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme R237A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


proof_lines: mutant enzyme D392E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme D392E, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


proof_lines: wild type enzyme, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: wild type enzyme, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2


proof_lines: mutant enzyme D233E, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


substrate_name: 3',5'-cyclic AMP

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

data_origin: experimental

substrate: 3',5'-cyclic AMP


organism: Pseudomonas aeruginosa


organism: Rattus norvegicus

substrate_name: cAMP (isoform 1)

substrate: cAMP (isoform 1)


substrate_name: Unknown

km_display: Not reported

substrate: Unknown


organism: Aedes aegypti

substrate_name: ADP

substrate: ADP


organism: Aedes albopictus


organism: Arabidopsis thaliana


organism: Thermus thermophilus

substrate_name: DNA-RNA-DNA hybrid

substrate: DNA-RNA-DNA hybrid


proof_lines: mutant A12S/K75M and A12S/K75M/A77P, pH 8.0, 30°C


substrate_name: M13 DNA/RNA

proof_lines:
at 37°C
at 70°C

substrate: M13 DNA/RNA


proof_lines: mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2

proof_lines: mutant enzyme H264A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


proof_lines: mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme H264Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


proof_lines: mutant enzyme H189D, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2

proof_lines: mutant enzyme H189D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2

proof_lines: mutant enzyme D236N, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2

proof_lines: mutant enzyme D236N, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme H189Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


proof_lines: mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM NiCl2

proof_lines: mutant enzyme D236A, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme D236A, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM MnCl2


mutation_signature: truncated mutant RNase HII-217

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: truncated mutant RNase HII-217, pH 8.0, 30°C


verification_status: corrected

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_paper_variant_reconstruction and applied mutation signature D135A to reconstruct the assayed variant sequence.


mutation_signature: truncated mutant RNase HII-213

proof_lines: truncated mutant RNase HII-213, pH 8.0, 30°C


mutation_signature: truncated mutant RNase HII-203

proof_lines: truncated mutant RNase HII-203, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_paper_variant_reconstruction and applied mutation signature H132A to reconstruct the assayed variant sequence.


mutation_signature: truncated mutant RNase HII-207

proof_lines: truncated mutant RNase HII-207, pH 8.0, 30°C


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


enzyme_display_name: sortase A

organism: Unknown

enzyme: sortase A


enzyme_display_name: xanthomonalisin

organism: Xanthomonas sp.

enzyme: xanthomonalisin


organism: Lactococcus lactis subsp. lactis

substrate_name: Dabsyl-LPFAGGAG-Edans

substrate: Dabsyl-LPFAGGAG-Edans


organism: Staphylococcus aureus

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


organism: Xanthomonas sp. (strain T-22)

assay_conditions_summary: pH 3.5; buffer 0.1 M sodium formate

proof_lines: kcat is 30.4 sec(-1) with Lys-Pro-Ala-Asp-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:8902622). kcat is 49.1 sec(-1) with Lys-Pro-Ala-Lys-Phe-p-nitrophenylalanine-Arg-Leu as substrate (PubMed:8902622).


proof_lines: mutant enzyme H376D, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme H376D, at 45°C, in 50 mM Tris-HCl (pH 8.0) 0.5 mM MnCl2


proof_lines: mutant enzyme H323Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C


proof_lines: mutant enzyme R237Q, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme R237Q, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


proof_lines: mutant enzyme R237K, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2, at 45°C

proof_lines: mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 7.5), 0.5 mM MnCl2

proof_lines: mutant enzyme R237K, at 45°C, in 50 mM Tris-HCl (pH 8.0), 0.5 mM NiCl2


organism: Homo sapiens


organism: Kostyavirus CJW1

substrate_name: dTMP

substrate: dTMP


organism: Omegavirus omega


substrate_name: DNA with 5'-hydroxyl ends

substrate: DNA with 5'-hydroxyl ends


organism: Rhodothermus phage RM378

substrate_name: cAMP

substrate: cAMP


organism: Bos taurus


organism: Dictyostelium discoideum


substrate_name: adenosine 3',5'-cyclic phosphate

substrate: adenosine 3',5'-cyclic phosphate


organism: Mus musculus

proof_lines: isoform PDE4D3, pH and temperature not specified in the publication


organism: Myxococcus xanthus

proof_lines: PdeA, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C

proof_lines: PdeB, in 50 mM Tris-HCl, pH 8.0, 0.05 mM MnCl2, at 40°C


organism: Rattus norvegicus

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

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

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


enzyme_display_name: cystinyl aminopeptidase

proof_lines:
pH 7.5, 37°C
CAP-II
pH 7.4

enzyme: cystinyl aminopeptidase


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


proof_lines:
mutant A429G, 37°C
pH 7.4, 37°C, mutant enzyme A429G


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature W375Y to reconstruct the assayed variant sequence.


sequence_source: NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering.

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


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature F484Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature V501A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature L391A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature W375F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature A590C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature P595I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature D440A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from NCBI GenBank L20965.1 CDS translation protein_id AAA03588.1, cited by PMID 11282454 as HSPDE4A4B residue numbering; variant reconstructed by direct residue substitution. and applied mutation signature D440N to reconstruct the assayed variant sequence.


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

proof_lines: PDE7B expressed in transfected COS-7 cells


organism: Leishmania mexicana


enzyme_display_name: D-xylose reductase (NADH)

organism: Candida parapsilosis

substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines:
pH 6.0
pH 6.0, coenzyme: NADH
pH 6.0, coenzyme: NADPH

enzyme: D-xylose reductase (NADH)

substrate: NADH


organism: Yamadazyma tenuis

substrate_name: D-xylose

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

substrate: D-xylose


assay_conditions_summary: pH 6.5; 315.15 K; cofactor NADH

proof_lines: pH 6.5, 42°C, recombinant His-tagged enzyme


source_db: oed

source: oed


substrate_name: D-Xylose

substrate: D-Xylose


enzyme_display_name: dipeptidyl-peptidase II

organism: Sus scrofa

enzyme: dipeptidyl-peptidase II


organism: Pseudomonas sp.

proof_lines:
autentic and recombinant PCP
recombinant PCP
autentic PCP


organism: Xanthomonas sp.

mutation_type: deletion


enzyme_display_name: chymotrypsin C

organism: Conogethes punctiferalis

proof_lines: in 50 mM Tris-HCl (pH 8.0), with 20 mM CaCl2, at 37°C

enzyme: chymotrypsin C


substrate_name: benzoyl-L-Leu methyl ester

substrate: benzoyl-L-Leu methyl ester


organism: Human alphaherpesvirus 1


organism: Human betaherpesvirus 5


proof_lines: pH 7.2, 30°C, wild-typelike mutant enzyme A143Q


organism: Staphylococcus aureus

substrate_name: Gly-Gly-Gly

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

substrate: Gly-Gly-Gly


proof_lines:
mutant enzyme
37°C, pH 7.5, mutant enzyme R197Cit


proof_lines:
37°C, pH 7.5, mutant enzyme E171A
mutant enzyme E171A


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


proof_lines:
37°C, pH 7.5, mutant enzyme D170A
mutant enzyme D170A


substrate_name: Dabcyl-QALPETGEE-Edans

proof_lines: pH 7.5, 37°C, recombinant circular truncated mutant CSrtADELTAN59 enzyme

proof_lines: pH 7.5, 37°C, recombinant linear truncated mutant LSrtADELTAN59 enzyme

substrate: Dabcyl-QALPETGEE-Edans


enzyme_display_name: N-methylcarbamate hydrolase

organism: Achromobacter sp. WM111

substrate_name: Carbaryl

proof_lines:
at pH 6.8 and 37°C
at pH 8.5 and 37Â°C
at pH 8.3 and 25°C

enzyme: N-methylcarbamate hydrolase

substrate: Carbaryl


proof_lines: pH 7.2, 30°C, mutant enzyme S134A/A143Q/H157A


proof_lines: pH 7.2, 30°C, mutant enzyme A143Q/S225Y/L229R


proof_lines: presence of 25% glycerol, enzyme HCMV A134Q

proof_lines: presence of 50% glycerol, enzyme HCMV A134Q


proof_lines:
soluble enzyme
pH 7.4, enzyme in solution
inclusion bodies


organism: Scheffersomyces stipitis

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from PMID 18028553 article text plus GenBank X59465/UniProt P31867; row-specific PsXR 2-2C12 sequence reconstructed from K270S/S271G/N272P/R276F. and applied mutation signature K270S/N272P/S271G/R276F to reconstruct the assayed variant sequence.

proof_lines: pH 6.0, temperature not specified in the publication, mutant enzyme K270S/N272P/S271G/R276F

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F

substrate: NADPH


sequence_source: PMID 18028553 article text plus GenBank X59465/UniProt P31867 canonical Scheffersomyces/Pichia stipitis XYL1 sequence.

proof_lines: pH 6.0, temperature not specified in the publication, wild-type enzyme, wild-type enzyme

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADH, wild-type enzyme

proof_lines: pH 6.0, temperature not specified in the publication, cofactor: NADPH, wild-type enzyme


organism: Sungouiella intermedia

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines: pH 7.0, 25°C, dual specific xylose reductase, cofactor: NADH

proof_lines: pH 7.0, 25°C, dual specific xylose reductase (dsXR)


substrate_name: NAD+

sequence_source: PMID 11513616 title plus UniProt O74237/XYL1_CANTE canonical Candida tenuis xylose reductase sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from PMID 17391061 title plus UniProt Q9UIQ6/LNPEP canonical human IRAP sequence; G428D reconstructed directly from the canonical Gly428 residue. and applied mutation signature G428D to reconstruct the assayed variant sequence.


substrate_name: Vasopressin

substrate: Vasopressin


organism: Saccharomyces cerevisiae

substrate_name: L-cysteine-nitroanilide

substrate: L-cysteine-nitroanilide


organism: Streptococcus thermophilus

substrate_name: L-Lysine-p-nitroanilide

verification_status: unverified

substrate: L-Lysine-p-nitroanilide

status: unverified


substrate_name: S-benzyl-L-cysteine-p-nitroanilide

substrate: S-benzyl-L-cysteine-p-nitroanilide


organism: Bos taurus

assay_conditions_summary: pH 5.5; 310.15 K; buffer acetate

proof_lines: enzyme from lung, in acetic buffer (pH 5.5), at 37°C

proof_lines: enzyme from renal cortex, in acetic buffer (pH 5.5), at 37°C


substrate_name: Lys-Pro-p-nitroanilide

substrate: Lys-Pro-p-nitroanilide


organism: Rattus norvegicus

substrate_name: Gly-Pro-Ala

proof_lines:
enzyme form DPP II-M
enzyme form DPP II-S

substrate: Gly-Pro-Ala


enzyme_display_name: pancreatic elastase

organism: Salmo salar

substrate_name: Suc-AAA-pNA (at 22 degrees Celsius)

enzyme: pancreatic elastase

substrate: Suc-AAA-pNA (at 22 degrees Celsius)


enzyme_display_name: [pyruvate dehydrogenase (acetyl-transferring)] kinase

organism: Arabidopsis thaliana

substrate_name: pyruvate dehydrogenase

proof_lines: pH 7.5, 37°C, recombinant PDK mutant L234A

substrate: pyruvate dehydrogenase


proof_lines: pH 7.5, 37°C, recombinant PDK mutant H233A

enzyme: [pyruvate dehydrogenase (acetyl-transferring)] kinase


proof_lines: pH 7.5, 37°C, recombinant PDK mutant E238A


substrate_name: ATP

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines: 37°C, recombinant mutant G319A of isozyme PDK2

substrate: ATP


proof_lines:
kidney enzyme
pH 7.5, 30°C
pH 7.0, 30°C


organism: Lathyrus oleraceus

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


organism: Sus scrofa

assay_conditions_summary: pH 7.8; 303.15 K; buffer and pH notes; cofactor ATP

proof_lines:
at 0.2 M buffer concentration
at 0.04 M buffer concentration
pH 7.8, 30°C


enzyme_display_name: rRNA N-glycosylase

organism: Cinnamomum camphora

substrate_name: rRNA

proof_lines:
pH 7.6, 35°C, 80S ribosome, cinnamomin
pH 7.6, 35°C, naked RNA, cinnamomin

enzyme: rRNA N-glycosylase

substrate: rRNA


organism: Escherichia coli

proof_lines: pH 7.4, 28°C, Artemia salina ribosomes, untreated holotoxin

proof_lines: pH 7.4, 28°C, Artemia salina ribosomes, A subunit treated with trypsin, urea and dithiothreitol

proof_lines: pH 7.4, 28°C, Artemia salina ribosomes, A subunit treated with urea and dithiothreitol


organism: Ricinus communis


organism: Saponaria officinalis

proof_lines:
37°C, presence of 50 mM KCl, 1 mM MgCl2
saporin-L1, pH 7.7, 20°C
pH 7.8, 25°C


proof_lines:
isoform CELA3A, at pH 8.0 and 22°C
isoform CELA3B, at pH 8.0 and 22°C
pancreatic elastase


organism: Ovis aries

substrate_name: succinyl-Ala-Ala-Ala-p-nitroanilide

substrate: succinyl-Ala-Ala-Ala-p-nitroanilide


substrate_name: succinyl-Ala-Ala-Pro-Ile-p-nitroanilide

substrate: succinyl-Ala-Ala-Pro-Ile-p-nitroanilide


assay_conditions_summary: pH 8; 295.15 K; buffer 0.1 M phosphate

proof_lines: in the presence of 0.2 mM spermidine, at pH 8.5 and 37°C

proof_lines: in the presence of 0.5 mM spermidine, at pH 8.5 and 37°C


proof_lines: 37°C, recombinant mutant G284A of isozyme PDK2


proof_lines: 37°C, recombinant isozyme PDK2 wild-type


assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines: recombinant His-tagged isozyme PDK1, 37°C, pH 7.8


substrate_name: Unknown

ki_unit: mM

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


assay_conditions_summary: pH 7.4; 303.15 K; buffer composition, overview; cofactor ATP

proof_lines: pH 7.4, 30°C, with oxidized E2, in presence of 2 mM DTT

proof_lines: pH 7.4, 30°C, with reduced E2, in presence of NADH/NAD+

proof_lines: pH 7.4, 30°C, with oxidized E2, in presence of NADH/NAD+


substrate_name: [Pyruvate dehydrogenase (lipoamide)]

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

proof_lines: phosphorylation site 1 of subunit E1, isozyme PDK1, pH 7.0, 30°C

proof_lines: phosphorylation site 3 of subunit E1, isozyme PDK1, pH 7.0, 30°C

proof_lines: phosphorylation site 2 of subunit E1, isozyme PDK4, pH 7.0, 30°C

substrate: [Pyruvate dehydrogenase (lipoamide)]


organism: Unknown


proof_lines: about, pH 7.5, 37°C, recombinant PDK mutant E238H


proof_lines: pH 7.5, 37°C, recombinant PDK mutant L234H


proof_lines: pH 7.5, 37°C, recombinant PDK mutant E238Q


substrate_name: 28S rRNA within the native ribosome

substrate: 28S rRNA within the native ribosome


enzyme_display_name: apyrase

organism: Mimosa pudica

substrate_name: ADP

enzyme: apyrase

substrate: ADP


organism: Ornithodoros savignyi

assay_conditions_summary: cofactor ATP


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C, presence of Mg2+
free ATP
pH 7.5, 37°C, presence of Ca2+


organism: Rhodnius prolixus


organism: Solanum tuberosum

assay_conditions_summary: pH 6; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 6.0, presence of Ca2+
pH 6.0, 22°C
variety Desiree, 20°C


substrate_name: ATP; H2O

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
pH 7.6, 37°C
pH 7.6, 37°C, substrate ADP
pH 7.6, 37°C, substrate ATP

substrate: ATP; H2O


organism: Taenia crassiceps


organism: Trichomonas vaginalis

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP


organism: Triticum aestivum

assay_conditions_summary: pH 5.5; 310.15 K; cofactor ATP


organism: Trypanosoma brucei brucei

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP


organism: Trypanosoma cruzi

substrate_name: UDP

substrate: UDP


enzyme_display_name: xylose isomerase

organism: Streptomyces sp.

substrate_name: D-Xylose

enzyme: xylose isomerase

substrate: D-Xylose


organism: Arabidopsis thaliana

substrate_name: ATP (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines: kcat is 0.55 sec(-1) with ATP as substrate (at pH 7.5, in PubMed:15629119).

substrate: ATP (at pH 7.5)


organism: Aedes aegypti


organism: Bacillus subtilis

substrate_name: dATP

substrate: dATP


organism: Bos taurus


organism: Candida parapsilosis


organism: Cicer arietinum


organism: Ctenocephalides felis

assay_conditions_summary: cofactor ADP


organism: Daboia russelii

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


organism: Gallus gallus


organism: Glycine max


organism: Homo sapiens

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP


organism: Legionella pneumophila


organism: Lupinus luteus


organism: Agrobacterium sp. XWY-2

substrate_name: Carbaryl

substrate: Carbaryl


organism: Aminobacter aminovorans

substrate_name: methomyl

substrate: methomyl


organism: Aspergillus niger

substrate_name: isoprocarb

assay_conditions_summary: pH 7

substrate: isoprocarb


organism: Blastobacter sp. M501

substrate_name: xylylcarb

substrate: xylylcarb


organism: Novosphingobium sp. KN65.2

substrate_name: carbofuran

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

substrate: carbofuran


organism: Pseudomonas aeruginosa


organism: Pseudomonas sp. 50432


organism: Pseudomonas sp. C7

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


organism: Pseudomonas sp. CRL-OK

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


organism: Pseudomonas sp. OXA20


organism: Sphingobium sp. CFD-1


organism: Sphingomonas sp. CDS-1

substrate_name: oxamyl

substrate: oxamyl


organism: Unknown

substrate_name: rRNA

substrate: rRNA


enzyme_display_name: strictosidine synthase

organism: Rauvolfia serpentina

substrate_name: tryptamine

enzyme: strictosidine synthase

substrate: tryptamine


substrate_name: serotonin

proof_lines:
wild-type enzyme
wild type, pH 7.0, 35°C, 15 min

substrate: serotonin


proof_lines: kcat is 78.2 min(-1) with tryptamine and secologanin as substrates (PubMed:16531499). kcat is 10.65 sec(-1) with tryptamine and secologanin as substrates (PubMed:17884630). kcat is 2.32 sec(-1) with 6-methyl-tryptamine and secologanin as su


organism: Streptomyces sp. 1

substrate_name: D-glucose

substrate: D-glucose


organism: Streptomyces sp. 32

substrate_name: D-xylose

substrate: D-xylose


organism: Streptomyces violaceoruber

proof_lines:
with 1 mM Co2+
with 10 mM Mg2+


organism: Streptomyces viridobrunneus

substrate_name: xylose

substrate: xylose


organism: Thermoanaerobacterium saccharolyticum

substrate_name: D-fructose

substrate: D-fructose


organism: Catharanthus roseus


substrate_name: secologanin

substrate: secologanin


proof_lines: wild-type strictosidine synthase expressed in yeast


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


organism: Cinchona robusta

proof_lines:
isoform II b
isoform I a
isoform I b


organism: Escherichia coli

proof_lines: HPLC, neutral pH, micromolar to low millimolar substrate concentrations


organism: Ophiorrhiza pumila

proof_lines: pH and temperature not specified in the publication


proof_lines:
in reaction with tryptamine
at pH 6.5 and 45°C


organism: Rauvolfia vomitoria


enzyme_display_name: plasma kallikrein

organism: Homo sapiens

proof_lines: catalytic domain expressed after mutagenizing three asparagines to glutamate in a baculovirus/Sf9 system

proof_lines: protease domain in Pichia pastoris as a heterologously glycosylated zymogen that is activated by limited trypsin digestion and treated with endoglycosidase H deglycosidase

enzyme: plasma kallikrein


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


organism: Rattus norvegicus

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: carboxypeptidase U

organism: Bos taurus

substrate_name: hippuryl-Arg

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

proof_lines:
Vmax: 46.05 micromol/l/min
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: brenda skid

enzyme: carboxypeptidase U

substrate: hippuryl-Arg


enzyme_display_name: peptidyl-glutamate 4-carboxylase

substrate_name: vitamin KH2

proof_lines: R406A/H408A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM

enzyme: peptidyl-glutamate 4-carboxylase

substrate: vitamin KH2


substrate_name: FLEEL

proof_lines: R234A/H235A mutant, peptides comprising residue YVFLDHQDADANLILNRPKR concentration 0 microM

substrate: FLEEL


proof_lines:
R359A/H360A/K361A mutant
FLEEL, R359A/H360A/K361A mutant


organism: Conus textile

substrate_name: 28-residue peptides based on residues -18 to +10 of human proprothrombin


substrate_name: reduced vitamin K

proof_lines: cosubstrate chimeric coagulation factor, pH not specified in the publication, temperature not specified in the publication

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

proof_lines: cosubstrate matrix Gla protein, pH not specified in the publication, temperature not specified in the publication

substrate: reduced vitamin K


substrate_name: anisylazoformyl-Lys

proof_lines:
24°C
room temperature
recombinant enzyme

substrate: anisylazoformyl-Lys


substrate_name: hippuryl-arginine

proof_lines: mutant P91S, activation of TAFI by plasmin

substrate: hippuryl-arginine


proof_lines: mutant S90D/S94V/S90D, activation of TAFI by plasmin


substrate_name: p-anisylazoformyl-L-arginine

proof_lines: mutant R92K, activation of TAFI by thrombin in the presence of thrombomodulin

proof_lines: mutant R92K, activation of TAFI by plasmin

substrate: p-anisylazoformyl-L-arginine


proof_lines: mutant S94V, activation of TAFI by plasmin

proof_lines: mutant S94V, activation of TAFI by thrombin in the presence of thrombomodulin


proof_lines: mutant A93V, activation of TAFI by thrombin in the presence of thrombomodulin

proof_lines: mutant A93V, activation of TAFI by plasmin


proof_lines: wild-type, activation of TAFI by thrombin in the presence of thrombomodulin

proof_lines: wild-type, activation of TAFI by plasmin


proof_lines: mutant S90P, activation of TAFI by plasmin

proof_lines: mutant S90P, activation of TAFI by thrombin in the presence of thrombomodulin


substrate_name: kininogen

proof_lines:
pH 8.0, 37°C
at pH 7.4 and 37°C
at 37°C

substrate: kininogen


proof_lines: ecotin with mutation H53P in the 50s loop, at room temperature


proof_lines: ecotin with mutations S82W/T83N/M84R/M85R/A86S in the 80s loop, at room temperature


proof_lines: ecotin with mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop, at room temperature


proof_lines: ecotin with mutation H53P in the 50s loop and mutations S82W/T83N/M84R/M85R/A86S in the 80s loop, at room temperature


proof_lines: ecotin with mutation H53P in the 50s loop, mutations S82W/T83N/M84R/M85R/A86S in the 80s loop and mutations R108S/N110S in the 100s loop, at room temperature


proof_lines: ecotin with mutations R108S/N110S in the 100s loop, at room temperature


proof_lines: ecotin with mutation H53P in the 50s loop and mutations R108S/N110S in the 100s loop, at room temperature


organism: Lachesis muta


organism: Macaca fascicularis


organism: Mus musculus


enzyme_display_name: assemblin

organism: Human betaherpesvirus 5

substrate_name: GVVNASCRLA

enzyme: assemblin

substrate: GVVNASCRLA


proof_lines:
mutant V141G/V207G, soluble
mutant V141G/V207G, refolded


organism: Human betaherpesvirus 6


enzyme_display_name: sortase A

organism: Bacillus anthracis

proof_lines: sortase A DELTA64 (residues Asp65–Lys210), in 20 mM HEPES, pH 7.5

enzyme: sortase A


proof_lines: sortase A DELTA56 (residues Asp-57-Lys210), in 20 mM HEPES, pH 7.5


organism: Staphylococcus aureus

substrate_name: Abz-LPETG-Dap(Dnp)

substrate: Abz-LPETG-Dap(Dnp)


organism: Thermotoga neapolitana

substrate_name: D-glucose

proof_lines: soluble wild type enzyme, at 90°C, pH 7.0

proof_lines: soluble wild type enzyme, at 80°C, pH 7.0


proof_lines: unbound CBD-TNX fusion protein, at 80°C, pH 7.0

proof_lines: immobilized CBD-TNX fusion protein, at 90°C, pH 7.0

proof_lines: unbound CBD-TNX fusion protein, at 90°C, pH 7.0


proof_lines:
FLEEL, R513A/K515A mutant
R513A/K515A mutant
proPT28, R513A/K515A mutant


enzyme_display_name: NAD(+) glycohydrolase

organism: Aspergillus fumigatus

substrate_name: NADP+

assay_conditions_summary: pH 7.5; 293.15 K; cofactor NADP+

enzyme: NAD(+) glycohydrolase

substrate: NADP+


substrate_name: etheno-NAD+

assay_conditions_summary: pH 5.5; 298.15 K; cofactor NAD+

substrate: etheno-NAD+


substrate_name: NAD+; H2O

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O


substrate_name: NADP+; Nicotinic acid

substrate: NADP+; Nicotinic acid


substrate_name: Nicotinamide guanine dinucleotide

substrate: Nicotinamide guanine dinucleotide


organism: Sphingobacterium faecium


organism: Streptococcus equisimilis

substrate_name: H2O; NAD+

substrate: H2O; NAD+


organism: Streptococcus pyogenes


proof_lines: wild-type carboxylase in bovine liver microsomes

proof_lines: for wild type FLAG-vitamin K-dependent gamma-glutamyl carboxylase


proof_lines: FLAG-vitamin K-dependent gamma-glutamyl carboxylase

proof_lines: recombinant His6-carboxylase present in Sf9 cell microsomes


organism: Unknown

substrate_name: NAD+

assay_conditions_summary: cofactor NADP+

substrate: NAD+


enzyme_display_name: flavodoxin--NADP(+) reductase

organism: Escherichia coli

substrate_name: reduced flavodoxin II

enzyme: flavodoxin--NADP(+) reductase

substrate: reduced flavodoxin II


organism: Lathyrus oleraceus

substrate_name: reduced flavodoxin

substrate: reduced flavodoxin


enzyme_display_name: steryl-sulfatase

organism: Pseudomonas aeruginosa

substrate_name: testosterone 3-sulfate

enzyme: steryl-sulfatase

substrate: testosterone 3-sulfate


organism: Nostoc sp.


organism: Rhodobacter capsulatus

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: substrate ferricyanide, pH 8.0, temperature not specified in the publication

proof_lines: presence of flavodoxin, pH 8.0, temperature not specified in the publication

substrate: NADPH


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines: wild-type, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: wild-type, substrate ferricyanide, pH 7.2, 25°C


proof_lines: mutant Del267-272, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: mutant Del267-272, substrate ferricyanide, pH 7.2, 25°C


proof_lines: mutant A266Y, substrate 2,6-dichlorophenolindophenol, pH 7.2, 25°C

proof_lines: mutant A266Y, substrate ferricyanide, pH 7.2, 25°C

proof_lines: mutant A266Y/Del267-272, substrate ferricyanide, pH 7.2, 25°C


organism: Danio rerio

substrate_name: pregnenolone 3-sulfate

substrate: pregnenolone 3-sulfate


organism: Homo sapiens

proof_lines: pH 7.4, 37°C, enzyme from human placenta


substrate_name: testosterone 17-sulfate

substrate: testosterone 17-sulfate


organism: Sus scrofa

substrate_name: Estrone sulfate

proof_lines: 37°C, 10 min reaction time, Ringer-HEPES buffer, Vmax=24.05 fmol/s/microgram protein

substrate: Estrone sulfate


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

substrate_name: NAD(+)

substrate: NAD(+)


organism: Mus musculus

substrate_name: NAD for the NADase activity (in the presence of 0.03 mM DTT)


enzyme_display_name: chloride peroxidase

organism: Curvularia inaequalis

substrate_name: Br-; Monochlorodimedone; H2O2

enzyme: chloride peroxidase

substrate: Br-; Monochlorodimedone; H2O2


organism: Leptoxyphium fumago

substrate_name: estrone

assay_conditions_summary: pH 3

proof_lines: with Cl-, pH 3.0, temperature not specified in the publication

proof_lines: with Br-, pH 3.0, temperature not specified in the publication

substrate: estrone


enzyme_display_name: 6-aminohexanoate aminotransferase

organism: Vibrio fluvialis

enzyme: 6-aminohexanoate aminotransferase


substrate_name: benzylamine

substrate: benzylamine


substrate_name: Styrene

assay_conditions_summary: pH 3; 293.15 K; buffer pH 5

proof_lines:
enzyme in ternary system P1
from the dimer model
pH 3, without Cl-

substrate: Styrene


organism: Musa x paradisiaca

substrate_name: monochlorodimedone

proof_lines: in 50 mM phosphate buffer pH 2.75 at 30°C, with 20 mM KCl

substrate: monochlorodimedone


organism: Streptomyces toyocaensis

substrate_name: Cl-

substrate: Cl-


organism: Bacillus cereus

substrate_name: reduced flavodoxin 2

proof_lines: pH 7.5, temperature not specified in the publication, recombinant FNR1

proof_lines: pH 7.5, temperature not specified in the publication, recombinant FNR2

substrate: reduced flavodoxin 2


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


substrate_name: NADH

substrate: NADH


substrate_name: ferricytochrome c2

substrate: ferricytochrome c2


organism: Chromobacterium violaceum


organism: Pseudomonas jessenii


organism: Bos taurus

substrate_name: dehydroepiandrosterone 3-sulfate

substrate: dehydroepiandrosterone 3-sulfate


organism: Chlamydomonas reinhardtii

substrate_name: p-Nitrophenyl sulfate

substrate: p-Nitrophenyl sulfate


organism: Haliotis sp.

substrate_name: 4-nitrophenyl sulfate

substrate: 4-nitrophenyl sulfate


organism: Helix pomatia


substrate_name: dehydroepiandrosterone sulfate

proof_lines:
pH 8, 37°C
esterone 3-sulfate
37°C, mammary myoepithelial cells

substrate: dehydroepiandrosterone sulfate


organism: Macaca mulatta


substrate_name: methylumbelliferyl sulfate

proof_lines:
hydropobic form
hydrophilic form

substrate: methylumbelliferyl sulfate


organism: Patella vulgata


organism: Rattus norvegicus


organism: Aplysia californica

substrate_name: NAD+

assay_conditions_summary: pH 7.4; cofactor NAD+

substrate: NAD+


organism: Bacillus subtilis

substrate_name: NAD+; H2O

substrate: NAD+; H2O


substrate_name: 1,N6-etheno-NAD+; H2O

assay_conditions_summary: 298.15 K; cofactor NAD+

proof_lines:
spleen
25°C , seminal fluid
erythrocytes

substrate: 1,N6-etheno-NAD+; H2O


organism: Bungarus fasciatus

substrate_name: NADP+

substrate: NADP+


organism: Escherichia coli (strain K12)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 338.9 min(-1) with NADPH as the donor. kcat is 33 min(-1) with NADP as the donor (PubMed:11085917). kcat is 0.15 sec(-1) with ferredoxin as substrate. kcat is 0.0042 sec(-1) with flavodoxin 1 as substrate. kcat is 0.0039 sec(-1) wit

substrate: NADPH


organism: Rhodobacter capsulatus

substrate_name: NADPH (in the presence of K(3)Fe(CN)(6))

proof_lines: kcat is 222 sec(-1) with K(3)Fe(CN)(6) as substrate. kcat is 20 sec(-1) with 2,6-dichlorophenolindophenol as substrate.


organism: Bacillus cereus (strain MSX-D12)

substrate_name: NAD(+)

substrate: NAD(+)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Sphingobacterium faecium (strain DSM 11690 / JCM 21820 / NBRC 15299 / NCIMB 13408 / KS 0470)


organism: Vibrio fluvialis

smiles: CCCCCN


smiles: NCCCCCC(=O)O


smiles: O=CCCCCC(=O)O


smiles: NCCCC(=O)O


proof_lines:
pH 8.0, 30°C
Raw SKiD Env: Temp=30°C, pH=8


smiles: NCCCCC(=O)O


enzyme_display_name: anthrax lethal factor endopeptidase

organism: Bacillus anthracis

enzyme: anthrax lethal factor endopeptidase


proof_lines: copper-substituted enzyme, at pH 6.5 and 20°C

proof_lines: pH 7.4, 22°C, apoprotein reconstituted in presence of Cu2+

proof_lines: pH 7.4, 22°C, apoprotein reconstituted in presence of Zn2+


organism: Thermus thermophilus

substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


enzyme_display_name: deacetoxycephalosporin-C hydroxylase

organism: Streptomyces clavuligerus

substrate_name: cephalosporin G

enzyme: deacetoxycephalosporin-C hydroxylase

substrate: cephalosporin G


proof_lines: pH 7.5, 25°C, recombinant mutant T90A/P72L/A311V


organism: Deinagkistrodon acutus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+


organism: Homo sapiens

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

proof_lines:
membrane fraction, pH 7.0, 37°C
pH 7.2, 37°C, purified enzyme


organism: Microdochium nivale


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


organism: Mycobacterium tuberculosis


organism: Neurospora crassa


organism: Oryctolagus cuniculus


organism: Pseudomonas putida


organism: Rattus norvegicus

proof_lines:
microsomal
chromatin
plasma membrane


organism: Streptococcus pyogenes

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

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


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


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


organism: Actinomyces sp.

substrate_name: Fe2+; 2-oxoglutarate; deacetoxycephalosporin C


substrate_name: Penicillin N; penicillin G

substrate: Penicillin N; penicillin G


substrate_name: penicillin G; Penicillin N

substrate: penicillin G; Penicillin N


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


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


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


enzyme_display_name: HtrA2 peptidase

enzyme: HtrA2 peptidase


substrate_name: beta-casein

substrate: beta-casein


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

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: Homo sapiens

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

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

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

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: brenda; skid


substrate_name: H3 monomethyl-K4

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


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

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.


organism: Streptomyces clavuligerus

substrate_name: Penicillin N

substrate: Penicillin N


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


substrate_name: penicillin G

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

substrate: penicillin G


substrate_name: Unknown

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

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)

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


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

assay_conditions_summary: cofactor NADPH

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


organism: Acremonium sp.

substrate_name: O2; Ascorbate

substrate: O2; Ascorbate


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

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

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

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