organism: Homo sapiens

substrate_name: UDP-galactose

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM sodium cacodylate

proof_lines: wild type enzyme, in 100 mM sodium cacodylate buffer (pH 7.4) containing 10 mM MnCl2, at 37°C

proof_lines: DELTA1-81, wild-type, pH and temperature not specified in the publication

proof_lines: wild type enzyme, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication

substrate: UDP-galactose


source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

assay_conditions_summary: pH 7; buffer 100 mM cacodylate

proof_lines: DELTA1-81, mutant L206P, pH and temperature not specified in the publication

proof_lines: mutant enzyme L206P, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication

source: brenda


proof_lines: DELTA1-81, mutant R270C, pH and temperature not specified in the publication

proof_lines: mutant enzyme R270C, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication


proof_lines: DELTA1-81, mutant A186D, pH and temperature not specified in the publication

proof_lines: mutant enzyme A186D, in 100 mM cacodylate buffer (pH 7.0) containing 10 mM MnCl2, temperature not specified in the publication


kcat_display: Not reported

proof_lines: mutant L206A, pH and temperature not specified in the publication


mutation_signature: Unknown

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

assay_conditions_summary: pH 5; 298.15 K; buffer sodium acetate; cofactor ATP

proof_lines: recombinant enzyme, in sodium acetate buffer (25 mM, pH 5.0), 20 mM MnCl2, 50 mM KCl, at 25°C

proof_lines: pH 5.5, 37°C before preincubation with ATP

proof_lines: pH 5.5, 37°C after preincubation with ATP


organism: Mus musculus


enzyme_display_name: xanthine phosphoribosyltransferase

organism: Enterococcus faecalis

substrate_name: xanthine

enzyme: xanthine phosphoribosyltransferase

substrate: xanthine


organism: Lacticaseibacillus casei


organism: Leishmania donovani

substrate_name: hypoxanthine

substrate: hypoxanthine


assay_conditions_summary: pH 7.5; 298.15 K; buffer TM

proof_lines: wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine

proof_lines: wild-type, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine


substrate_name: guanine

proof_lines: mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine

proof_lines: mutant E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine

substrate: guanine


proof_lines: mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine

proof_lines: mutant E198D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine


proof_lines: mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine

proof_lines: mutant E198D/E215D, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine


proof_lines: mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM xanthine

proof_lines: mutant E215Q, at 25°C, 40 mM Tris-HCl, pH 7.5, 1 mM hypoxanthine


organism: Plasmodium falciparum

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

proof_lines: unactivated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication

proof_lines: IMP-activated mutant enzyme W181S, at pH 7.4, temperature not specified in the publication

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


enzyme_display_name: ADP-specific glucose/glucosamine kinase

organism: Thermococcus litoralis

substrate_name: ADP

source_db: oed

protein_accession_database: UniProt

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence and applied mutation signature E279Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 313.15 K; cofactor ADP

data_origin: experimental

enzyme: ADP-specific glucose/glucosamine kinase

substrate: ADP

source: oed


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence and applied mutation signature E279L to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q7M537 direct REST/FASTA lookup plus selected source accession evidence and applied mutation signature E308Q to reconstruct the assayed variant sequence.


substrate_name: D-glucose

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

substrate: D-glucose


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

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

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

source_databases_merged: brenda skid


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.6; 323.15 K; cofactor ADP

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


assay_conditions_summary: pH 7; 310.15 K; cofactor ADP


organism: Pyrococcus furiosus

proof_lines: in the presence of 1 mM Mg2+, pH 7.8, 40°C

proof_lines: in the presence of 1 mM Mn2+, pH 7.8, 40°C

proof_lines: in the presence of 1 mM Co2+, pH 7.8, 40°C


organism: Pyrococcus horikoshii

assay_conditions_summary: pH 6.5; 323.15 K; cofactor ADP

proof_lines: in the presence of 1 mM Mn2+, pH 6.5, 50°C

proof_lines: in the presence of 1 mM Mg2+, pH 6.5, 50°C

proof_lines: in the presence of 1 mM Co2+, pH 6.5, 50°C


organism: Thermococcus kodakarensis

substrate_name: D-glucosamine

assay_conditions_summary: pH 7.5; 353.15 K; cofactor ADP

substrate: D-glucosamine


organism: uncultured bacterium


proof_lines:
pH 7.8, 60°C
MgADP, pH 7.8, 60°C


enzyme_display_name: pyridoxal kinase

organism: Bacillus subtilis

enzyme: pyridoxal kinase


organism: Escherichia coli

substrate_name: pyridoxamine

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines: kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C

proof_lines: kinase 1 with MgATP2- as substrate, pH 7.3, 37°C

proof_lines: kinase 1 with pyridoxal as substrate, pH 7.3, 37°C

substrate: pyridoxamine


substrate_name: pyridoxal

assay_conditions_summary: pH 6.5; 310.15 K; cofactor ATP

proof_lines: in the presence of Zn2+, at pH 6.5 and 37°C

proof_lines: in the presence of K+, at pH 7.0 and 30°C

substrate: pyridoxal


organism: Ovis aries

substrate_name: ATP

assay_conditions_summary: pH 5.8; 310.15 K; cofactor ATP

proof_lines: pH 5.8, 37°C, with MnATP2- as the second substrate

substrate: ATP


assay_conditions_summary: pH 6.5; 303.15 K; cofactor ATP


organism: Photobacterium sp.

proof_lines: pH 5.0, 37°C, cosubstrate: CMP-9-benzamido-Neu5Ac

proof_lines: pH 5.0, 37°C, cosubstrate: CMP-9-phenylacetamido-Neu5Ac


organism: Photobacterium sp. JT-ISH-224

substrate_name: CMP-N-acetyl-beta-neuraminate

substrate: CMP-N-acetyl-beta-neuraminate


organism: Rattus norvegicus

substrate_name: CMP-N-acetylneuraminate

proof_lines:
with asialo-alpha1-acid glycoprotein
pH 5.0, 37°C
pH 6.5, 37°C

substrate: CMP-N-acetylneuraminate


enzyme_display_name: alanine--glyoxylate transaminase

organism: Aedes aegypti

substrate_name: glyoxylate

proof_lines: pH 7.0, 50°C, glyoxylate as amino acceptor

enzyme: alanine--glyoxylate transaminase

substrate: glyoxylate


organism: Arabidopsis thaliana

proof_lines:
cosubstrate L-alanine, pH 7.5, 25°C
cosubstrate L-glutamate, pH 7.5, 25°C
pH 7.5, 25°C


organism: Canis familiaris

substrate_name: Glyoxylate; L-Alanine

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

substrate: Glyoxylate; L-Alanine


organism: Homo sapiens

substrate_name: L-alanine

proof_lines: G82E, pH not specified in the publication, temperature not specified in the publication

substrate: L-alanine


proof_lines: major allele (P11, I340), pH not specified in the publication, temperature not specified in the publication

proof_lines: pH 8.0, 37°C, recombinant AGT-His, L-alanine as amino donor


proof_lines: P11L/I340M minor allele, pH not specified in the publication, temperature not specified in the publication


proof_lines: P11L/I340M/F152I, pH not specified in the publication, temperature not specified in the publication


proof_lines: F152I, pH not specified in the publication, temperature not specified in the publication


proof_lines: P11L/I340M/G41R, pH not specified in the publication, temperature not specified in the publication


proof_lines: G41V, pH not specified in the publication, temperature not specified in the publication


proof_lines: G41R, pH not specified in the publication, temperature not specified in the publication


organism: Spinacia oleracea

proof_lines: pH 7.0, 27°C, glyoxylate as amino acceptor


organism: Thermococcus litoralis


substrate_name: asialo-transferrin

proof_lines: expressed as concentration of terminal galactosyl residues

substrate: asialo-transferrin


organism: Mus musculus


organism: Photobacterium damselae

substrate_name: 4-methylumbelliferyl beta-D-lactoside

mutation_type: deletion

proof_lines: pH 8.5, 37°C, enzyme form DELTA112Pd2,6ST(N)

substrate: 4-methylumbelliferyl beta-D-lactoside


proof_lines: pH 8.5, 37°C, enzyme form DELTA15Pd2,6ST(N)

proof_lines: alpha2,6-trans-sialidase activity of DELTA15Pd2,6ST


substrate_name: lactose

proof_lines: mutant enzyme I411T/L433T, at pH 8.0 and 22°C

substrate: lactose


proof_lines: mutant enzyme I411T/L433S, at pH 8.0 and 22°C


organism: Photobacterium leiognathi

mutation_signature: 6-sialyltransferase activity of the truncated recombinant enzyme alpha2 / 6-sialyltransferase activity of the truncated recombinant enzyme

mutation_type: truncation

proof_lines: alpha2,6-sialyltransferase activity of the truncated recombinant enzyme


organism: Plasmodium falciparum

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

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


proof_lines: IMP-activated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication

proof_lines: unactivated mutant enzyme W181F, at pH 7.4, temperature not specified in the publication


proof_lines: IMP-activated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication

proof_lines: unactivated mutant enzyme W181Y, at pH 7.4, temperature not specified in the publication


organism: Toxoplasma gondii

substrate_name: xanthine

substrate: xanthine


organism: Bombyx mori


organism: Bos taurus

substrate_name: asialo-thyroglobulin glycopeptides

substrate: asialo-thyroglobulin glycopeptides


organism: Capra hircus

proof_lines:
with N-acetyllactosamine
with lactose


organism: Cavia porcellus


organism: Drosophila sp. (in: flies)

proof_lines: non-reducing terminus of asialofetuin glycans


organism: Helicobacter cetorum


enzyme_display_name: cellulose 1,4-beta-cellobiosidase (reducing end)

organism: Penicillium digitatum

substrate_name: carboxymethyl cellulose

km_display: Not reported

substrate: carboxymethyl cellulose


organism: Phanerodontia chrysosporium

substrate_name: bacterial cellulose

proof_lines: in 50 mM sodium acetate, pH 5.0, at 30°C

enzyme: cellulose 1,4-beta-cellobiosidase (reducing end)

substrate: bacterial cellulose


organism: Rasamsonia emersonii


organism: Thermoascus aurantiacus


organism: Trametes versicolor

substrate_name: p-nitrophenyl beta-D-cellobioside

substrate: p-nitrophenyl beta-D-cellobioside


organism: Trichoderma harzianum

substrate_name: 2-chloro-4-nitrophenyl beta-D-lactoside

proof_lines: 50 mM sodium acetate buffer, pH 5.0, at 50°C

substrate: 2-chloro-4-nitrophenyl beta-D-lactoside


organism: Trichoderma reesei

assay_conditions_summary: pH 5; 303.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium acetate with 2 mM CaCl2 and pH 5.0 at 25°C


substrate_name: 4-nitrophenyl beta-lactoside

proof_lines:
pH 5.7, 37°C, wild-type enzyme
wild type enzyme, at pH 5.0 and 27°C

substrate: 4-nitrophenyl beta-lactoside


substrate_name: 4-methylumbelliferyl beta-lactoside

substrate: 4-methylumbelliferyl beta-lactoside


substrate_name: 2,4-dinitrophenyl beta-lactoside

substrate: 2,4-dinitrophenyl beta-lactoside


enzyme_display_name: UMP/CMP kinase

organism: Tetrahymena pyriformis

substrate_name: ATP

assay_conditions_summary: cofactor ATP

enzyme: UMP/CMP kinase

substrate: ATP


enzyme_display_name: nucleoside-diphosphate kinase

organism: Acanthamoeba polyphaga Mimivirus

substrate_name: dTDP

assay_conditions_summary: pH 7.5; cofactor ATP

enzyme: nucleoside-diphosphate kinase

substrate: dTDP


organism: Avena sativa

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 8.0
cosubstrate dTDP, 30°C, pH 8.0
cosubstrate ATP, 30°C, pH 8.0


assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines:
pH 7.5, 37°C
cosubstrate ATP, pH 7.5, 37°C


organism: Halomonas sp.

substrate_name: GTP

assay_conditions_summary: pH 8

proof_lines:
pH 8.0
pH 8.0, presence of 0.2 M NaCl
pH 8.0, presence of 0.5 M NaCl

substrate: GTP


organism: Lathyrus oleraceus


organism: Plasmodium falciparum


organism: Pseudomonas sp.

proof_lines:
pH 8.0
pH 8.0, presence of 0.5 M NaCl
pH 8.0, presence of 0.2 M NaCl


organism: Rattus norvegicus

substrate_name: UDP

proof_lines: cosubstrate ATP, membrane-associated kinase

substrate: UDP


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
cosubstrate ATP, 37°C, pH 7.6
37°C, pH 7.6
cosubstrate ATP


organism: Saccharum officinarum


organism: Spinacia oleracea

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: cosubstrate GDP, NDP-kinase II, 37°C, pH 7.4

proof_lines: cosubstrate ATP, NDP-kinase I and II, 37°C, pH 7.4


enzyme_display_name: oleoyl-[acyl-carrier-protein] hydrolase

organism: Helianthus annuus

substrate_name: palmitoleoyl-[acyl-carrier protein]

enzyme: oleoyl-[acyl-carrier-protein] hydrolase

substrate: palmitoleoyl-[acyl-carrier protein]


organism: Mangifera indica

substrate_name: oleoyl-[acyl-carrier protein]

substrate: oleoyl-[acyl-carrier protein]


organism: Umbellularia californica

substrate_name: decanoyl-[acyl-carrier protein]

substrate: decanoyl-[acyl-carrier protein]


organism: Anabaena sp.

proof_lines: pH and temperature not specified in the publication


organism: Corynebacterium glutamicum


organism: Dictyostelium discoideum

substrate_name: cAMP

proof_lines:
isoform PDE7, 22°C, pH 7.0
isoform PDE3, 22°C, pH 7.0
isoform PDE2, 22°C, pH 7.0

substrate: cAMP


organism: Drosophila melanogaster


organism: Homo sapiens

proof_lines: catalytic domain of PDE2A (PDE2A residues 578-919), enzyme expressed in Escherichia coli


organism: Mus musculus

proof_lines:
soluble enzyme
particulate enzyme


organism: Mycobacterium tuberculosis


organism: Myxococcus xanthus

assay_conditions_summary: pH 8; 313.15 K; cofactor ATP

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

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

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


organism: Pseudomonas aeruginosa

sequence_source: RCSB:5B6A; UniProt:Q9HT57

sequence_variant_note: Resolved canonical sequence from RCSB:5B6A; UniProt:Q9HT57 and applied mutation signature C124A to reconstruct the assayed variant sequence.


substrate_name: pyridoxal

substrate: pyridoxal


organism: Sus scrofa

assay_conditions_summary: pH 6; 310.15 K; cofactor ATP


organism: Trypanosoma brucei

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines: recombinant enzyme, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C


organism: Dictyostelium sp.

substrate_name: dCMP

substrate: dCMP


substrate_name: UMP

substrate: UMP


organism: Escherichia coli

substrate_name: CMP; ATP

substrate: CMP; ATP


proof_lines:
pH 7.4, 37°C, His-tagged UMP-CMP kinase
pH 7.4, 37°C, GST fusion UMP-CMP kinase
pH 7.4, 37°C, GST fusion UMP/CMP kinase


organism: Rattus norvegicus

assay_conditions_summary: pH 7.1; 310.15 K; cofactor ATP

proof_lines:
reaction with dATP, liver enzyme
reaction with ATP, liver enzyme
pH 7.1, 37°C


organism: Saccharomyces cerevisiae


proof_lines:
pH 7.0, 25°C, AUA chimeric enzyme
pH 7.0, 25°C, UMP-CMP kinase
pH 7.0, 25°C, UAU chimeric enzyme


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

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

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


organism: Sinorhizobium fredii


organism: Trypanosoma cruzi


organism: Xenopus laevis


enzyme_display_name: protein O-GlcNAcase

sequence_source: UniProtKB reviewed accession O60502 (direct EC 3.2.1.169 + Homo sapiens lookup)

enzyme: protein O-GlcNAcase


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O60502 with D174A reconstructed from selected source note and PMID 16533067 and applied mutation signature D174A to reconstruct the assayed variant sequence.

proof_lines:
D174A mutant (pH 7.4)
D174A mutant (pH 5.0)


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession O60502 with D175A reconstructed from selected source note and PMID 16533067 and applied mutation signature D175A to reconstruct the assayed variant sequence.


proof_lines:
OGA-FL
OGA-NV
for OGA-FL


proof_lines: compared to the control, pancreas of rats treated with saline

proof_lines: compared to the control, muscles of rats treated with saline


organism: Acetivibrio thermocellus

substrate_name: Avicel

substrate: Avicel


enzyme_display_name: glutamyl aminopeptidase

organism: Tetragenococcus halophilus

substrate_name: Glu-p-nitroanilide

enzyme: glutamyl aminopeptidase

substrate: Glu-p-nitroanilide


enzyme_display_name: ubiquitinyl hydrolase 1

substrate_name: Unknown

ki_unit: mM

enzyme: ubiquitinyl hydrolase 1

substrate: Unknown


organism: Oryctolagus cuniculus

proof_lines:
at 0.0006 mM ubiquitin, pH 7.8, 25°C
in absence of ubiquitin, pH 7.8, 25°C


organism: Oryza sativa

proof_lines: pH 8.0, temperature not specified in the publication, ubiquitin C-terminal hydrolase OsUCH3


organism: synthetic construct

proof_lines:
with UCH-L3
with UCH-L1


enzyme_display_name: coagulation factor VIIa

organism: Bos taurus

enzyme: coagulation factor VIIa


organism: Homo sapiens

substrate_name: Factor X

proof_lines: mutant enzyme E154A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles

substrate: Factor X


proof_lines: mutant enzyme L192A or E154A, tissue factor/phosphatidylcholine vesicles


proof_lines: mutant enzyme L144A, tissue factor/phosphatidylcholine vesicles

proof_lines: mutant enzyme L144A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles


proof_lines: mutant enzyme K192A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles

proof_lines: mutant enzyme K192A, tissue factor/phosphatidylcholine vesicles


proof_lines: mutant enzyme L192A, tissue factor/phosphatidylcholine-phosphatidylserine vesicles


proof_lines: pH 8.0, 37°C, mutant enzyme M156Q, addition of tissue factor


proof_lines: wild-type enzyme VIIa, tissue factor/phosphatidylcholine-phosphatidylserine vesicles


substrate_name: D-Ile-Pro-Arg-p-nitroanilide

proof_lines: pH 8.0, 30°C, mutant enzyme DELTA360-329, without tissue factor

proof_lines: pH 8.0, 30°C, mutant enzyme DELTA360-329, activated by tissue factor

substrate: D-Ile-Pro-Arg-p-nitroanilide


proof_lines: mutant enzyme L305V, in absence of tissue factor


proof_lines: mutant enzyme L305V/M306D/D309S, in absence of tissue factor


proof_lines: 37°C, mutant enzyme N100A/H101A/Y179A/F256A


organism: Gallus gallus

substrate_name: Glu-beta-naphthylamide

substrate: Glu-beta-naphthylamide


proof_lines: recombinant enzyme, pH 7.5, 37°C, in absence of Ca2+

proof_lines: recombinant enzyme, pH 7.5, 37°C, in presence of 1 mM Ca2+


proof_lines: mutant D221N, in the presence of 1.0 mM CaCl2


proof_lines: mutant D221E, in the presence of 1.0 mM CaCl2


proof_lines: mutant D221Q, in the presence of 1.0 mM CaCl2


proof_lines: mutant D221, in the presence of 1 mM CaCl2


substrate_name: angiotensin II

proof_lines: wild-type, in the presence of 1.0 mM CaCl2

proof_lines: wild-type enzyme, in the absence of CaCl2

substrate: angiotensin II


proof_lines: mutant D221A, in the presence of 1.0 mM CaCl2


organism: Lactococcus lactis

substrate_name: Asp-Ala

substrate: Asp-Ala


organism: Lactococcus lactis ssp. lactis


organism: Mus musculus


organism: Streptomyces coelicolor

substrate_name: ATP

sequence_source: UniProtKB P50589 from direct EC 2.7.4.6 + Streptomyces coelicolor lookup

assay_conditions_summary: 300.15 K; cofactor ATP

substrate: ATP


organism: Thermus thermophilus

substrate_name: GDP

substrate: GDP


organism: white spot syndrome virus

substrate_name: dTDP

proof_lines: pH 7.5, temperature not specified in the publication

substrate: dTDP


organism: Brassica rapa subsp. oleifera

substrate_name: oleoyl-[acyl-carrier protein]

substrate: oleoyl-[acyl-carrier protein]


organism: Camelina sativa

substrate_name: stearoyl-[acyl-carrier protein]

substrate: stearoyl-[acyl-carrier protein]


organism: Cuphea lanceolata

proof_lines:
medium-chain acyl-ACP thioesterase
oleoyl-ACP thioesterase


organism: Diploknema butyracea

substrate_name: palmitoyl-[acyl-carrier protein]

substrate: palmitoyl-[acyl-carrier protein]


organism: Helianthus annuus

proof_lines: pH 8.0, 22°C, recombinant His-tagged enzyme

proof_lines: isoform FatA, palmitoyl-[acyl-carrier protein] from Escherichia coli, at pH 8.0, temperature not specified in the publication

proof_lines: isoform FatB, palmitoyl-[acyl-carrier protein] from Escherichia coli, at pH 8.0, temperature not specified in the publication


substrate_name: palmitoleoyl-[acyl-carrier protein]

substrate: palmitoleoyl-[acyl-carrier protein]


proof_lines: mutant enzyme C164V/V299C FVIIa, in the presence of tissue factor, pH 7.4


proof_lines: mutant enzyme L280I/V299M-FVIIa, in the presence of tissue factor, pH 7.4


proof_lines: mutant enzyme V299M-FVIIa, in the presence of tissue factor, pH 7.4


organism: Rattus norvegicus


enzyme_display_name: coagulation factor XIa

substrate_name: factor IX

proof_lines: in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C

enzyme: coagulation factor XIa

substrate: factor IX


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

proof_lines: wild type enzyme, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme I151A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192E, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192Q, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme Y5901A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: kcat less than 0.2 s-1, mutant enzyme E98D, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


enzyme_display_name: non-specific protein-tyrosine kinase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

source_db: uniprot

proof_lines: kcat is 27.23 min(-1) for lipopolysaccharide kinase activity.

enzyme: non-specific protein-tyrosine kinase

source: uniprot


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: ADP

assay_conditions_summary: cofactor ADP

proof_lines: kcat is 248 sec(-1) with glucose as substrate. kcat is 120 sec(-1) with glucosamine as substrate. kcat is 210 sec(-1) with ADP as substrate.

substrate: ADP


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

substrate_name: cAMP

proof_lines: kcat is 2008 min(-1) and 957 min(-1) with cAMP and cGMP as substrate, respectively.

substrate: cAMP


organism: Homo sapiens

substrate_name: 3',5'-cyclic GMP

proof_lines: kcat is 0.6 sec(-1) with 3',5'-cyclic GMP as substrate (PubMed:15938621). kcat is 0.12 sec(-1) with 3',5'-cyclic AMP as substrate (PubMed:15938621).

substrate: 3',5'-cyclic GMP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

proof_lines: kcat is 2.8 sec(-1) with 2',3'-cAMP as substrate. kcat is 0.55 sec(-1) with pNPP as substrate. kcat is 12.4 sec(-1) with bis(pNPP) as substrate.


substrate_name: linear diubiquitin

proof_lines: kcat is 6.3 sec(-1) with linear diubiquitin as substrate.

substrate: linear diubiquitin


substrate_name: Arg-Leu-Arg-Gly-Gly-AMC

proof_lines: kcat is 4.9 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate (PubMed:29476094). kcat is 0.084 sec(-1) with Ub-Rhodamine as substrate (PubMed:29576528).

substrate: Arg-Leu-Arg-Gly-Gly-AMC


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: ubiquitin-AMC

proof_lines: kcat is 3.2 sec(-1) with ubiquitin-AMC as substrate.

substrate: ubiquitin-AMC


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.17 sec(-1) with ubiquitin-AMC as substrate.


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

proof_lines: kcat is 7.2 sec(-1) with Arg-Leu-Arg-Gly-Gly-AMC as substrate.


organism: Severe acute respiratory syndrome coronavirus

substrate_name: peptide TSAVLQSGFRK-NH(2)

proof_lines: The kinetic parameters are studied for the 3C-like proteinase domain.

substrate: peptide TSAVLQSGFRK-NH(2)


substrate_name: Factor X

substrate: Factor X


proof_lines: pH 6.5, MES buffer, without tissue factor

proof_lines: in 50 mM HEPES, pH 7.4, with 0.1 M NaCl, 5 mM CaCl2, 0.1% (w/v) bovine serum albumin, and 0.01% Tween 80, at 37°C


proof_lines: pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q


proof_lines: pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/L305V


proof_lines: pH 7.4, 37°C, mutant enzyme V158D/D296V/M298Q/K337A


substrate_name: spectrozyme fVIIa

substrate: spectrozyme fVIIa


proof_lines: pH 8.0, mutant enzyme V21N/E154I/M156Q, with addition of tissue factor

proof_lines: pH 8.0, mutant enzyme V21N/E154I/M156Q, without tissue factor

proof_lines: pH 8.0, mutant enzyme V21N/E154I/M156Q, chromozym tPA as substrate without addition of tissue factor


proof_lines:
mutant FVIIaVEAY
mutant FVIIaIIa-sTF
mutant FVIIaVEAY-sTF


enzyme_display_name: chymase

proof_lines:
in presence of heparin proteoglycan
in absence of heparin
pH 7.5, 37°C

enzyme: chymase


enzyme_display_name: tryptase

organism: Bos taurus

enzyme: tryptase


substrate_name: N-p-tosyl-Gly-Pro-Arg-p-nitroanilide

substrate: N-p-tosyl-Gly-Pro-Arg-p-nitroanilide


substrate_name: Bz-Arg-p-nitroanilide

proof_lines:
pH 7.6, 20°C, isoform L1
pH 6.0, 25°C, 200 ng protamine
pH 7.6, 20°C, isoform L2

substrate: Bz-Arg-p-nitroanilide


organism: Mus musculus

substrate_name: N-p-tosyl-Gly-Pro-Lys-p-nitroanilide

proof_lines:
pH 6.0, 25°C, 1200 ng polybrene
pH 6.0, 25°C, 1000 ng polybrene
pH 6.0, 25°C, 800 ng polybrene

substrate: N-p-tosyl-Gly-Pro-Lys-p-nitroanilide


substrate_name: bovine prothrombin

substrate: bovine prothrombin


enzyme_display_name: cathepsin H

enzyme: cathepsin H


organism: Bubalus bubalis

substrate_name: L-Leu-beta-naphthylamide

substrate: L-Leu-beta-naphthylamide


organism: Capra hircus

substrate_name: Unknown

assay_conditions_summary: pH 7; 310.15 K; buffer 0.1 M acetate

proof_lines:
pH 7, 37°C
at pH 7.0 and 37°C
pH 5, 37°C

substrate: Unknown


organism: Cyprinus carpio


proof_lines: mutant T11_E18del-cathepsin H, pH 6.8, 30°C

proof_lines: pH 6.5, 25°C, mutant lacking the mini chain


enzyme_display_name: nicotinamidase

organism: Arabidopsis thaliana

substrate_name: nicotinamide

enzyme: nicotinamidase

substrate: nicotinamide


organism: Aspergillus niger


organism: Borreliella burgdorferi

assay_conditions_summary: pH 7.3; 298.15 K; buffer 100 mM phosphate

proof_lines: wild type enzyme, in 100 mM phosphate buffer, pH 7.3 at 25°C


proof_lines: in 100 mM phosphate buffer, pH 7.3 at 25°C


organism: Caenorhabditis elegans

proof_lines: wild type enzyme isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C

proof_lines: wild type enzyme isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C


proof_lines: isoform PNC1, in 100 mM phosphate buffer, pH 7.3 at 25°C

proof_lines: isoform PNC2, in 100 mM phosphate buffer, pH 7.3 at 25°C


organism: Escherichia coli


organism: Flavobacterium peregrinum


organism: Micrococcus luteus


organism: Mycobacterium tuberculosis

proof_lines: Ki about 0.1 mM, wild type enzyme, in 100 mM HEPES at pH 8.0 and 25°C


proof_lines: mutant enzyme H57D, in 100 mM HEPES at pH 8.0 and 25°C


organism: Plasmodium falciparum


assay_conditions_summary: pH 7.5; 310.15 K; buffer 100 mM phosphate


organism: Pseudomonas sp.


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


assay_conditions_summary: pH 7.3; 298.15 K; buffer notes


organism: Streptococcus pneumoniae


assay_conditions_summary: pH 7.3; 298.15 K; buffer notes but no substrate


organism: unidentified

substrate_name: ethylnicotinate

proof_lines: pH 7.3, temperature not specified in the publication, substrate: pyrazinamide

substrate: ethylnicotinate


enzyme_display_name: glutathionylspermidine amidase

organism: Crithidia fasciculata

substrate_name: glutathionylspermidine

assay_conditions_summary: pH 7.3; cofactor ATP

proof_lines:
pH 7.3, amidase activity
pH 7.3, synthetase activity

enzyme: glutathionylspermidine amidase

substrate: glutathionylspermidine


organism: Homo sapiens

proof_lines:
pH 6.0, enzyme from normal tissue
pH 6.0, enzyme from meningioma
pH 6.8, 22°C


organism: Oryctolagus cuniculus


organism: Sus scrofa

proof_lines:
pH 6.5, 25°C, native enzyme
similar value


enzyme_display_name: cathepsin K

enzyme: cathepsin K


assay_conditions_summary: pH 7.4; 298.15 K; buffer 100 mM sodium acetate

proof_lines: enzyme in the presence of 300 mM NaCl, in 50 mM HEPES, pH 7.4, containing 1 mM EDTA and 2.5 mM dithiothreitol, at 25°C

proof_lines: enzyme in the absence of NaCl, in 50 mM HEPES, pH 7.4, containing 1 mM EDTA and 2.5 mM dithiothreitol, at 25°C


proof_lines: tert-butyloxycarbonyl-Ala-Gly-Pro- Arg 4-methylcoumarin 7-amide


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: cruzipain

organism: Trypanosoma congolense

enzyme: cruzipain


organism: Trypanosoma cruzi

proof_lines: at pH 6.5 the propeptide of cruzipain inactivates cruzipain competitively


enzyme_display_name: dihydropyrimidinase

organism: Geobacillus stearothermophilus

substrate_name: DL-hydroxyphenylhydantoin

enzyme: dihydropyrimidinase

substrate: DL-hydroxyphenylhydantoin


substrate_name: dihydrouracil

substrate: dihydrouracil


organism: Geobacillus thermocatenulatus

substrate_name: p-hydroxyphenylhydantoin

substrate: p-hydroxyphenylhydantoin


organism: Niallia circulans

substrate_name: allantoin

substrate: allantoin


organism: Pseudomonas fluorescens


organism: Pseudomonas putida


substrate_name: H2O; 5,6-Dihydrouracil

substrate: H2O; 5,6-Dihydrouracil


organism: Sinorhizobium meliloti


organism: Vigna angularis


enzyme_display_name: arginine deiminase

organism: Aspergillus fumigatus

substrate_name: L-lysine

proof_lines: pH 7.0, 45°C, enzyme covalently immobilized on dextran

enzyme: arginine deiminase

substrate: L-lysine


organism: Aspergillus nidulans

substrate_name: L-arginine

substrate: L-arginine


organism: Bacillus cereus


organism: Burkholderia mallei

proof_lines:
pH 5.6, 25°C
at pH 5.6 and 25°C


organism: Escherichia coli

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


organism: Giardia duodenalis

substrate_name: L-canavanine

substrate: L-canavanine


organism: Halobacterium salinarum


organism: Lactococcus lactis subsp. lactis


organism: Lentilactobacillus buchneri

assay_conditions_summary: pH 6


organism: Metamycoplasma arthritidis

substrate_name: L-Arg

proof_lines:
ammonium assay at 25°C
at pH 7.2, 25°C
ammonium assay at 37°C

substrate: L-Arg


organism: Metamycoplasma hominis

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


organism: Porphyromonas gingivalis

substrate_name: L-Pro-L-Phe-L-Arg

proof_lines: in 50 mM CHES/HCl, pH 9.5 containing 10 mM dithiothreitol, at 37°C

substrate: L-Pro-L-Phe-L-Arg


organism: Pseudomonas aeruginosa


organism: Agrobacterium sp.

substrate_name: hydantoin

substrate: hydantoin


organism: Agrobacterium tumefaciens

proof_lines:
at 25°C
at 40°C
at 20°C


organism: Blastobacter sp.

substrate_name: H2O; Hydantoin

substrate: H2O; Hydantoin


organism: Bos taurus

substrate_name: Hydrothymine

substrate: Hydrothymine


organism: Burkholderia cepacia

substrate_name: D,L-benzylhydantoin

proof_lines:
free enzyme, at pH 8.5 and 45°C
immobilized enzyme, at pH 8.5 and 45°C

substrate: D,L-benzylhydantoin


organism: Crystallibacter crystallopoietes

substrate_name: phenylhydantoin

substrate: phenylhydantoin


organism: Geobacillus stearothermophilus


substrate_name: Nomega-methyl-L-arginine

substrate: Nomega-methyl-L-arginine


organism: Pseudomonas plecoglossicida

assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.5 M phosphate

proof_lines: wild type enzyme, in 0.5 M phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K5T/D44E/H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C


assay_conditions_summary: pH 7.4; 310.15 K; buffer phosphate

proof_lines: mutant enzyme H404R, in 0.5 M phosphate buffer, pH 7.4, at 37°C


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R299K


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R319K


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R338K


proof_lines: pH 7.4, 55°C, M31 mutant enzyme R299K/R382K

proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R299K/R382K


proof_lines: pH 7.4, 55°C, PEGylated M31 mutant enzyme R382K


proof_lines: pH 7.4, 55°C, PEGylated variant M31 (parent)

proof_lines: pH 7.4, 55°C, variant M31 (parent enzyme)


organism: Pseudomonas putida


organism: Streptococcus pyogenes

proof_lines: pH and temperature not specified in the publication


organism: Trichomonas vaginalis

proof_lines:
strain MR-5
strain MR-100
at pH 6.0 and 37°C


organism: Tritrichomonas foetus


enzyme_display_name: (R)-2-methylmalate dehydratase

organism: Pseudomonas sp.

enzyme: (R)-2-methylmalate dehydratase


organism: Homo sapiens

proof_lines: mutant enzyme Y5901V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192R, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme K192A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: mutant enzyme R3704A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


substrate_name: factor IX

proof_lines: kcat less than 0.2 s-1, mutant enzyme E98V, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C

substrate: factor IX


proof_lines: kcat less than 0.2 s-1, mutant enzyme Y143A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


proof_lines: kcat less than 0.2 s-1, mutant enzyme E98A, in 50 mM Tris-HCl, 150 mM NaCl, 5 mM CaCl2, 0.5% (w/v) bovine serum albumin, pH 7.3, at 37°C


organism: Canis lupus familiaris


proof_lines: in the presence of heparin, at pH 7.4 and 37°C

proof_lines: in the absence of heparin, at pH 7.4 and 37°C


organism: Mesocricetus auratus

substrate_name: angiotensin I

substrate: angiotensin I


organism: Mus musculus

proof_lines:
enzyme form 1A
enzyme form 1E
enzyme form 1B


enzyme_display_name: chitosanase

organism: Streptomyces sp. N174

substrate_name: chitosan

sequence_source: UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844

sequence_variant_note: Mutation signature T45S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant T45S, assayed as the amount of D-glucosamine released from chitosan

enzyme: chitosanase

substrate: chitosan


sequence_variant_note: Resolved canonical sequence from UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844 and applied mutation signature D40G/T45D with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.

proof_lines: mutant D40G/T45D, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature T45E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant T45E, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Resolved canonical sequence from UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844 and applied mutation signature E36Q/D40G with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.

proof_lines: mutant E36Q/D40G, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Resolved canonical sequence from UniProtKB P33665 canonical precursor with mature-chain mutation reconstruction from PMID 19143844 and applied mutation signature E36A/D40G with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.

proof_lines: mutant E36A/D40G, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature E36D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E36D, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature D40G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant D40G, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature E36A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E36A, assayed as the amount of D-glucosamine released from chitosan


organism: Bacillus subtilis

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


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


organism: Gynuella sunshinyii


sequence_variant_note: Mutation signature L117D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature N21W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature D236A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E206Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature E149Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: uracil-DNA glycosylase

organism: Thermus thermophilus

substrate_name: double stranded DNA containing G-U mismatch

sequence_source: UniProtKB Q5SKC5 canonical protein sequence from direct accession lookup

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

enzyme: uracil-DNA glycosylase


substrate_name: DNA; H2O

sequence_source: UniProtKB Q5SKC5 canonical sequence used only as mutation-position context; row-specific variant sequence unresolved

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

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E41Q-G42D C-terminal His6-tagged

proof_lines: mutant enzyme E41Q/G42D, at pH 7.6 and 60°C

substrate: DNA; H2O


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E41Q C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E47A C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant H155S C-terminal His6-tagged


substrate_name: H2O; DNA

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant E41A-G42D C-terminal His6-tagged

substrate: H2O; DNA


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant F54A C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant N89A C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant N80A C-terminal His6-tagged


organism: Vibrio cholerae

substrate_name: dUMP DNA

sequence_source: UniProtKB Q9KPK8 canonical sequence used only as mutation-position context; row-specific variant sequence unresolved

substrate: dUMP DNA


sequence_source: UniProtKB Q9KPK8 canonical protein sequence from direct accession lookup


enzyme_display_name: low-specificity L-threonine aldolase

organism: Aphanothece halophytica

substrate_name: L-erythro-phenylserine

verification_status: unverified

enzyme: low-specificity L-threonine aldolase

substrate: L-erythro-phenylserine

status: unverified


organism: Arabidopsis thaliana

substrate_name: L-Threonine

sequence_source: UniProtKB Q8RXU4 canonical protein sequence from direct accession lookup

substrate: L-Threonine


sequence_source: UniProtKB Q9FPH3 canonical protein sequence from direct accession lookup


organism: Escherichia coli

sequence_source: UniProtKB:P12295 direct accession lookup


substrate_name: 5-hydroxymethyluracil-mismatched double-stranded DNA with U-G mismatch


substrate_name: uracil-mismatched double-stranded DNA with U-G mismatch

sequence_source: UniProtKB:Q53HV7 direct accession lookup


sequence_source: UniProtKB:P13051 direct accession lookup for canonical context only

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant H268N


sequence_source: UniProtKB:P13051 direct accession lookup

unit: Mswedgeone


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13051 direct accession lookup plus direct mutation reconstruction and applied mutation signature D145N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant D145N


substrate_name: uracil-containing calf thymus DNA

proof_lines:
mutant enzyme D183G, at pH 7.5 and 15°C
mutant enzyme D183G, at pH 7.5 and 22°C
mutant enzyme D183G, at pH 7.5 and 37°C

substrate: uracil-containing calf thymus DNA


proof_lines: mutant enzyme D183G/K302R, at pH 7.5 and 15°C

proof_lines: mutant enzyme D183G/K302R, at pH 7.5 and 22°C

proof_lines: mutant enzyme D183G/K302R, at pH 7.5 and 37°C


proof_lines:
wild type enzyme, at pH 7.5 and 15°C
wild type enzyme, at pH 7.5 and 22°C
wild type enzyme, at pH 7.5 and 37°C


organism: Human herpesvirus 1

sequence_variant_note: Resolved canonical sequence from UniProtKB:P10186 direct accession lookup plus direct mutation reconstruction and applied mutation signature D88N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant D88N


sequence_source: UniProtKB:P10186 direct accession lookup for canonical context only

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant H210N


organism: Mesoplasma lactucae

sequence_source: UniProtKB:A0A291IS31 direct accession lookup


organism: Monkeypox virus

substrate_name: uracil-mismatched double-stranded DNA

sequence_source: UniProtKB:Q8V4Y4 direct accession lookup

proof_lines: pH 7.5, 37°C, excision of a single uracil residue from U-A, recombinant enzyme

proof_lines: pH 7.0, 37°C, excision of a single uracil residue from U-G, recombinant enzyme

proof_lines: pH 7.5, 37°C, excision of a single uracil residue from PS-U, recombinant enzyme

substrate: uracil-mismatched double-stranded DNA


organism: Orthopoxvirus vaccinia

sequence_source: UniProtKB:P20536 direct accession lookup

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


substrate_name: uracil-mismatched single-stranded DNA

sequence_source: UniProtKB:Q5SKC5 direct accession lookup

substrate: uracil-mismatched single-stranded DNA


sequence_source: UniProtKB:Q5SKC5 direct accession lookup for canonical context only

proof_lines: SABIO-RK modifier species: uracil-DNA glycosylase(Enzyme) mutant G42D C-terminal His6-tagged


organism: Abelson murine leukemia virus

substrate_name: Protein tyrosine; ATP

proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant Y59W fusion protein to glutathione S-transferase

substrate: Protein tyrosine; ATP


substrate_name: ATP; Protein tyrosine

proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant L444E fusion protein to glutathione S-transferase

substrate: ATP; Protein tyrosine


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant W525H fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant Y59L fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant I523V fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant L444K fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant F521A fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant G556V fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant S558N fusion protein to glutathione S-transferase


proof_lines: SABIO-RK modifier species: non-specific protein-tyrosine kinase(Enzyme) mutant W525F fusion protein to glutathione S-transferase


organism: Homo sapiens

substrate_name: ATP; Peptide

substrate: ATP; Peptide


substrate_name: Unknown

proof_lines:
30°C, Lck
30°C, Src

substrate: Unknown


organism: Opisthokonta

substrate_name: p-cyclin_cdc2; ATP

assay_conditions_summary: cofactor ATP

substrate: p-cyclin_cdc2; ATP


substrate_name: H2O; 4-Nitrophenyl phenyl phosphonate

sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q13822 (ENPP2_HUMAN)

substrate: H2O; 4-Nitrophenyl phenyl phosphonate


sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q9R1E6 (ENPP2_MOUSE)


sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q9CRY7 (GDPD1_MOUSE)

proof_lines: pH 7.4, temperature not specified in the publication


sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q99LY2 (GDPD3_MOUSE)


organism: Rattus norvegicus

substrate_name: 1-Acyl-sn-glycero-3-phosphocholine; H2O

sequence_source: UniProtKB REST direct accession check on 2026-06-17: Q64610 (ENPP2_RAT)

substrate: 1-Acyl-sn-glycero-3-phosphocholine; H2O


organism: Aspergillus sp. W-2

substrate_name: chitosan

sequence_source: UniProtKB REST direct accession check on 2026-06-17: A0A0B5L773 (A0A0B5L773_9EURO)


organism: Bacillus sp. TS

sequence_source: UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI)


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318N and applied mutation signature D318N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318K and applied mutation signature D318K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318R and applied mutation signature D318R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318E and applied mutation signature D318E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession check on 2026-06-17: A0A167KLN5 (A0A167KLN5_9BACI); row-specific reconstruction for D318A and applied mutation signature D318A to reconstruct the assayed variant sequence.


organism: Microbacterium sp.

sequence_source: UniProtKB REST direct accession check on 2026-06-17: A7KBW5 (A7KBW5_9MICO)


organism: Paenibacillus ehimensis

sequence_source: UniProtKB REST direct accession check on 2026-06-17: O24825 (O24825_9BACL)

proof_lines: 40°C, pH not specified in the publication, wild-type enzyme, calculated as micromol reducing sugar liberated from chitosan


organism: Caulobacter vibrioides

substrate_name: L-allo-Threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y and applied mutation signature D95Y to reconstruct the assayed variant sequence.

substrate: L-allo-Threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95M and applied mutation signature D95M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95N/E96S and applied mutation signature D95N/E96S to reconstruct the assayed variant sequence.


substrate_name: L-threonine

sequence_source: UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y

substrate: L-threonine


sequence_source: UniProtKB REST accession Q9A3V8


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95G/E96G and applied mutation signature D95G/E96G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95G/E96G


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95L and applied mutation signature D95L to reconstruct the assayed variant sequence.


substrate_name: L-allo-threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95W and applied mutation signature D95W to reconstruct the assayed variant sequence.

substrate: L-allo-threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y/E96T and applied mutation signature D95Y/E96T to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST accession Q9A3V8; row-specific variant reconstructed from mutation_signature D95Y/E96T


substrate_name: L-Threonine

sequence_source: UniProtKB REST accession P75823

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


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature K222A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-Threonine', enzyme heading 'K222A'; the enzyme heading spans three numeric columns: column 'kcat' = 43, column 'Km' = 72, column 'kcat/Km' = 0.6. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 43 min^-1; 43 / 60 = 0.7166666667 s^-1; the exported value is 0.72 s^(-1). km: printed Table 4 cell 72 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 72.0 mM. kcat/Km: printed Table 4 cell 0.6 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.6 / 60 = 0.01 s^-1 mM^-1; the exported value is 0.01 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-Threonine', enzyme column 'K222A': kcat = 43 min^-1; Km = 72 mM; printed kcat/Km = 0.6 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.

table_label: Table 4: Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine (FEBS J. 2014, 281(1):129-145)

status: corrected


column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-allo-Threonine', enzyme heading 'K222A'; the enzyme heading spans three numeric columns: column 'kcat' = 80, column 'Km' = 1.2, column 'kcat/Km' = 67. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 80 min^-1; 80 / 60 = 1.3333333333 s^-1; the exported value is 1.33 s^(-1). km: printed Table 4 cell 1.2 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 1.2 mM. kcat/Km: printed Table 4 cell 67 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 67 / 60 = 1.1166666667 s^-1 mM^-1; the exported value is 1.1083333333333334 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-allo-Threonine', enzyme column 'K222A': kcat = 80 min^-1; Km = 1.2 mM; printed kcat/Km = 67 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature H83F/H126F to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-allo-Threonine', enzyme heading 'H83F/H126F'; the enzyme heading spans three numeric columns: column 'kcat' = 1.7, column 'Km' = 7.4, column 'kcat/Km' = 0.23. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 1.7 min^-1; 1.7 / 60 = 0.0283333333 s^-1; the exported value is 0.028 s^(-1). km: printed Table 4 cell 7.4 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 7.4 mM. kcat/Km: printed Table 4 cell 0.23 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 0.23 / 60 = 0.0038333333 s^-1 mM^-1; the exported value is 0.0037837837837837837 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-allo-Threonine', enzyme column 'H83F/H126F': kcat = 1.7 min^-1; Km = 7.4 mM; printed kcat/Km = 0.23 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P75823 and applied mutation signature F87A to reconstruct the assayed variant sequence.

column_label: Table 4 (Kinetic parameters of the retro-aldol cleavage reactions catalysed by wild type and mutant eTAs with the threo and erythro isomers of L-threonine), substrate row 'L-Threonine', enzyme heading 'F87A'; the enzyme heading spans three numeric columns: column 'kcat' = 43, column 'Km' = 8.7, column 'kcat/Km' = 4.9. Footnote a gives kcat in min^-1 and footnote b gives Km in mM, so the third column is in min^-1 mM^-1.

normalized_value_unit_evidence: kcat: printed Table 4 cell 43 min^-1; 43 / 60 = 0.7166666667 s^-1; the exported value is 0.72 s^(-1). km: printed Table 4 cell 8.7 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 8.7 mM. kcat/Km: printed Table 4 cell 4.9 min^-1 mM^-1; 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 4.9 / 60 = 0.0816666667 s^-1 mM^-1; the exported value is 0.08275862068965517 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, substrate row 'L-Threonine', enzyme column 'F87A': kcat = 43 min^-1; Km = 8.7 mM; printed kcat/Km = 4.9 min^-1 mM^-1. Footnote a of Table 4 gives the kcat unit as min^-1 and footnote b gives the Km unit as mM; the third numeric column of each enzyme heading is the specificity constant kcat/Km, which the paper itself reads that way when it computes the wild-type substrate preference as 887/5.8 = 153.


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

proof_lines: 40°C, pH not specified in the publication, mutant enzyme A207C/L286C, calculated as micromol reducing sugar liberated from chitosan

substrate: chitosan


organism: Paenibacillus sp.

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


organism: Streptomyces sp.

sequence_source: UniProtKB:P33665 reviewed canonical sequence checked during exact accession review

assay_conditions_summary: pH 5.5; 310.15 K; buffer 50 mM sodium acetate

proof_lines: wild type enzyme, at 37°C in 50 mM sodium acetate buffer (pH 5.5)


proof_lines: mutant enzyme R42E at 37°C in 50 mM sodium acetate buffer (pH 5.5)


proof_lines: mutant enzyme R42K, at 37°C in 50 mM sodium acetate buffer (pH 5.5)


proof_lines: chitosan with less than 75% deacetylation, at pH 6.0 and 45°C

proof_lines: chitosan with 75-85% deacetylation, at pH 6.0 and 45°C

proof_lines: chitosan with more than 90% deacetylation, at pH 6.0 and 45°C


substrate_name: Chitosan; H2O

proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E22A

unit: lgwedgeoneswedgeone

substrate: Chitosan; H2O


substrate_name: H2O; Chitosan

substrate: H2O; Chitosan


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E22D


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D40E


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E36Q


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D37N


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant E22Q


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D37E


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D40N


proof_lines: SABIO-RK modifier species: chitosanase(Enzyme) mutant D6N


substrate_name: 30% N-acetylated chitosan

sequence_source: UniProtKB reviewed accession P33665 direct lookup; variant reconstructed from source mutation label.

sequence_variant_note: Mutation signature W28F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: 30% N-acetylated chitosan


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -10, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P33665 direct lookup; variant reconstructed from source mutation label. and applied mutation signature W28F/W101F with inferred residue-numbering offset +40 to reconstruct the assayed variant sequence.


organism: Streptomyces sp. N174

sequence_source: UniProtKB reviewed accession P33665 direct lookup.

proof_lines: wild-type, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

proof_lines: mutant E36Q, assayed as the amount of D-glucosamine released from chitosan


sequence_variant_note: Mutation signature E36N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant E36N, assayed as the amount of D-glucosamine released from chitosan


organism: Archaeoglobus fulgidus

sequence_source: UniProtKB reviewed accession O28007 direct lookup.

proof_lines:
pH 7.8, 95°C
pH 7.5, 80°C, recombinant enzyme
pH 7.5, 80°C


substrate_name: uracil-mismatched double-stranded DNA

proof_lines: pH 7.5, 80°C, cell extract (wild-type enzyme)


organism: Bacillus subtilis

substrate_name: DNA; H2O

sequence_source: UniProtKB reviewed accession P39615 direct lookup.

substrate: DNA; H2O


organism: Chlamydia pneumoniae

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9Z7D3 direct lookup; variant reconstructed from source mutation label. and applied mutation signature H200Q to reconstruct the assayed variant sequence.

substrate: uracil-mismatched double-stranded DNA


substrate_name: uracil-mismatched double-stranded DNA with A-U mismatch +

sequence_source: UniProtKB reviewed accession Q9Z7D3 direct lookup.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9Z7D3 direct lookup; variant reconstructed from source mutation label. and applied mutation signature A205S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9Z7D3 direct lookup; variant reconstructed from source mutation label. and applied mutation signature D77N to reconstruct the assayed variant sequence.


organism: Deinococcus radiodurans

sequence_source: UniProtKB reviewed accession Q9RWH9 direct lookup.


organism: Escherichia coli


enzyme_display_name: 4-hydroxyacetophenone monooxygenase

organism: Pseudomonas fluorescens

sequence_source: UniProtKB reviewed entry Q93TJ5 / HAPMO_PSEFL direct lookup

enzyme: 4-hydroxyacetophenone monooxygenase


substrate_name: methyl 4-tolyl sulfide

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Methyl 4-tolyl sulfide'; column 'Km (uM)' = 370 (50); column 'kcat (s^-1)' = 7.3 (0.6); column 'kcat/Km (10^3 s^-1 . M^-1)' = 20; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 370 uM; 370 / 1000 = 0.37 mM. kcat: printed Table 1 cell 7.3 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 7.3 s^(-1). kcat/Km: printed Table 1 cell 20 in the column headed 10^3 s^-1 M^-1, that is 20000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20000 / 1000 = 20 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Methyl 4-tolyl sulfide': Km = 370 uM; kcat = 7.3 s^-1; printed kcat/Km = 20 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Methyl 4-tolyl sulfide'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

table_label: Table 1: Steady-state kinetic parameters for HAPMO (Appl. Environ. Microbiol. 2003, 69(1):419-426)

substrate: methyl 4-tolyl sulfide


substrate_name: Benzaldehyde

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Benzaldehyde'; column 'Km (uM)' = 1,600 (200); column 'kcat (s^-1)' = 2.2 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 1.4; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,600 uM; 1600 / 1000 = 1.6 mM. kcat: printed Table 1 cell 2.2 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.2 s^(-1). kcat/Km: printed Table 1 cell 1.4 in the column headed 10^3 s^-1 M^-1, that is 1400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1400 / 1000 = 1.4 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Benzaldehyde': Km = 1,600 uM; kcat = 2.2 s^-1; printed kcat/Km = 1.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Benzaldehyde'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Benzaldehyde


smiles: CC(=O)C(C)Cl

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '3-Chloro-2-butanone'; column 'Km (uM)' = 23,000 (4,000); column 'kcat (s^-1)' = 7.4 (1.0); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.32; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 23,000 uM; 23000 / 1000 = 23 mM. kcat: printed Table 1 cell 7.4 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 7.4 s^(-1). kcat/Km: printed Table 1 cell 0.32 in the column headed 10^3 s^-1 M^-1, that is 320 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 320 / 1000 = 0.32 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '3-Chloro-2-butanone': Km = 23,000 uM; kcat = 7.4 s^-1; printed kcat/Km = 0.32 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '3-Chloro-2-butanone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: NADPH; O2; 4'-Hydroxyacetophenone; H+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH; O2; 4'-Hydroxyacetophenone; H+


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '3-Hydroxyacetophenone'; column 'Km (uM)' = 1,400 (200); column 'kcat (s^-1)' = 4.8 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 3.4; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,400 uM; 1400 / 1000 = 1.4 mM. kcat: printed Table 1 cell 4.8 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 4.8 s^(-1). kcat/Km: printed Table 1 cell 3.4 in the column headed 10^3 s^-1 M^-1, that is 3400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3400 / 1000 = 3.4 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '3-Hydroxyacetophenone': Km = 1,400 uM; kcat = 4.8 s^-1; printed kcat/Km = 3.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '3-Hydroxyacetophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: Hydroxyacetone

smiles: CC(=O)CO

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Hydroxyacetone (acetol)'; column 'Km (uM)' = 29,000 (3,000); column 'kcat (s^-1)' = 4.1 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.14; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 29,000 uM; 29000 / 1000 = 29 mM. kcat: printed Table 1 cell 4.1 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 4.1 s^(-1). kcat/Km: printed Table 1 cell 0.14 in the column headed 10^3 s^-1 M^-1, that is 140 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 140 / 1000 = 0.14 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Hydroxyacetone (acetol)': Km = 29,000 uM; kcat = 4.1 s^-1; printed kcat/Km = 0.14 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Hydroxyacetone (acetol)'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Hydroxyacetone


verification_status: verified

column_label: Table 1: Steady-state kinetic parameters for HAPMO. Substrate row '2-Acetylpyridine'; column 'K_m (uM)' = 1,200; column 'k_cat (s^-1)' = 7.8; column 'k_cat/K_m (10^3 s^-1 . M^-1)' = 6.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,200 uM; 1200 / 1000 = 1.2 mM; the exported value is 1.2 mM. kcat: printed Table 1 cell 7.8 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 7.8 s^(-1). kcat/Km: printed Table 1 cell 6.5 in the column unit 10^3 s^-1 . M^-1; 10^3 M^-1 is exactly mM^-1, so the cell is 6.5 s^-1 mM^-1 with no numeric rescaling; the exported value is 6.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row '2-Acetylpyridine': K_m = 1,200 uM; k_cat = 7.8 s^-1; k_cat/K_m = 6.5 in the printed column unit 10^3 s^-1 . M^-1.

status: verified


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'rac-Bicyclo[3.2.0]hept-2-en-6-one'; column 'Km (uM)' = 3,300 (300); column 'kcat (s^-1)' = 6.7 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 2.0; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 3,300 uM; 3300 / 1000 = 3.3 mM. kcat: printed Table 1 cell 6.7 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 6.7 s^(-1). kcat/Km: printed Table 1 cell 2.0 in the column headed 10^3 s^-1 M^-1, that is 2000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2000 / 1000 = 2 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'rac-Bicyclo[3.2.0]hept-2-en-6-one': Km = 3,300 uM; kcat = 6.7 s^-1; printed kcat/Km = 2.0 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'rac-Bicyclo[3.2.0]hept-2-en-6-one'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: butyrophenone

column_label: Table 1: Steady-state kinetic parameters for HAPMO. Substrate row 'Butyrophenone'; column 'K_m (uM)' = 2,000; column 'k_cat (s^-1)' = 1.2; column 'k_cat/K_m (10^3 s^-1 . M^-1)' = 0.60.

normalized_value_unit_evidence: Km: printed Table 1 cell 2,000 uM; 2000 / 1000 = 2.0 mM; the exported value is 2.0 mM. kcat: printed Table 1 cell 1.2 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the exported value is 1.2 s^(-1). kcat/Km: printed Table 1 cell 0.60 in the column unit 10^3 s^-1 . M^-1; 10^3 M^-1 is exactly mM^-1, so the cell is 0.6 s^-1 mM^-1 with no numeric rescaling; the exported value is 0.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate row 'Butyrophenone': K_m = 2,000 uM; k_cat = 1.2 s^-1; k_cat/K_m = 0.60 in the printed column unit 10^3 s^-1 . M^-1.

row_label: Table 1, substrate row 'Butyrophenone'

substrate: butyrophenone


substrate_name: Acetylcyclohexane

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Acetylcyclohexane'; column 'Km (uM)' = 4,800 (900); column 'kcat (s^-1)' = 3.9 (0.3); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.81; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 4,800 uM; 4800 / 1000 = 4.8 mM. kcat: printed Table 1 cell 3.9 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 3.9 s^(-1). kcat/Km: printed Table 1 cell 0.81 in the column headed 10^3 s^-1 M^-1, that is 810 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 810 / 1000 = 0.81 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Acetylcyclohexane': Km = 4,800 uM; kcat = 3.9 s^-1; printed kcat/Km = 0.81 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Acetylcyclohexane'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Acetylcyclohexane


sequence_source: UniProtKB Q93TJ5 direct REST/FASTA lookup


substrate_name: 2-Pyrrole carboxaldehyde

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '2-Pyrrole carboxaldehyde'; column 'Km (uM)' = 410 (30); column 'kcat (s^-1)' = 8.6 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 21; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 410 uM; 410 / 1000 = 0.41 mM. kcat: printed Table 1 cell 8.6 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 8.6 s^(-1). kcat/Km: printed Table 1 cell 21 in the column headed 10^3 s^-1 M^-1, that is 21000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '2-Pyrrole carboxaldehyde': Km = 410 uM; kcat = 8.6 s^-1; printed kcat/Km = 21 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2-Pyrrole carboxaldehyde'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: 2-Pyrrole carboxaldehyde


substrate_name: methylphenyl sulfide

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Methylphenyl sulfide'; column 'Km (uM)' = 1,400 (400); column 'kcat (s^-1)' = 4.7 (0.6); column 'kcat/Km (10^3 s^-1 . M^-1)' = 3.4; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,400 uM; 1400 / 1000 = 1.4 mM. kcat: printed Table 1 cell 4.7 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 4.7 s^(-1). kcat/Km: printed Table 1 cell 3.4 in the column headed 10^3 s^-1 M^-1, that is 3400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3400 / 1000 = 3.4 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Methylphenyl sulfide': Km = 1,400 uM; kcat = 4.7 s^-1; printed kcat/Km = 3.4 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Methylphenyl sulfide'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: methylphenyl sulfide


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '2-Acetylpyrrole'; column 'Km (uM)' = 330 (20); column 'kcat (s^-1)' = 9.4 (0.14); column 'kcat/Km (10^3 s^-1 . M^-1)' = 28; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 330 uM; 330 / 1000 = 0.33 mM. kcat: printed Table 1 cell 9.4 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 9.4 s^(-1). kcat/Km: printed Table 1 cell 28 in the column headed 10^3 s^-1 M^-1, that is 28000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 28000 / 1000 = 28 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '2-Acetylpyrrole': Km = 330 uM; kcat = 9.4 s^-1; printed kcat/Km = 28 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2-Acetylpyrrole'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


smiles: CC(=O)CC(C)=O

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '2,4-Pentanedione'; column 'Km (uM)' = 4,900 (900); column 'kcat (s^-1)' = 2.1 (0.5); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.43; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 4,900 uM; 4900 / 1000 = 4.9 mM. kcat: printed Table 1 cell 2.1 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.1 s^(-1). kcat/Km: printed Table 1 cell 0.43 in the column headed 10^3 s^-1 M^-1, that is 430 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 430 / 1000 = 0.43 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '2,4-Pentanedione': Km = 4,900 uM; kcat = 2.1 s^-1; printed kcat/Km = 0.43 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '2,4-Pentanedione'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: cyclohexane carboxaldehyde

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Cyclohexane carboxaldehyde'; column 'Km (uM)' = 3,000 (500); column 'kcat (s^-1)' = 5.0 (0.4); column 'kcat/Km (10^3 s^-1 . M^-1)' = 1.7; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 3,000 uM; 3000 / 1000 = 3 mM. kcat: printed Table 1 cell 5.0 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 5 s^(-1). kcat/Km: printed Table 1 cell 1.7 in the column headed 10^3 s^-1 M^-1, that is 1700 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1700 / 1000 = 1.7 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Cyclohexane carboxaldehyde': Km = 3,000 uM; kcat = 5.0 s^-1; printed kcat/Km = 1.7 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Cyclohexane carboxaldehyde'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: cyclohexane carboxaldehyde


column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row '4-Acetylpyridine'; column 'Km (uM)' = 1,900 (100); column 'kcat (s^-1)' = 0.5 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 0.3; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 1,900 uM; 1900 / 1000 = 1.9 mM. kcat: printed Table 1 cell 0.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 0.5 s^(-1). kcat/Km: printed Table 1 cell 0.3 in the column headed 10^3 s^-1 M^-1, that is 300 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 300 / 1000 = 0.3 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row '4-Acetylpyridine': Km = 1,900 uM; kcat = 0.5 s^-1; printed kcat/Km = 0.3 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row '4-Acetylpyridine'; the numbers in parentheses are the standard errors stated by Table 1 footnote c


substrate_name: Isobutyrophenone

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Isobutyrophenone'; column 'Km (uM)' = 540 (40); column 'kcat (s^-1)' = 2.5 (0.1); column 'kcat/Km (10^3 s^-1 . M^-1)' = 4.6; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 540 uM; 540 / 1000 = 0.54 mM. kcat: printed Table 1 cell 2.5 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 2.5 s^(-1). kcat/Km: printed Table 1 cell 4.6 in the column headed 10^3 s^-1 M^-1, that is 4600 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4600 / 1000 = 4.6 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Isobutyrophenone': Km = 540 uM; kcat = 2.5 s^-1; printed kcat/Km = 4.6 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Isobutyrophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Isobutyrophenone


substrate_name: Acetophenone

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Acetophenone'; column 'Km (uM)' = 2,300 (900); column 'kcat (s^-1)' = 13.2 (1.7); column 'kcat/Km (10^3 s^-1 . M^-1)' = 5.7; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 2,300 uM; 2300 / 1000 = 2.3 mM. kcat: printed Table 1 cell 13.2 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 13.2 s^(-1). kcat/Km: printed Table 1 cell 5.7 in the column headed 10^3 s^-1 M^-1, that is 5700 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 5700 / 1000 = 5.7 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Acetophenone': Km = 2,300 uM; kcat = 13.2 s^-1; printed kcat/Km = 5.7 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Acetophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Acetophenone


substrate_name: Propiophenone

column_label: Table 1 (Steady-state kinetic parameters for HAPMO), substrate row 'Propiophenone'; column 'Km (uM)' = 530 (100); column 'kcat (s^-1)' = 11.0 (0.2); column 'kcat/Km (10^3 s^-1 . M^-1)' = 21; the 'Structure' column of this row holds a drawn structure and no numeral.

normalized_value_unit_evidence: Km: printed Table 1 cell 530 uM; 530 / 1000 = 0.53 mM. kcat: printed Table 1 cell 11.0 s^-1; the cell is already in s^-1 and no unit conversion applies, so the paper value is 11 s^(-1). kcat/Km: printed Table 1 cell 21 in the column headed 10^3 s^-1 M^-1, that is 21000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 21000 / 1000 = 21 s^-1 mM^-1, and this record carries the paper's own printed catalytic-efficiency cell as the paper value for that metric.

raw_value_unit_evidence: Table 1, substrate row 'Propiophenone': Km = 530 uM; kcat = 11.0 s^-1; printed kcat/Km = 21 x 10^3 M^-1 s^-1.

row_label: Table 1, substrate row 'Propiophenone'; the numbers in parentheses are the standard errors stated by Table 1 footnote c

substrate: Propiophenone


substrate_name: 4'-Hydroxyacetophenone; H+; NADH

sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TJ5 direct REST/FASTA lookup and applied mutation signature K439F to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADP+

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439F

substrate: 4'-Hydroxyacetophenone; H+; NADH


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TJ5 direct REST/FASTA lookup and applied mutation signature R339A to reconstruct the assayed variant sequence.


substrate_name: H+; 4'-Hydroxyacetophenone; NADH

sequence_variant_note: Resolved canonical sequence from UniProtKB Q93TJ5 direct REST/FASTA lookup and applied mutation signature K439A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439A

substrate: H+; 4'-Hydroxyacetophenone; NADH


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439P variant reconstructed during review and applied mutation signature K439P to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: NADH; 4'-Hydroxyacetophenone; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific R339A variant reconstructed during review and applied mutation signature R339A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant R339A

substrate: NADH; 4'-Hydroxyacetophenone; H+


sequence_source: UniProtKB:Q93TJ5 FASTA/JSON direct accession check

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 UniProtKB:Q93TJ5 canonical sequence; row-specific K439A variant reconstructed during review and applied mutation signature K439A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439P variant reconstructed during review


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439F variant reconstructed during review and applied mutation signature K439F to reconstruct the assayed variant sequence.


substrate_name: 4'-Hydroxyacetophenone; NADH; H+

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439P

substrate: 4'-Hydroxyacetophenone; NADH; H+


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific K439N variant reconstructed during review and applied mutation signature K439N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439A variant reconstructed during review


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439N variant reconstructed during review

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant K439N


substrate_name: H+; 4'-Hydroxyacetophenone; O2; NADPH

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q93TJ5 canonical sequence; row-specific R440A variant reconstructed during review and applied mutation signature R440A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADPH

proof_lines: SABIO-RK modifier species: 4-hydroxyacetophenone monooxygenase(Enzyme) mutant R440A

substrate: H+; 4'-Hydroxyacetophenone; O2; NADPH


sequence_source: UniProtKB:Q93TJ5 canonical sequence; row-specific K439F variant reconstructed during review


organism: Pseudomonas putida

sequence_source: UniProtKB:B7T912 FASTA/JSON direct accession check

assay_conditions_summary: pH 8; 303.15 K; buffer air-saturated; cofactor NADPH

column_label: TABLE 2. Kinetic parameters of HAPMO from P. putida JD1 (footnote a: All values were measured in Tris-HCl buffer (pH 8.0, 50 mM) at 30°C using a fixed NADPH concentration of 312 μM.) Block 'Aromatic compounds'; substrate row '2-Phenylpropionaldehyde'; column 'Km (uM)' = 21,241; column 'kcat (s^-1)' = 8.7; column 'kcat/Km (10^3 s^-1 M^-1)' = 0.4.

normalized_value_unit_evidence: Km: printed Table 2 cell 21,241 uM; 21241 / 1000 = 21.241 mM; the exported value is 21.24 mM. kcat: printed Table 2 cell 8.7 s^-1; already in s^-1, no conversion; the exported value is 8.7 s^(-1). kcat/Km: printed Table 2 cell 0.4 in the column headed 10^3 s^-1 M^-1; 1 unit of 10^3 M^-1 s^-1 is 1 mM^-1 s^-1, so the printed cell is 0.4 s^(-1)*mM^(-1); the exported value is 0.4096045197740113 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, block 'Aromatic compounds', substrate row '2-Phenylpropionaldehyde': Km = 21,241 uM; kcat = 8.7 s^-1; printed kcat/Km = 0.4 (column unit 10^3 s^-1 M^-1).


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '4-Aminoacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 5.6; column 'kcat (s-1)' = 8.2; column 'kcat/Km (10^3 s-1 . M-1)' = 1,450; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 5.6 uM for the substrate row '4-Aminoacetophenone'; 5.6 / 1000 = 0.0056 mM; the exported value is 0.0056 mM. kcat: printed Table 2 cell 8.2 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 8.2 s^(-1). kcat/Km: printed Table 2 cell 1,450 in the column head unit 10^3 s^-1 M^-1, i.e. 1,450 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1,450 x 10^3 x 0.001 = 1450.0 s^-1 mM^-1; the exported value is 1464.2857142857142 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '4-Aminoacetophenone': Km = 5.6 uM; kcat = 8.2 s^-1; printed kcat/Km = 1,450 in the column head unit 10^3 s^-1 M^-1.

table_label: Table 2: Kinetic parameters of HAPMO from P. putida JD1 (Applied and Environmental Microbiology 2009, 75(10):3106-3114)


column_label: Table 2 (Kinetic parameters of HAPMO from P. putida JD1), substrate row '3-Aminoacetophenone'; the printed column heads are 'Substrate', 'Structure', 'Km (uM)', 'kcat (s-1)' and 'kcat/Km (10^3 s-1 . M-1)'; column 'Km (uM)' = 287; column 'kcat (s-1)' = 1.0; column 'kcat/Km (10^3 s-1 . M-1)' = 3.3; the Structure column holds a drawn chemical structure and no number.

normalized_value_unit_evidence: Km: printed Table 2 cell 287 uM for the substrate row '3-Aminoacetophenone'; 287 / 1000 = 0.287 mM; the exported value is 0.287 mM. kcat: printed Table 2 cell 1.0 s^-1 for the same row; already in s^-1, no unit conversion applies; the exported value is 1.0 s^(-1). kcat/Km: printed Table 2 cell 3.3 in the column head unit 10^3 s^-1 M^-1, i.e. 3.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.3 x 10^3 x 0.001 = 3.3 s^-1 mM^-1; the exported value is 3.4843205574912894 s^(-1)*mM^(-1), so this metric is corrected to the printed cell.

raw_value_unit_evidence: Table 2, substrate row '3-Aminoacetophenone': Km = 287 uM; kcat = 1.0 s^-1; printed kcat/Km = 3.3 in the column head unit 10^3 s^-1 M^-1.


substrate_name: methyl-4-tolyl sulfide

sequence_source: UniProtKB REST FASTA accession B7T912

column_label: TABLE 2. Kinetic parameters of HAPMO from P. putida JD1 (footnote a: All values were measured in Tris-HCl buffer (pH 8.0, 50 mM) at 30°C using a fixed NADPH concentration of 312 μM.) Block 'Aromatic compounds'; substrate row 'Methyl-4-tolyl sulfide'; column 'Km (uM)' = 18,848; column 'kcat (s^-1)' = 20; column 'kcat/Km (10^3 s^-1 M^-1)' = 1.1.

normalized_value_unit_evidence: Km: printed Table 2 cell 18,848 uM; 18848 / 1000 = 18.848 mM; the exported value is 18.85 mM. kcat: printed Table 2 cell 20 s^-1; already in s^-1, no conversion; the exported value is 20.0 s^(-1). kcat/Km: printed Table 2 cell 1.1 in the column headed 10^3 s^-1 M^-1; 1 unit of 10^3 M^-1 s^-1 is 1 mM^-1 s^-1, so the printed cell is 1.1 s^(-1)*mM^(-1); the exported value is 1.0610079575596816 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, block 'Aromatic compounds', substrate row 'Methyl-4-tolyl sulfide': Km = 18,848 uM; kcat = 20 s^-1; printed kcat/Km = 1.1 (column unit 10^3 s^-1 M^-1).

substrate: methyl-4-tolyl sulfide


substrate_name: trifluoroacetophenone

substrate: trifluoroacetophenone


enzyme_display_name: dopamine beta-monooxygenase

organism: Bos taurus

sequence_source: UniProtKB REST FASTA accession P15101

enzyme: dopamine beta-monooxygenase


organism: Gallus gallus

substrate_name: Dopamine; O2; L-Ascorbate

sequence_source: UniProtKB REST FASTA accession Q9I9A1

substrate: Dopamine; O2; L-Ascorbate


enzyme_display_name: histone deacetylase

organism: Homo sapiens

substrate_name: Fluor de Lys

sequence_source: UniProtKB REST FASTA accession Q9UBN7

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q9UBN7 and applied mutation signature H216A to reconstruct the assayed variant sequence.

enzyme: histone deacetylase

substrate: Fluor de Lys


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q9UBN7 and applied mutation signature H611A to reconstruct the assayed variant sequence.


substrate_name: RHK(acetyl)K(acetyl)-fluorophore

sequence_source: UniProtKB REST FASTA accession Q9BY41

proof_lines:
presence of Zn(II), 25°C. pH 8.0
pH 8, 30Â°C
presence of Co(II), 25°C. pH 8.0

substrate: RHK(acetyl)K(acetyl)-fluorophore


substrate_name: Fluor de Lys HDAC substrate

sequence_source: UniProtKB REST FASTA accession Q8WUI4

substrate: Fluor de Lys HDAC substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q8WUI4 and applied mutation signature H843F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q8WUI4 and applied mutation signature H843A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q8WUI4 and applied mutation signature H843Y to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST FASTA accession Q13547


sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q13547 and applied mutation signature F150A to reconstruct the assayed variant sequence.


substrate_name: Fluor de Lys HDAC8 substrate

sequence_variant_note: Resolved canonical sequence from UniProtKB REST FASTA accession Q9BY41 and applied mutation signature D101L to reconstruct the assayed variant sequence.

substrate: Fluor de Lys HDAC8 substrate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed D101A variant after residue check and applied mutation signature D101A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed D101E variant after residue check and applied mutation signature D101E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98)

proof_lines:
Zn2+-wild type
Co2+-wild type


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed D101N variant after residue check and applied mutation signature D101N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9BY41 (HDAC8_HUMAN, Histone deacetylase 8, Homo sapiens, EC 3.5.1.98); reconstructed H143A variant after residue check and applied mutation signature H143A to reconstruct the assayed variant sequence.


substrate_name: GK(Ac)F

sequence_source: UniProtKB reviewed Q9UBN7 (HDAC6_HUMAN, Protein deacetylase HDAC6, Homo sapiens, UniProt EC 3.5.1.-)

substrate: GK(Ac)F


substrate_name: GGK(Ac)FF

proof_lines:
pH 7.4, 37°C, recombinant enzyme
catalytic domain II, pH 7.2, 23°C

substrate: GGK(Ac)FF


substrate_name: RYSSRRK(Ac)ARPYML

substrate: RYSSRRK(Ac)ARPYML


substrate_name: RGGK(Ac)FFR

substrate: RGGK(Ac)FFR


substrate_name: TYSRGGK(Ac)FFRRFP

substrate: TYSRGGK(Ac)FFRRFP


substrate_name: SQSEEEK(Ac)FFRRFP

substrate: SQSEEEK(Ac)FFRRFP


substrate_name: SRGGK(Ac)FFRR

substrate: SRGGK(Ac)FFRR


substrate_name: YSRGGK(Ac)FFRRF

substrate: YSRGGK(Ac)FFRRF


substrate_name: TYSRGGK(Ac)KSEESE

substrate: TYSRGGK(Ac)KSEESE


organism: Mus musculus

substrate_name: H2O; Acetylhistone

sequence_source: UniProtKB reviewed O09106 (HDAC1_MOUSE, Histone deacetylase 1, Mus musculus, EC 3.5.1.98)

substrate: H2O; Acetylhistone


enzyme_display_name: cytidine deaminase

organism: Mycobacterium tuberculosis

substrate_name: cytidine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPH3 and applied mutation signature E47D to reconstruct the assayed variant sequence.

enzyme: cytidine deaminase

substrate: cytidine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WPH3 and applied mutation signature E47Q to reconstruct the assayed variant sequence.


organism: Trypanosoma brucei brucei

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

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


organism: Caulobacter vibrioides

substrate_name: L-threonine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95C to reconstruct the assayed variant sequence.

substrate: L-threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95M to reconstruct the assayed variant sequence.


substrate_name: L-Threonine

substrate: L-Threonine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9A3V8 and applied mutation signature D95N/E96S to reconstruct the assayed variant sequence.


substrate_name: L-allo-Threonine

substrate: L-allo-Threonine