column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row dopamine; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row dopamine: Km 7.3 uM; kcat 3.6 1/min; kcat/Km 0.5 1/uM*min.


enzyme_display_name: norbelladine O-methyltransferase

organism: Narcissus aff. pseudonarcissus MK-2014

substrate_name: N-methylnorbelladine

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row N-methylnorbelladine; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row N-methylnorbelladine: Km 1.9 uM; kcat 2.6 1/min; kcat/Km 1.3 1/uM*min.

row_label: N-methylnorbelladine

data_origin: experimental

enzyme: norbelladine O-methyltransferase

substrate: N-methylnorbelladine

status: corrected

source: oed


substrate_name: norbelladine

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row norbelladine; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row norbelladine: Km 1.6 uM; kcat 1.3 1/min; kcat/Km 0.8 1/uM*min.

row_label: norbelladine

substrate: norbelladine


substrate_name: S-adenosyl-L-methionine

column_label: Table 1 'Table 1: Kinetic parameters of Narcissus norbelladine 4'-O-methyltransferase'; row AdoMet; kcat, kcat_over_km, km cells.

raw_value_unit_evidence: Table 1 row AdoMet: Km 28.5 uM; kcat 4.5 1/min; kcat/Km 0.16 1/uM*min.

row_label: AdoMet

substrate: S-adenosyl-L-methionine


enzyme_display_name: methanethiol S-methyltransferase

organism: Pseudomonas deceptionensis

source_db: brenda

verification_status: unverified

kcat_over_km_origin: calculated

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

smiles: S

assay_conditions_summary: pH 8

enzyme: methanethiol S-methyltransferase

status: unverified

source: brenda


substrate_name: methanethiol

smiles: CS

column_label: Table 1 columns Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); row MeSH.

row_label: PdMddA / MeSH (methanethiol)

table_label: Table 1: Kinetic parameters of PdMddA with different substrates

substrate: methanethiol


substrate_name: dithiothreitol

smiles: C(C(C(CS)O)O)S

column_label: Table 1 columns Km (mM), kcat (s^-1), kcat/Km (M^-1 s^-1); row DTT.

row_label: PdMddA / DTT

substrate: dithiothreitol


enzyme_display_name: xanthohumol 4-O-methyltransferase

organism: Humulus lupulus

substrate_name: resveratrol

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

sequence_source: multiple

column_label: Table 3 row OMT2 Resveratrol under Km Substrate column: 19 +/- 1 uM.

row_label: OMT2 / Resveratrol

table_label: Table 3

source_databases_merged: brenda uniprot

enzyme: xanthohumol 4-O-methyltransferase

substrate: resveratrol

status: verified


substrate_name: desmethylxanthohumol

column_label: Table 3 row OMT2 Desmethylxanthohumol under Km Substrate column: 23 +/- 6 uM.

row_label: OMT2 / Desmethylxanthohumol

substrate: desmethylxanthohumol


substrate_name: xanthohumol

column_label: Table 3 row OMT2 Xanthohumol under Km Substrate column: 31 +/- 3 uM.

row_label: OMT2 / Xanthohumol

substrate: xanthohumol


column_label: Table 3 row OMT2 SAM under Km Substrate column: 34 +/- 3 uM; footnote c says determined with xanthohumol as cosubstrate.

raw_value_unit_evidence: Km 34 +/- 3 uM; footnote c determined with xanthohumol as cosubstrate.

row_label: OMT2 / SAM


substrate_name: chalconaringenin

column_label: Table 3 row OMT2 Chalconaringenin under Km Substrate column: 237 +/- 19 uM.

row_label: OMT2 / Chalconaringenin

substrate: chalconaringenin


enzyme_display_name: reticuline N-methyltransferase

organism: Papaver somniferum

substrate_name: (R)-reticuline

column_label: Table 2; Table 2 row (R)-Reticuline; columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row (R)-Reticuline reports Km 85 +/- 11 uM, Vmax 74.8 +/- 3.6 pmol min^-1 ug^-1 protein, kcat 0.053 s^-1, and kcat/Km 618 s^-1 M^-1.

row_label: Table 2 row (R)-Reticuline

table_label: PMID 27634038, Table 2: Michaelis-Menten enzyme kinetic parameters for RNMT with respect to (S)-reticuline, (R)-reticuline, and AdoMet

enzyme: reticuline N-methyltransferase

substrate: (R)-reticuline


column_label: Table 2; Table 2 row AdoMet; columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row AdoMet reports Km 168 +/- 8 uM, Vmax 66.5 +/- 1.4 pmol min^-1 ug^-1 protein, kcat 0.047 s^-1, and kcat/Km 280 s^-1 M^-1.

row_label: Table 2 row AdoMet


substrate_name: (S)-reticuline

column_label: Table 2; Table 2 row (S)-Reticuline; columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: Table 2 row (S)-Reticuline reports Km 42 +/- 3 uM, Vmax 39.6 +/- 0.9 pmol min^-1 ug^-1 protein, kcat 0.028 s^-1, and kcat/Km 655 s^-1 M^-1.

row_label: Table 2 row (S)-Reticuline

substrate: (S)-reticuline


enzyme_display_name: 3-aminomethylindole N-methyltransferase

organism: Hordeum vulgare subsp. vulgare

enzyme: 3-aminomethylindole N-methyltransferase


enzyme_display_name: UniProt Q9NR48

organism: Homo sapiens

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q9NR48

source: skid


enzyme_display_name: Botryococcene C-methyltransferase

organism: Botryococcus braunii

substrate_name: botryococcene

source_db: uniprot

enzyme: Botryococcene C-methyltransferase

substrate: botryococcene

source: uniprot


enzyme_display_name: Flavone 3'-O-methyltransferase 1

organism: Arabidopsis thaliana

substrate_name: N-acetylserotonin (at pH 7.8 and 37 degrees Celsius)

enzyme: Flavone 3'-O-methyltransferase 1


enzyme_display_name: juvenile hormone-III synthase

organism: Diaphorina citri

substrate_name: farnesoic acid

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

enzyme: juvenile hormone-III synthase

substrate: farnesoic acid


substrate_name: homofarnesoic acid

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

substrate: homofarnesoic acid


enzyme_display_name: Bergaptol O-methyltransferase

organism: Glehnia littoralis

substrate_name: bergaptol

enzyme: Bergaptol O-methyltransferase

substrate: bergaptol


substrate_name: quercetin

substrate: quercetin


enzyme_display_name: UniProt P51580

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

source_databases_merged: skid uniprot

enzyme: UniProt P51580


organism: Lycoris radiata

column_label: PDF pages 8-9, Table 1, 3,4-Dihydroxybenzaldehyde substrate / Vanillin product column: Km, kcat, kcat/Km

row_label: 3,4-Dihydroxybenzaldehyde -> Vanillin

table_label: PMID 31494163 Table 1. Kinetic parameters for LrOMT-catalyzed O-methylation


substrate_name: caffeic acid

column_label: PDF pages 8-9, Table 1, Caffeic acid substrate / Ferulic acid product column: Km, kcat, kcat/Km

row_label: Caffeic acid -> Ferulic acid

substrate: caffeic acid


substrate_name: norbelladine


substrate_name: serotonin

substrate: serotonin


enzyme_display_name: Indolethylamine N-methyltransferase

substrate_name: tryptamine

column_label: Abstract reports the recombinant enzyme catalyzed methylation of tryptamine with an apparent K(m) value of 2.9 mM.

raw_value_unit_evidence: Km raw_value=2.9 mM raw_unit=mM

row_label: Human recombinant indolethylamine N-methyltransferase / tryptamine

table_label: PubMed XML abstract PMID 10552930

enzyme: Indolethylamine N-methyltransferase

substrate: tryptamine


enzyme_display_name: demethylphylloquinol methyltransferase

substrate_name: menadione

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines:
NDC1
demethylphylloquinone
vitamin K1

enzyme: demethylphylloquinol methyltransferase

substrate: menadione


enzyme_display_name: tabersonine 16-O-methyltransferase

organism: Catharanthus roseus

substrate_name: S-adenosyl-L-methionine

enzyme: tabersonine 16-O-methyltransferase

substrate: S-adenosyl-L-methionine


enzyme_display_name: nicotinate methyltransferase

organism: Glycine max

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

enzyme: nicotinate methyltransferase


substrate_name: nicotinate

substrate: nicotinate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


proof_lines:
at pH 7.5 and 28°C
pH 7.0, 23°C


enzyme_display_name: sialate 8-O-methyltransferase

organism: Asterias rubens

proof_lines: pH 8.0, 25°C, with N-acetylneuraminyl alpha2,3-lactose

enzyme: sialate 8-O-methyltransferase


substrate_name: N-acetylneuraminyl alpha2,3-lactose

substrate: N-acetylneuraminyl alpha2,3-lactose


substrate_name: N-acetylneuraminic acid

substrate: N-acetylneuraminic acid


enzyme_display_name: resveratrol 4'-O-methyltransferase

organism: Acorus calamus

substrate_name: resveratrol

enzyme: resveratrol 4'-O-methyltransferase

substrate: resveratrol


substrate_name: isorhapontigenin

substrate: isorhapontigenin


organism: Methanocaldococcus jannaschii

proof_lines: pH and temperature not specified in the publication


organism: Methanococcus maripaludis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y51F to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant enzyme Y51F, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T6V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T6V, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S233A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S233A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S175A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S175A, pH and temperature not specified in the publication


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


enzyme_display_name: thymidylate synthase (FAD)

organism: Helicobacter pylori

substrate_name: dUMP

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

enzyme: thymidylate synthase (FAD)

substrate: dUMP


enzyme_display_name: 24-methylenesterol C-methyltransferase

enzyme: 24-methylenesterol C-methyltransferase


substrate_name: Zymosterol

substrate: Zymosterol


substrate_name: Cycloartenol

substrate: Cycloartenol


substrate_name: obtusifoliol

substrate: obtusifoliol


substrate_name: lanosterol

substrate: lanosterol


enzyme_display_name: glycine hydroxymethyltransferase

organism: Psychromonas ingrahamii

substrate_name: L-serine

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

proof_lines:
pH 7.2, 20°C
Raw SKiD Env: Temp=20°C, pH=7.2

source_databases_merged: brenda skid

enzyme: glycine hydroxymethyltransferase

substrate: L-serine


enzyme_display_name: UniProt P07511

organism: Oryctolagus cuniculus

substrate_name: tetrahydrofolate

enzyme: UniProt P07511

substrate: tetrahydrofolate


enzyme_display_name: UniProt Q7SIB6

organism: Geobacillus stearothermophilus

enzyme: UniProt Q7SIB6


enzyme_display_name: caffeate O-methyltransferase

enzyme: caffeate O-methyltransferase


substrate_name: Protocatechuic aldehyde

substrate: Protocatechuic aldehyde


substrate_name: 5-hydroxyferulic acid

substrate: 5-hydroxyferulic acid


substrate_name: 3,4,5-trihydroxycinnamic acid

substrate: 3,4,5-trihydroxycinnamic acid


substrate_name: caffeic acid

substrate: caffeic acid


enzyme_display_name: trans-aconitate 2-methyltransferase

organism: Escherichia coli

substrate_name: trans-aconitate

enzyme: trans-aconitate 2-methyltransferase

substrate: trans-aconitate


substrate_name: DL-isocitrate

substrate: DL-isocitrate


substrate_name: citrate

substrate: citrate


organism: Neomoorella thermoacetica

substrate_name: [methyl-Co(III) corrinoid Fe-S protein]

proof_lines: kcat below 0.02 s(-1), in 1 mM Tris-HCl (pH 7.6), at 25°C

substrate: [methyl-Co(III) corrinoid Fe-S protein]


substrate_name: hydroxocobalamin

substrate: hydroxocobalamin


proof_lines: using hydroxocobalamin as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C

proof_lines: using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C


substrate_name: methylcobalamin

substrate: methylcobalamin


proof_lines: Km above 0.2 mM, using [Co(I) corrinoid Fe-S protein] as cosubstrate, in 1 mM Tris-HCl (pH 7.6), at 25°C


organism: Mycobacterium tuberculosis

substrate_name: dUMP

substrate: dUMP


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: trans-aconitate 3-methyltransferase

organism: Saccharomyces cerevisiae

enzyme: trans-aconitate 3-methyltransferase


substrate_name: isopropylmaleate

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

substrate: isopropylmaleate


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


enzyme_display_name: norbelladine O-methyltransferase

organism: Narcissus aff. pseudonarcissus MK-2014

substrate_name: norbelladine

enzyme: norbelladine O-methyltransferase

substrate: norbelladine


substrate_name: N-methylnorbelladine

substrate: N-methylnorbelladine


substrate_name: dopamine

substrate: dopamine


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


substrate_name: [Co(I) corrinoid Fe-S protein]

proof_lines: mutant enzyme N199A, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C

substrate: [Co(I) corrinoid Fe-S protein]


proof_lines: wild type enzyme, in 0.1 M potassium succinate, pH 5.0, 60 mM NaCl, at 25°C


organism: Sorghum bicolor


enzyme_display_name: UniProt P31939

organism: Homo sapiens

substrate_name: (6R,6S)-10-formyltetrahydrofolic acid

enzyme: UniProt P31939

substrate: (6R,6S)-10-formyltetrahydrofolic acid


enzyme_display_name: 2-methylserine hydroxymethyltransferase

organism: Paracoccus sp

substrate_name: alpha-methyl-L-serine

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

enzyme: 2-methylserine hydroxymethyltransferase

substrate: alpha-methyl-L-serine


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


substrate_name: uracil1498 in 16S rRNA

proof_lines: pH 7.0, 37°C, the Km-value for 16S rRNA is measured as a Km for the physiological substrate, 30S ribosomal subunit

substrate: uracil1498 in 16S rRNA


organism: Bacillus cereus

proof_lines: pH 7, 37°C, cosubstrate malonyl-[acyl-carrier protein]


substrate_name: malonyl-[acyl-carrier protein]

substrate: malonyl-[acyl-carrier protein]


enzyme_display_name: aspartate carbamoyltransferase

substrate_name: L-asparagine

enzyme: aspartate carbamoyltransferase

substrate: L-asparagine


assay_conditions_summary: pH 8; 295.15 K; cofactor NADPH

proof_lines: in 50 mM Tris-HCl pH 8.0, 10 mM MgCl2, 2 mM NADPH, 0.5 mM FAD, at 22°C


enzyme_display_name: thiopurine S-methyltransferase

organism: Mus musculus

enzyme: thiopurine S-methyltransferase


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

proof_lines:
at pH 7.5 and 25°C
apparent value, at pH 7.5 and 30°C

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


organism: Nicotiana tabacum

substrate_name: 24-methylene lophenol

substrate: 24-methylene lophenol


substrate_name: Cycloartenol

substrate: Cycloartenol


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Cucurbita maxima

substrate_name: gibberellin a15

enzyme: gibberellin 3beta-dioxygenase

substrate: gibberellin a15


organism: Equus caballus

substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: UniProt Q837U7

organism: Enterococcus faecalis

substrate_name: L-ornithine

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

enzyme: UniProt Q837U7

substrate: L-ornithine


enzyme_display_name: UniProt P84010

organism: Ovis aries

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9
Raw SKiD Env: Temp=37°C, pH=8.2

enzyme: UniProt P84010


enzyme_display_name: UniProt P00480

substrate_name: Carbamoyl phosphate

enzyme: UniProt P00480

substrate: Carbamoyl phosphate


enzyme_display_name: formate dehydrogenase-N

substrate_name: formate

enzyme: formate dehydrogenase-N

substrate: formate


substrate_name: uracil1939 in 23S rRNA

proof_lines: the enzymatic activity of RumA is measured for a 12-mer 5' RNA segment (1932?1943) lacking the 3' hairpin

proof_lines: pH 7.5, 37°C, uracil1939 in 40-nucleotide 23 S rRNA fragment (nucleotide 1930?1969)

proof_lines: the enzymatic activity of RumA is measured for a 37-mer RNA (1932?1968) segment lacking the 3' hairpin

substrate: uracil1939 in 23S rRNA


substrate_name: homocysteine

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

substrate: homocysteine


substrate_name: S-adenosyl-L-methionine

substrate: S-adenosyl-L-methionine


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: CDP

proof_lines: activity of subunit B1 assayed in the presence of an excess of subunit B2

proof_lines: activity of subunit B2 assayed in the presence of an excess of subunit B1

enzyme: ribonucleoside-diphosphate reductase

substrate: CDP


enzyme_display_name: DNA oxidative demethylase

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

enzyme: DNA oxidative demethylase


enzyme_display_name: taurine dioxygenase

substrate_name: palmitoyl[zDHHC6 protein]

proof_lines:
commercially available substrate
deuterated substrate

enzyme: taurine dioxygenase

substrate: palmitoyl[zDHHC6 protein]


enzyme_display_name: UniProt P34736

organism: Scheffersomyces stipitis

substrate_name: D-xylulose 5-phosphate

smiles: C(C(C(C(=O)CO)O)O)OP(=O)(O)O

enzyme: UniProt P34736

substrate: D-xylulose 5-phosphate


substrate_name: sedoheptulose 7-phosphate

smiles: C(C(C(C(C(C(=O)CO)O)O)O)O)OP(=O)(O)O

substrate: sedoheptulose 7-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


enzyme_display_name: UniProt Q8MPM3

organism: Leishmania mexicana

smiles: C(C(C(C(C=O)O)O)O)OP(=O)(O)O

enzyme: UniProt Q8MPM3


enzyme_display_name: UniProt A0A0I9QGZ2

organism: Geobacillus stearothermophilus

substrate_name: L-glyceraldehyde

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

enzyme: UniProt A0A0I9QGZ2

substrate: L-glyceraldehyde


substrate_name: L-lactaldehyde

smiles: CC(C=O)O

substrate: L-lactaldehyde


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=50°C, pH=7.5


substrate_name: L-erythrulose

smiles: C(C(C(=O)CO)O)O

proof_lines:
Raw SKiD Env: Temp=50°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: L-erythrulose


enzyme_display_name: UniProt P23254

enzyme: UniProt P23254


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyceraldehyde 3-phosphate

smiles: C(C(C=O)O)OP(=O)(O)O

substrate: glyceraldehyde 3-phosphate


enzyme_display_name: UniProt P29401

substrate_name: D-ribose 5-phosphate

enzyme: UniProt P29401

substrate: D-ribose 5-phosphate


enzyme_display_name: UniProt P9WG25

enzyme: UniProt P9WG25


substrate_name: fructose 6-phosphate

smiles: C(C(C(C(C(=O)CO)O)O)O)OP(=O)(O)O

substrate: fructose 6-phosphate


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: Transketolase

substrate_name: D-ribose 5-phosphate (at 25 degrees Celsius)

enzyme: Transketolase


enzyme_display_name: transaldolase

organism: Dictyostelium discoideum

enzyme: transaldolase


substrate_name: D-erythrose 4-phosphate

smiles: C(C(C(C=O)O)O)OP(=O)(O)O

substrate: D-erythrose 4-phosphate


enzyme_display_name: UniProt Q9HKI3

organism: Thermoplasma acidophilum

enzyme: UniProt Q9HKI3


organism: Escherichia coli

substrate_name: nucleoside32 in EctRNAGln1(UUG)

proof_lines: pH 9.0, 37°C, recombinant wild-type enzyme

substrate: nucleoside32 in EctRNAGln1(UUG)


substrate_name: glutaredoxin

substrate: glutaredoxin


enzyme_display_name: alkanesulfonate monooxygenase

substrate_name: octanesulfonate

enzyme: alkanesulfonate monooxygenase

substrate: octanesulfonate


enzyme_display_name: superoxide dismutase

substrate_name: Unknown

enzyme: superoxide dismutase

substrate: Unknown


enzyme_display_name: mercury(II) reductase

enzyme: mercury(II) reductase


organism: Herpes simplex virus

proof_lines:
derived from slope
derived from intercept


smiles: O=O


substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: L-arginine

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

proof_lines: in presence of tetrahydrobiopterin and L-arginine

enzyme: nitric-oxide synthase (NADPH)

substrate: L-arginine


enzyme_display_name: phytanoyl-CoA dioxygenase

assay_conditions_summary: cofactor CoA

enzyme: phytanoyl-CoA dioxygenase


enzyme_display_name: cuproxidase

substrate_name: Cu+

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication

enzyme: cuproxidase

substrate: Cu+


enzyme_display_name: indoleamine 2,3-dioxygenase

substrate_name: tryptamine

enzyme: indoleamine 2,3-dioxygenase

substrate: tryptamine


enzyme_display_name: transketolase

organism: Saccharomyces cerevisiae

enzyme: transketolase


substrate_name: D-xylulose 5-phosphate

substrate: D-xylulose 5-phosphate


enzyme_display_name: ferroxidase

organism: Homo sapiens

substrate_name: Ferrous ammonium sulfate

enzyme: ferroxidase

substrate: Ferrous ammonium sulfate


enzyme_display_name: sterol 14alpha-demethylase

substrate_name: lanosterol

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


organism: Gallus sp.

substrate_name: N,N'-dimethyl-p-phenylenediamine

substrate: N,N'-dimethyl-p-phenylenediamine


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: arachidonic acid

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

proof_lines: cytosolic hp-12LOX, pH 7.4, recombinant wild-type enzyme

proof_lines: membrane hp-12LOX, pH 7.4, recombinant wild-type enzyme

enzyme: arachidonate 12-lipoxygenase

substrate: arachidonic acid


enzyme_display_name: arachidonate 15-lipoxygenase

substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

proof_lines:
recombinant enzyme
pH 7.5, 20°C
pH 7.5, 30°C

enzyme: arachidonate 15-lipoxygenase

substrate: linoleic acid


enzyme_display_name: UniProt P77488

enzyme: UniProt P77488


substrate_name: pyruvate

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=8

substrate: pyruvate


substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


enzyme_display_name: UniProt P23970

organism: Bacillus subtilis

enzyme: UniProt P23970


enzyme_display_name: mRNA N6-methyladenine demethylase

substrate_name: N3-methylthymine in single-stranded DNA

proof_lines: pH and temperature not specified in the publication

enzyme: mRNA N6-methyladenine demethylase

substrate: N3-methylthymine in single-stranded DNA


enzyme_display_name: ribonucleoside-diphosphate reductase

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

enzyme: ribonucleoside-diphosphate reductase


substrate_name: linoleate

smiles: CCCCCC=CCC=CCCCCCCCC(=O)[O-]

proof_lines: fully deuterated, in the presence of 13-(S)-hydroxyoctadecadienoic acid

substrate: linoleate


enzyme_display_name: thymidylate synthase (FAD)

organism: Helicobacter pylori

enzyme: thymidylate synthase (FAD)


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: o-Dianisidine

substrate: o-Dianisidine


substrate_name: Unknown

proof_lines: enzyme hVKOR, microsomal hVKOR not subjected to detergent solubilization, endoplasmic reticulum-enriched microsomes, in presence of glutahione with substrate KO, pH and temperature not specified in the publication

substrate: Unknown


enzyme_display_name: UniProt Q5FAK7

organism: Pseudomonas aeruginosa

substrate_name: acetyl-CoA

enzyme: UniProt Q5FAK7

substrate: acetyl-CoA


enzyme_display_name: UniProt Q8N159

enzyme: UniProt Q8N159


substrate_name: L-glutamate

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

substrate: L-glutamate


enzyme_display_name: Arginine biosynthesis bifunctional protein ArgJ, chloroplastic

organism: Citrullus lanatus

substrate_name: N(2)-acetyl-L-ornithine (at pH 7.0)

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

substrate: N(2)-acetyl-L-ornithine (at pH 7.0)


substrate_name: L-glutamate (at pH 7.0)

enzyme: Arginine biosynthesis bifunctional protein ArgJ, chloroplastic

substrate: L-glutamate (at pH 7.0)


enzyme_display_name: UniProt Q17427

organism: Caenorhabditis elegans

substrate_name: D-glucosamine 6-phosphate

enzyme: UniProt Q17427

substrate: D-glucosamine 6-phosphate


enzyme_display_name: UniProt Q5CPU3

organism: Cryptosporidium parvum

enzyme: UniProt Q5CPU3


enzyme_display_name: UniProt Q96EK6

substrate_name: propionyl-CoA

enzyme: UniProt Q96EK6

substrate: propionyl-CoA


enzyme_display_name: UniProt O86309

organism: Mycolicibacterium smegmatis

enzyme: UniProt O86309


substrate_name: hydralazine

substrate: hydralazine


enzyme_display_name: UniProt P18440

enzyme: UniProt P18440


substrate_name: 5-aminosalicylic acid

substrate: 5-aminosalicylic acid


enzyme_display_name: UniProt Q5YYQ3

organism: Nocardia farcinica

substrate_name: isoniazid

enzyme: UniProt Q5YYQ3

substrate: isoniazid


substrate_name: hypoxia-inducible factor2alpha C-terminal oxygen-dependent degradation domain-L-proline


enzyme_display_name: ferroxidase

substrate_name: N,N'-dimethyl-p-phenylenediamine

enzyme: ferroxidase

substrate: N,N'-dimethyl-p-phenylenediamine


enzyme_display_name: nitric-oxide synthase (NADPH)

proof_lines: irreversible inactivation of endothelial isoform after preincubation

proof_lines: at lower concentration than the Ki value agmatine leads to time-, concentration-, NADPH- and calmodulin-dependent inhibition of the neuronal enzyme in presence of calmodulin

enzyme: nitric-oxide synthase (NADPH)


assay_conditions_summary: pH 7; 303.15 K; buffer pH 7

proof_lines:
pH 7.0, 30°C, 0.2 M phosphate buffer
pH 7.0, 30°C, 0.2 M acetate buffer
pH 5.2, 30°C, 0.0133 M phosphate buffer


enzyme_display_name: phytanoyl-CoA dioxygenase

enzyme: phytanoyl-CoA dioxygenase


enzyme_display_name: FAD-dependent urate hydroxylase

organism: Klebsiella pneumoniae

substrate_name: Urate

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
pH 8.0, 1.5 mM NADH as cosubstrate
pH 8.0, cosubstrate 1.5 mM NADH

enzyme: FAD-dependent urate hydroxylase

substrate: Urate


smiles: CSCCC(=O)C(=CO)O


enzyme_display_name: trimethylamine monooxygenase

substrate_name: N,N,N-trimethylamine

smiles: CN(C)C

proof_lines: the Km for isoform FMO3 determined in human liver microsomes ranges from 0.013.to 0.0548 mM, at pH 7.4 and 22°C

proof_lines: recombinant isoform FMO3, at pH 7.4 and 22°C

enzyme: trimethylamine monooxygenase

substrate: N,N,N-trimethylamine


enzyme_display_name: UniProt P47934

organism: Mus musculus

substrate_name: hexanoyl-CoA

enzyme: UniProt P47934

substrate: hexanoyl-CoA


enzyme_display_name: UniProt P43155

substrate_name: L-carnitine

enzyme: UniProt P43155

substrate: L-carnitine


substrate_name: carnitine

substrate: carnitine


substrate_name: CoA

substrate: CoA


enzyme_display_name: acetyl-CoA C-acetyltransferase

organism: Bacopa monnieri

substrate_name: acetoacetyl-CoA

enzyme: acetyl-CoA C-acetyltransferase

substrate: acetoacetyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: UniProt P76461

enzyme: UniProt P76461


enzyme_display_name: Acetyl-CoA acetyltransferase erg10B, cytosolic

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

substrate_name: acetoacetyl-CoA (in law salt conditions)


enzyme_display_name: UniProt Q2KIR7

organism: Bos taurus

substrate_name: glycine

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

enzyme: UniProt Q2KIR7

substrate: glycine


substrate_name: benzoyl-CoA

substrate: benzoyl-CoA


enzyme_display_name: ent-kaurene monooxygenase

organism: Malus sp.

substrate_name: Unknown

enzyme: ent-kaurene monooxygenase

substrate: Unknown


enzyme_display_name: coenzyme F420 hydrogenase

organism: Methanosarcina barkeri

smiles: [HH]

proof_lines: 37°C, pH 7.2, cosubstrate: oxidized coenzyme F420

proof_lines: 37°C, pH 7.2, cosubstrate: oxidized methyl viologen

enzyme: coenzyme F420 hydrogenase


substrate_name: oxidized coenzyme F420

substrate: oxidized coenzyme F420


organism: Methanothermobacter thermautotrophicus


enzyme_display_name: ribonucleoside-diphosphate reductase

substrate_name: CDP

assay_conditions_summary: cofactor ATP

proof_lines: CDP reduction in the absence of allosteric effectors

proof_lines: CDP reduction in the presence of 1 mM ATP

proof_lines: CDP reduction in the presence of 0.2 mM ATP

enzyme: ribonucleoside-diphosphate reductase

substrate: CDP


enzyme_display_name: gibberellin 2beta-dioxygenase

organism: Lathyrus oleraceus

substrate_name: gibberellin 20

proof_lines: in 100 mM Tris-HCl pH 7.9 containing 4 mM ascorbate, 4 mM DTT, 4 mM 2-oxoglutarate, 0.5 mM FeSO4, 2 mg/ml bovine serum albumin and 1 mg/ml catalase

enzyme: gibberellin 2beta-dioxygenase

substrate: gibberellin 20


substrate_name: Ngamma-hydroxy-L-arginine

proof_lines:
nonlinear regression analysis
Eadie-Hofstee graph
25°C, with tetrahydrobiopterin

substrate: Ngamma-hydroxy-L-arginine


enzyme_display_name: cysteine dioxygenase

substrate_name: L-cysteine

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

proof_lines: presence of 0.1 mol Fe2+, absence of EDTA. Cysteine sulfinic acid content is determined by ion-paired reverse-phase chromatopraphy using UV detection at 215 nm.

enzyme: cysteine dioxygenase

substrate: L-cysteine


enzyme_display_name: thiopurine S-methyltransferase

enzyme: thiopurine S-methyltransferase


enzyme_display_name: UniProt P35610

organism: Homo sapiens

substrate_name: pregnenolone

enzyme: UniProt P35610

substrate: pregnenolone


substrate_name: vitamin K1 2,3-epoxide

substrate: vitamin K1 2,3-epoxide


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Nitratidesulfovibrio vulgaris

substrate_name: [Fe] hydrogenase-cytochrome Hmc complex

proof_lines:
pH 7.0, electron transfer kinetics
25°C, pH 7.0

enzyme: cytochrome-c3 hydrogenase

substrate: [Fe] hydrogenase-cytochrome Hmc complex


enzyme_display_name: catechol 1,2-dioxygenase

organism: Nocardia sp.

substrate_name: catechol

proof_lines:
immobilized enzyme
free enzyme

enzyme: catechol 1,2-dioxygenase

substrate: catechol


substrate_name: GDP

substrate: GDP


enzyme_display_name: UniProt Q401L4

organism: Entamoeba histolytica

substrate_name: L-serine

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

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=8

enzyme: UniProt Q401L4

substrate: L-serine


enzyme_display_name: UniProt P43886

organism: Haemophilus influenzae

enzyme: UniProt P43886


enzyme_display_name: UniProt P9WPZ3

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WPZ3


enzyme_display_name: chlorite O2-lyase

organism: Nitrospira defluvii

substrate_name: Chlorite

smiles: [O-]Cl=O

enzyme: chlorite O2-lyase

substrate: Chlorite


enzyme_display_name: ferroxidase

organism: Ovis aries

enzyme: ferroxidase


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


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: L-arginine

proof_lines:
detrusor
urethra
pH 7.4, 30°C

enzyme: nitric-oxide synthase (NADPH)

substrate: L-arginine


enzyme_display_name: UniProt P9WNG5

substrate_name: malonyl-CoA

enzyme: UniProt P9WNG5

substrate: malonyl-CoA


organism: Cavia porcellus

substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: caffeate O-methyltransferase

organism: Populus trichocarpa

proof_lines: isoform COMT2, in 50 mM Tris-HCl, pH 7.5, at 30°C

enzyme: caffeate O-methyltransferase


organism: Oryza sativa


organism: Pseudomonas aeruginosa

proof_lines:
pH 7.5, 25°C
pH 7.5, 25°C, in presence of ascorbate


enzyme_display_name: mercury(II) reductase

substrate_name: NADPH

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH

proof_lines:
in presence of 1 mM cysteine
25°C, pH 7.3

enzyme: mercury(II) reductase

substrate: NADPH


enzyme_display_name: protocatechuate 3,4-dioxygenase

substrate_name: Unknown

enzyme: protocatechuate 3,4-dioxygenase

substrate: Unknown


enzyme_display_name: nitrite reductase (NO-forming)

substrate_name: ferricytochrome c551

proof_lines: recombinant Y10F mutant enzyme, at pH 6.2 and 27°C

enzyme: nitrite reductase (NO-forming)

substrate: ferricytochrome c551


organism: Pseudomonas chlororaphis

substrate_name: nitrite

assay_conditions_summary: pH 7

proof_lines:
pH 7.0, electron donor azurin
pH 7.0, electron donor benzyl viologen

substrate: nitrite


enzyme_display_name: homogentisate 1,2-dioxygenase

organism: Pseudomonas fluorescens

substrate_name: homogentisate

assay_conditions_summary: pH 6

enzyme: homogentisate 1,2-dioxygenase

substrate: homogentisate


enzyme_display_name: UniProt Q9H7Z6

enzyme: UniProt Q9H7Z6


enzyme_display_name: UniProt Q93UV0

organism: Sphingomonas paucimobilis

substrate_name: caproyl-CoA

enzyme: UniProt Q93UV0

substrate: caproyl-CoA


organism: Pseudomonas putida


enzyme_display_name: benzoate 1,2-dioxygenase

substrate_name: benzoate

assay_conditions_summary: pH 6.8; cofactor NADH

proof_lines: at pH 6.8 temperature not specified in the publication

proof_lines: in the presence of saturating amounts of NADH-cytochrome c reductase

enzyme: benzoate 1,2-dioxygenase

substrate: benzoate


proof_lines: multi-walled carbon nanotube-immobilized enzyme, at pH 10.0 and 60°C


enzyme_display_name: 2-oxoadipate dioxygenase/decarboxylase

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

enzyme: 2-oxoadipate dioxygenase/decarboxylase


proof_lines:
6°C, pH 7.3
in presence of 1 mM cysteine
1 mM cysteine, 25°C, pH 7.3


organism: Pseudomonas sp.

substrate_name: L-glutamate

assay_conditions_summary: cofactor FMN

proof_lines:
5-deazaFMN reconstituted enzyme
FMN reconstituted enzyme

substrate: L-glutamate


substrate_name: ammonia

smiles: N

substrate: ammonia


substrate_name: Hg

smiles: [Hg]

substrate: Hg


enzyme_display_name: trans-cinnamate 4-monooxygenase

organism: Pyrus x bretschneideri

substrate_name: trans-cinnamate

enzyme: trans-cinnamate 4-monooxygenase

substrate: trans-cinnamate


enzyme_display_name: UniProt K9MUA0

organism: Malus domestica

enzyme: UniProt K9MUA0


proof_lines:
at pH 7.0
at pH 8.4


enzyme_display_name: gentisate 1,2-dioxygenase

organism: Ralstonia solanacearum

enzyme: gentisate 1,2-dioxygenase


enzyme_display_name: cysteine dioxygenase

organism: Rattus norvegicus

substrate_name: L-cysteine

assay_conditions_summary: pH 6.1; 310.15 K; buffer the presence of 62.5 mM Mes

proof_lines: assay standart conditions are: the enzyme is incubated at 37°C in the presence of 62.5 mM Mes buffer (pH 6.1), 0.3 mM ferrous sulfate, 0.0125 mM bathocuproine disulfonate and 1.2 mM cysteine

enzyme: cysteine dioxygenase

substrate: L-cysteine


organism: Homo sapiens

substrate_name: beta-D-glucosamine

substrate: beta-D-glucosamine


enzyme_display_name: UniProt Q51405

substrate_name: neomycin E

enzyme: UniProt Q51405

substrate: neomycin E


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: neomycin

substrate: neomycin


substrate_name: sisomycin

substrate: sisomycin


substrate_name: kanamycin A

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.6
Raw SKiD Env: Temp=25°C, pH=6.6

substrate: kanamycin A


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: tobramycin

substrate: tobramycin


enzyme_display_name: UniProt Q44057

organism: Acinetobacter haemolyticus

substrate_name: arbekacin

enzyme: UniProt Q44057

substrate: arbekacin


substrate_name: dibekacin

substrate: dibekacin


substrate_name: sisomicin

substrate: sisomicin


substrate_name: butirosin A

substrate: butirosin A


substrate_name: gentamicin

substrate: gentamicin


substrate_name: tobramicin

substrate: tobramicin


substrate_name: neomycin C

substrate: neomycin C


substrate_name: amikacin

substrate: amikacin


substrate_name: isepamicin

substrate: isepamicin


enzyme_display_name: UniProt Q43899

organism: Acinetobacter baumannii

enzyme: UniProt Q43899


enzyme_display_name: UniProt P19096

organism: Mus musculus

substrate_name: crotonyl-CoA

enzyme: UniProt P19096

substrate: crotonyl-CoA


substrate_name: phenylacetyl-CoA

substrate: phenylacetyl-CoA


substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: methylmalonyl-CoA

substrate: methylmalonyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


substrate_name: succinyl-CoA

substrate: succinyl-CoA


substrate_name: octanoyl-CoA

substrate: octanoyl-CoA


substrate_name: L-cysteine

proof_lines: 20% cross-linked wild-type enzyme, pH 9.1, temperature not specified in the publication

proof_lines: 60% cross-linked wild-type enzyme, pH 7.7, temperature not specified in the publication

proof_lines: not cross-linked wild-type enzyme, pH 7.7, temperature not specified in the publication

substrate: L-cysteine


enzyme_display_name: aminoglycoside 6'-N-acetyltransferase

organism: Enterococcus faecium

enzyme: aminoglycoside 6'-N-acetyltransferase


substrate_name: neomycin

substrate: neomycin


substrate_name: kanamycin A

substrate: kanamycin A


substrate_name: neamine

substrate: neamine


substrate_name: acetyl-CoA

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: tobramycin

substrate: tobramycin


proof_lines:
pH 6.0, 37°C, wild-type enzyme
wild-type enzyme


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: amikacin

substrate: amikacin


substrate_name: neomycin C

substrate: neomycin C


substrate_name: propionyl-CoA

substrate: propionyl-CoA


substrate_name: sisomicin

substrate: sisomicin


substrate_name: gentamicin B

substrate: gentamicin B


substrate_name: butirosin

substrate: butirosin


substrate_name: netilmicin

substrate: netilmicin


substrate_name: dibekacin

substrate: dibekacin


enzyme_display_name: alcohol O-acetyltransferase

organism: Fragaria x ananassa

substrate_name: eugenol

enzyme: alcohol O-acetyltransferase

substrate: eugenol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: hexanoyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

proof_lines: cosubstrate cinnamyl alcohol, pH 7.5, 30°C

substrate: hexanoyl-CoA


substrate_name: butanoyl-CoA

substrate: butanoyl-CoA


organism: Streptomyces noursei


substrate_name: neomycin B

substrate: neomycin B


substrate_name: kanamycin A

substrate: kanamycin A


substrate_name: n-propionyl-CoA

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

substrate: n-propionyl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: lividomycin A

substrate: lividomycin A


substrate_name: n-butyryl-CoA

substrate: n-butyryl-CoA


substrate_name: malonyl-CoA

substrate: malonyl-CoA


substrate_name: ribostamycin

substrate: ribostamycin


substrate_name: neamine

substrate: neamine


substrate_name: neomycin C

substrate: neomycin C


organism: Petunia x hybrida

substrate_name: coniferyl alcohol

assay_conditions_summary: pH 7.5; 293.15 K; cofactor CoA

proof_lines: recombinant protein with acetyl-CoA, pH 6.0, 20°C

proof_lines: apparent KM value of recombinant protein with acetyl-CoA, pH 7.5, 20°C

substrate: coniferyl alcohol


substrate_name: benzyl alcohol

proof_lines: recombinant protein with acetyl-CoA, pH 7.5, 20°C

substrate: benzyl alcohol


proof_lines: recombinant protein with 2-phenylethanol, pH 7.5, 20°C

proof_lines: recombinant protein with benzyl alcohol, pH 7.5, 20°C

proof_lines: recombinant protein with coniferyl alcohol, pH 7.5, 20°C


substrate_name: alpha-D-glucosamine

substrate: alpha-D-glucosamine


organism: uncultured bacterium

substrate_name: kanamycin

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=kanamycin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 0.207 s^-1; K0.5 0.3464 mM (not paper-labeled Km); kcat/K0.5 0.6 s^-1 mM^-1. Expected row has Km 0.346 mM and kcat_over_km 0.598266 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column kanamycin

table_label: Table 1. Steady State Kinetic Parameters for the Wild-Type meta-AAC Proteins and AAC(3)-Ib

substrate: kanamycin


substrate_name: tobramycin

proof_lines:
wild-type enzyme
pH 6.0, 37°C, wild-type enzyme

substrate: tobramycin


substrate_name: gentamicin C

substrate: gentamicin C


organism: Rosa hybrid cultivar


proof_lines:
cosubstrate: benzyl alcohol
cosubstrate: geraniol
cosubstrate: phenylethanol


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


substrate_name: phenyl ethanol

substrate: phenyl ethanol


organism: Musa x paradisiaca


substrate_name: Isoamylalcohol

smiles: CC(C)CCO

substrate: Isoamylalcohol


organism: Mycobacterium tuberculosis

substrate_name: amikacin

substrate: amikacin


organism: Cymbopogon martini

smiles: CCC=CCCO


substrate_name: (-)-beta-citronellol

smiles: CC(CCC=C(C)C)CCO

substrate: (-)-beta-citronellol


substrate_name: Heptanol

smiles: CCCCCCCO

substrate: Heptanol


substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


substrate_name: Nonanol

smiles: CCCCCCCCCO

substrate: Nonanol


organism: Hanseniaspora valbyensis

substrate_name: 2-phenylethyl alcohol

substrate: 2-phenylethyl alcohol


substrate_name: isoamyl alcohol

substrate: isoamyl alcohol


substrate_name: Unknown

proof_lines:
versus acetyl-CoA
versus N-acetyl-alpha-D-glucosamine
versus glusosamine, no detergents added

substrate: Unknown


enzyme_display_name: aminoglycoside 3-N-acetyltransferase

organism: Corynebacterium striatum

substrate_name: dibekacin

proof_lines: recombinant His-tagged enzyme, pH 6.0, 37°C

enzyme: aminoglycoside 3-N-acetyltransferase

substrate: dibekacin


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: Propanol

smiles: CCCO

substrate: Propanol


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: geraniol

substrate: geraniol


proof_lines:
cosubstrate heptanol, pH 7.5, 30°C
cosubstrate eugenol, pH 7.5, 30°C
cosubstrate octanol, pH 7.5, 30°C


substrate_name: Pentanol

smiles: CCCCCO

substrate: Pentanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: sisomicin

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=sisomicin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 2.42 s^-1; K0.5 0.038 mM (not paper-labeled Km); kcat/K0.5 64 s^-1 mM^-1. Expected row has Km 0.038 mM and kcat_over_km 63.6842 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column sisomicin

substrate: sisomicin


substrate_name: tobramycin

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=tobramycin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 1.2 s^-1; K0.5 0.028 mM (not paper-labeled Km); kcat/K0.5 43 s^-1 mM^-1. Expected row has Km 0.028 mM and kcat_over_km 42.8571 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column tobramycin

substrate: tobramycin


substrate_name: gentamycin

column_label: Table 1 columns enzyme=meta-AAC0020, substrate=gentamicin; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 1.17 s^-1; K0.5 0.022 mM (not paper-labeled Km); kcat/K0.5 52 s^-1 mM^-1. Expected row has Km 0.022 mM and kcat_over_km 53.1818 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column gentamicin

substrate: gentamycin


substrate_name: kanamycin

substrate: kanamycin


column_label: Table 1 columns enzyme=meta-AAC0020, substrate=acetyl-CoA; kinetic parameter rows K0.5 (uM), kcat (s^-1), kcat/K0.5 (M^-1 s^-1, x10^4), and H.

normalized_value_unit_evidence: kcat 1.51 s^-1; K0.5 0.021 mM (not paper-labeled Km); kcat/K0.5 69 s^-1 mM^-1. Expected row has Km 0.021 mM and kcat_over_km 71.9048 s^-1 mM^-1, but the primary metric labels are K0.5 and kcat/K0.5.

row_label: meta-AAC0020; substrate column acetyl-CoA


organism: Mycobacteroides abscessus

assay_conditions_summary: 298.15 K; cofactor CoA

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


organism: Rattus norvegicus

substrate_name: dolichol

substrate: dolichol


substrate_name: poly-L-Lys

proof_lines:
pH 7.5, 37°C
competitive inhibition

substrate: poly-L-Lys


organism: Staphylococcus aureus

substrate_name: Unknown

proof_lines: pH 6.9, 37°C, inhibition of the reaction with neamine

substrate: Unknown


enzyme_display_name: UniProt A0QY29

organism: Mycolicibacterium smegmatis

substrate_name: propionyl-CoA

enzyme: UniProt A0QY29

substrate: propionyl-CoA


substrate_name: octopamine

substrate: octopamine


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: histamine

substrate: histamine


enzyme_display_name: UniProt P9WFK7

enzyme: UniProt P9WFK7


organism: Sus scrofa


enzyme_display_name: fatty-acid synthase system

enzyme: fatty-acid synthase system


enzyme_display_name: Maltose O-acetyltransferase

organism: Escherichia coli (strain K12)

substrate_name: maltotriose

proof_lines: Acetylates glucose, maltose, mannose, galactose, and fructose with a decreasing relative rate of 1, 0.55, 0.20, 0.07, 0.04.

enzyme: Maltose O-acetyltransferase

substrate: maltotriose


substrate_name: Acetyl-CoA; L-cysteine-S-conjugate

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

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; L-cysteine-S-conjugate


organism: Escherichia coli

substrate_name: Ciprofloxacin

substrate: Ciprofloxacin


substrate_name: Norfloxacin

substrate: Norfloxacin


substrate_name: kanamycin B

substrate: kanamycin B


substrate_name: neomycin B

substrate: neomycin B


enzyme_display_name: UniProt Q9GPZ4

organism: Leishmania major

substrate_name: myristoyl-CoA

enzyme: UniProt Q9GPZ4

substrate: myristoyl-CoA


enzyme_display_name: UniProt Q9UVX3

organism: Aspergillus fumigatus

substrate_name: myristoleoyl-CoA

enzyme: UniProt Q9UVX3

substrate: myristoleoyl-CoA


enzyme_display_name: quinate O-hydroxycinnamoyltransferase

organism: Solanum lycopersicum

substrate_name: coumaroyl-CoA

enzyme: quinate O-hydroxycinnamoyltransferase

substrate: coumaroyl-CoA


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: chlorogenic acid

substrate: chlorogenic acid


substrate_name: CoA

substrate: CoA


substrate_name: glucose

substrate: glucose


substrate_name: maltose

substrate: maltose


enzyme_display_name: fatty-acid synthase

substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH; Acetyl-CoA; H+

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

assay_conditions_summary: cofactor NADPH

enzyme: fatty-acid synthase


organism: Homo sapiens


organism: Acinetobacter baumannii

substrate_name: 2'-N-ethyl netilmicin

substrate: 2'-N-ethyl netilmicin


organism: Saccharomyces cerevisiae

substrate_name: Acetyl-CoA; 3-Methylbutanol

substrate: Acetyl-CoA; 3-Methylbutanol


organism: Gallus gallus

substrate_name: Acetyl-CoA; H+; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA

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


substrate_name: n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA; Acetyl-CoA; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH


organism: Anthoceros agrestis

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

proof_lines: cosubstrate shikimate, Hanes-Woolf plot, pH 7.0, 30°C

proof_lines: cosubstrate shikimate, Michaelis-Menten plot, pH 7.0, 30°C

proof_lines: cosubstrate 3-hydroxyanthranilate, Michaelis-Menten plot, pH 9.0, 30°C


proof_lines: cosubstrate 2,3-dihydroxybenzoate, Hanes-Woolf plot, pH 7.0, 30°C


substrate_name: shikimate

proof_lines: cosubstrate 4-coumaroyl-CoA, Michaelis-Menten plot, pH 7.0, 30°C

proof_lines: cosubstrate 4-coumaroyl-CoA, Hanes-Woolf plot, pH 7.0, 30°C

proof_lines: cosubstrate caffeoyl-CoA, Michaelis-Menten plot, pH 7.0, 30°C

substrate: shikimate


assay_conditions_summary: pH 9; 303.15 K; cofactor CoA

proof_lines: cosubstrate 4-coumaroyl-CoA, Michaelis-Menten plot, pH 9.0, 30°C

proof_lines: cosubstrate 4-coumaroyl-CoA, Hanes-Woolf plot, pH 9.0, 30°C

proof_lines: cosubstrate caffeoyl-CoA, Michaelis-Menten plot, pH 9.0, 30°C


proof_lines: cosubstrate caffeoyl-CoA, Hanes-Woolf plot, pH 7.0, 30°C


organism: Malus sylvestris


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: quinate

substrate: quinate


substrate_name: Acetyl-CoA; beta-D-Glucosamine

assay_conditions_summary: pH 6.5; 310.15 K; cofactor CoA

proof_lines: substrate 1-[4,4-difluoro-5,7-dimethyl-4-bora-3a,4a-diaza-s-indacene-3-propionyl-glycylamino]-beta-D-glucosamine, pH 6.5, 37°C

substrate: Acetyl-CoA; beta-D-Glucosamine


substrate_name: Unknown

substrate: Unknown


organism: Columba sp.

substrate_name: H+; Acetyl-CoA; n n n n n n n n n n n n n n n n n n n n n n n n n n n n n n Malonyl-CoA; 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n 2n NADPH


organism: Fragaria x ananassa

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row 2-Phenyl ethanol; columns Km (mM), Kcat, Kcat/Km; cells 4.32, 49.6, 11.4

raw_value_unit_evidence: 2-Phenyl ethanol: Km=4.32 mM; kcat=49.6 s^-1; kcat/Km=11.4 s^-1 mM^-1

row_label: 2-Phenyl ethanol


substrate_name: acetyl-CoA

column_label: Table 3. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols in combination with acetyl-CoA at variable concentrations; row Cinnamyl alcohol; columns Km (uM), Kcat, Kcat/Km; cells 77, 3890, 50.53

raw_value_unit_evidence: Cinnamyl alcohol co-substrate / acetyl-CoA varied: Km=77 uM; kcat=3890 s^-1; kcat/Km=50.53 s^-1 uM^-1

substrate: acetyl-CoA


substrate_name: benzyl alcohol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Benzyl Alcohol; columns Km (mM), Kcat, Kcat/Km; cells 4.57, 23.5, 5.14

raw_value_unit_evidence: Benzyl Alcohol: Km=4.57 mM; kcat=23.5 s^-1; kcat/Km=5.14 s^-1 mM^-1

row_label: Benzyl Alcohol

substrate: benzyl alcohol


substrate_name: butanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Butanol; columns Km (mM), Kcat, Kcat/Km; cells 2.34, 21.5, 9.1

row_label: Butanol

substrate: butanol


substrate_name: cinnamyl alcohol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Cinnamyl Alcohol; columns Km (mM), Kcat, Kcat/Km; cells 2.03, 1480, 727

raw_value_unit_evidence: Cinnamyl Alcohol: Km=2.03 mM; kcat=1480 s^-1; kcat/Km=727 s^-1 mM^-1

row_label: Cinnamyl Alcohol

substrate: cinnamyl alcohol


substrate_name: ethanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Ethanol; columns Km (mM), Kcat, Kcat/Km; cells 4.35, 7.5, 1.7

row_label: Ethanol

substrate: ethanol


substrate_name: eugenol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Eugenol; columns Km (mM), Kcat, Kcat/Km; cells 3.78, 548.5, 150

row_label: Eugenol

substrate: eugenol


substrate_name: geraniol

smiles: CC(C)=CCC/C(C)=C/CO

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Geraniol; columns Km (mM), Kcat, Kcat/Km; cells 2.04, 370.5, 180

row_label: Geraniol

substrate: geraniol


substrate_name: Heptanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Heptanol; columns Km (mM), Kcat, Kcat/Km; cells 2.71, 170, 62

raw_value_unit_evidence: Heptanol: Km=2.71 mM; kcat=170 s^-1; kcat/Km=62 s^-1 mM^-1

row_label: Heptanol

substrate: Heptanol


substrate_name: Hexanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Hexanol; columns Km (mM), Kcat, Kcat/Km; cells 1.53, 483, 314

row_label: Hexanol

substrate: Hexanol


organism: Solanum tuberosum

substrate_name: CoA

substrate: CoA


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


substrate_name: chlorogenic acid

substrate: chlorogenic acid


organism: Bambusa multiplex


assay_conditions_summary: pH 8; 313.15 K; cofactor CoA


substrate_name: feruloyl-CoA


substrate_name: quinate


organism: Pseudomonas aeruginosa

substrate_name: gentamicin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y146F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor CoA

column_label: Table 3; row Y146F; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=4.33 s^-1; kcat/Km=510 s^-1 mM^-1; Km=0.0085 mM. Export values: Km=0.0085 mM; kcat=4.33 s^-1; kcat/Km=509.412 s^-1 mM^-1.

substrate: gentamicin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y64F to reconstruct the assayed variant sequence.

column_label: Table 3; row Y64F; columns kcat (s^-1), kcat/Km (s^-1 uM^-1), Km (uM).

normalized_value_unit_evidence: Normalized paper values: kcat=12.5 s^-1; kcat/Km=870 s^-1 mM^-1; Km=0.0143 mM. Export values: Km=0.0143 mM; kcat=12.5 s^-1; kcat/Km=874.126 s^-1 mM^-1.


substrate_name: neomycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Neomycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0066 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Neomycin: kcat 6.15 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.93 s^-1 uM^-1 (930.0 s^-1 mM^-1).

row_label: Neomycin


substrate_name: paromomycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Paromomycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0067 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Paromomycin: kcat 5.52 s^-1; Km 6.7 uM (0.0067 mM); kcat/Km 0.82 s^-1 uM^-1 (820.0 s^-1 mM^-1).

row_label: Paromomycin


substrate_name: ribostamycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Ribostamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0079 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Ribostamycin: kcat 5.38 s^-1; Km 7.9 uM (0.0079 mM); kcat/Km 0.68 s^-1 uM^-1 (680.0 s^-1 mM^-1).

row_label: Ribostamycin


substrate_name: sisomicin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Sisomicin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.0109 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Sisomicin: kcat 10.48 s^-1; Km 10.9 uM (0.0109 mM); kcat/Km 0.97 s^-1 uM^-1 (970.0 s^-1 mM^-1).

row_label: Sisomicin


substrate_name: gentamicin (at pH 6.5 and 22 degrees Celsius)

column_label: PDF Table 4. Kinetic parameters for antibiotics row Gentamicin; Km normalized_value=0.0101 normalized_unit=mM.

raw_value_unit_evidence: Km raw_value=10.1 raw_unit=uM.

row_label: Gentamicin


substrate_name: kanamycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Kanamycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

normalized_value_unit_evidence: km paper=0.007 mM

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Kanamycin: kcat 4.45 s^-1; Km 7 uM (0.007 mM); kcat/Km 0.63 s^-1 uM^-1 (630.0 s^-1 mM^-1).

row_label: Kanamycin


substrate_name: tobramycin (at pH 6.5 and 22 degrees Celsius)

column_label: Table 4. Kinetic parameters for antibiotics; row Tobramycin; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1) as required for this row.

raw_value_unit_evidence: Table 4. Kinetic parameters for antibiotics, row Tobramycin: kcat 5.68 s^-1; Km 6.6 uM (0.0066 mM); kcat/Km 0.86 s^-1 uM^-1 (860.0 s^-1 mM^-1).

row_label: Tobramycin


organism: Nicotiana tabacum

assay_conditions_summary: pH 6.6; 303.15 K; cofactor CoA

proof_lines:
pH 6.6, 30°C, cosubstrate: shikimate
pH 6.6, 30°C, cosubstrate: quinate


substrate_name: p-Coumaroyl-CoA

proof_lines:
pH 6.6, 30°C, cosubstrate: quinate
pH 6.6, 30°C, cosubstrate: shikimate

substrate: p-Coumaroyl-CoA


substrate: feruloyl-CoA


substrate_name: shikimate

proof_lines: pH 6.6, 30°C, cosubstrate: p-coumaroyl-CoA

substrate: shikimate


organism: Lonicera japonica

assay_conditions_summary: 303.15 K; cofactor CoA

proof_lines: cosubstrate 4-coumaroyl-CoA, pH not specified in the publication, 30°C


proof_lines: cosubstrate CoA, pH not specified in the publication, 30°C


proof_lines: cosubstrate quinate, pH not specified in the publication, 30°C


organism: Taraxacum antungense

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


substrate: quinate


organism: Cichorium endivia

substrate_name: coumaroyl-CoA

substrate: coumaroyl-CoA


organism: Marchantia paleacea


assay_conditions_summary: pH 6.5; 303.15 K; cofactor CoA


enzyme_display_name: trihydroxystilbene synthase

organism: Cannabis sativa

enzyme: trihydroxystilbene synthase


substrate_name: Dihydrocaffeoyl-CoA

substrate: Dihydrocaffeoyl-CoA


organism: Rattus norvegicus

substrate_name: palmitoyl-CoA

substrate: palmitoyl-CoA


substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


substrate_name: stearoyl-CoA

substrate: stearoyl-CoA


substrate_name: myristoyl-CoA

substrate: myristoyl-CoA


organism: Pinus strobus

assay_conditions_summary: pH 4; 303.15 K; cofactor CoA


substrate_name: Unknown

proof_lines:
pH 4.0, 30°C, uncompetitive inhibition
pH 4.0, 30°C, competitive inhibition

substrate: Unknown


organism: Plagiochasma appendiculatum


substrate_name: quinate


organism: Homo sapiens

substrate_name: HIV1 Nef protein N-terminal peptide

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

substrate: HIV1 Nef protein N-terminal peptide


organism: Solanum lycopersicum

substrate_name: glucaric acid

substrate: glucaric acid


substrate_name: chlorogenic acid


organism: Secale cereale

substrate_name: feruloyl-CoA


organism: Pinus massoniana

assay_conditions_summary: pH 4; cofactor CoA

column_label: Table 3; P. massoniana column; rows kcat (min^-1), Km (uM), and kcat/Km (M^-1 s^-1)

row_label: P. massoniana stilbene synthase


assay_conditions_summary: pH 7.9; 298.15 K; cofactor CoA


proof_lines:
with coumaroyl-CoA
with caffeoyl-CoA


enzyme_display_name: 6-deoxyerythronolide-B synthase

organism: Saccharopolyspora erythraea

substrate_name: propanoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S315A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; cofactor CoA

proof_lines: mutant S315A, pH 7.2, temperature not specified in the publication

enzyme: 6-deoxyerythronolide-B synthase

substrate: propanoyl-CoA


organism: uncultured archaeon

substrate_name: formylmethanofuran

substrate: formylmethanofuran


enzyme_display_name: UniProt P30419

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines: kcat is 0.41 sec(-1) with tetradecanoyl-CoA as substrate.

enzyme: UniProt P30419


substrate_name: caffeoyl-CoA

assay_conditions_summary: pH 7.5; cofactor CoA

substrate: caffeoyl-CoA


column_label: Official Thieme full-text HTML Figure 5 caption, panel a, reports caffeoyl-CoA Km=293.6 uM and Vmax=79.0 nkat/mg; required metric for this row is Km only.

normalized_value_unit_evidence: Km 0.2936 mM; matches exported Km 0.2936 mM.

raw_value_unit_evidence: Fig. 5 panel a: Km 293.6 uM and Vmax 79.0 nkat/mg for caffeoyl-CoA.

row_label: Varying caffeoyl-CoA / recombinant HQT

table_label: Fig. 5


proof_lines: cosubstrate caffeoyl-CoA, pH not specified in the publication, 30°C


assay_conditions_summary: pH 7; cofactor CoA

column_label: Results section prose, right column, journal page 747: tobacco HQT Km for quinate 871 +/- 53 uM.

raw_value_unit_evidence: Results prose reports tobacco HQT Km for quinate as 871 +/- 53 uM.

row_label: Tobacco HQT; quinate Km

table_label: Results prose, journal page 747


organism: Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)


enzyme_display_name: Formyltransferase/hydrolase complex subunit D

organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)


proof_lines:
pH 7.4, 37°C, isozyme NMT2
pH 7.9-8.0, 25°C, isozyme NMT2


organism: Leishmania major

substrate_name: Myristoyl-CoA; Glycylpeptide

assay_conditions_summary: cofactor CoA

substrate: Myristoyl-CoA; Glycylpeptide


organism: Plasmodium vivax

substrate_name: peptide pp60src(2-16)

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

substrate: peptide pp60src(2-16)


organism: Trypanosoma brucei

substrate_name: Glycylpeptide; Myristoyl-CoA

substrate: Glycylpeptide; Myristoyl-CoA


substrate_name: coumaroylquinate

substrate: coumaroylquinate


organism: Vitis vinifera

column_label: Table 3; V. vinifera column; rows kcat (min^-1), Km (uM), and kcat/Km (M^-1 s^-1)

row_label: V. vinifera stilbene synthase


organism: Acinetobacter baumannii

substrate_name: 2'-N-ethyl netilmicin

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / 2'-N-ethyl netilmicin; organism mapping Acinetobacter baumannii

normalized_value_unit_evidence: Normalized evidence: kcat=0.098 s^-1; km/S0.5=0.049 mM; kcat_over_km=2 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / 2'-N-ethyl netilmicin; kcat 0.098 s^-1; S0.5 49.0 ± 5.9 μM (normalized km 0.049 mM); kcat/S0.5 2.00 x10^3 M^-1 s^-1 (normalized kcat_over_km 2 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / 2'-N-ethyl netilmicin

table_label: ACS Infectious Diseases 2016 Table 1

substrate: 2'-N-ethyl netilmicin


substrate_name: amikacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / amikacin; organism mapping Acinetobacter baumannii; kcat_over_km paper=4.98 s^-1 mM^-1; export=4.97991967871486 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.496 s^-1; km/S0.5=0.0996 mM; kcat_over_km=4.98 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / amikacin; kcat 0.496 s^-1; S0.5 99.6 ± 12.5 μM (normalized km 0.0996 mM); kcat/S0.5 4.98 x10^3 M^-1 s^-1 (normalized kcat_over_km 4.98 s^-1 mM^-1).

row_label: AAC(6′)-Ih / amikacin

substrate: amikacin


substrate_name: arbekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / arbekacin; organism mapping Acinetobacter baumannii; kcat_over_km paper=3.56 s^-1 mM^-1; export=3.5593220338983054 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.021 s^-1; km/S0.5=0.0059 mM; kcat_over_km=3.56 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / arbekacin; kcat 0.021 s^-1; S0.5 5.9 ± 0.8 μM (normalized km 0.0059 mM); kcat/S0.5 3.56 x10^3 M^-1 s^-1 (normalized kcat_over_km 3.56 s^-1 mM^-1).

row_label: AAC(6′)-Ih / arbekacin

substrate: arbekacin


substrate_name: butirosin A

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / butirosin A; organism mapping Acinetobacter baumannii; kcat_over_km paper=5.23 s^-1 mM^-1; export=5.231481481481481 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.113 s^-1; km/S0.5=0.0216 mM; kcat_over_km=5.23 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / butirosin A; kcat 0.113 s^-1; S0.5 21.6 ± 2.4 μM (normalized km 0.0216 mM); kcat/S0.5 5.23 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.23 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / butirosin A

substrate: butirosin A


substrate_name: dibekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / dibekacin; organism mapping Acinetobacter baumannii; kcat_over_km paper=4.08 s^-1 mM^-1; export=4.081632653061225 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.04 s^-1; km/S0.5=0.0098 mM; kcat_over_km=4.08 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / dibekacin; kcat 0.040 s^-1; S0.5 9.8 ± 1.4 μM (normalized km 0.0098 mM); kcat/S0.5 4.08 x10^3 M^-1 s^-1 (normalized kcat_over_km 4.08 s^-1 mM^-1).

row_label: AAC(6′)-Ih / dibekacin

substrate: dibekacin


substrate_name: gentamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / gentamicin; organism mapping Acinetobacter baumannii; kcat_over_km paper=1.84 s^-1 mM^-1; export=1.8390804597701151 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.016 s^-1; km/S0.5=0.0087 mM; kcat_over_km=1.84 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / gentamicin; kcat 0.016 s^-1; S0.5 8.7 ± 3.1 μM (normalized km 0.0087 mM); kcat/S0.5 1.84 x10^3 M^-1 s^-1 (normalized kcat_over_km 1.84 s^-1 mM^-1).

row_label: AAC(6′)-Ih / gentamicin

substrate: gentamicin


substrate_name: isepamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / isepamicin; organism mapping Acinetobacter baumannii; kcat_over_km paper=5.59 s^-1 mM^-1; export=5.585585585585585 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.62 s^-1; km/S0.5=0.111 mM; kcat_over_km=5.59 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / isepamicin; kcat 0.620 s^-1; S0.5 111 ± 13 μM (normalized km 0.111 mM); kcat/S0.5 5.59 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.59 s^-1 mM^-1).

row_label: AAC(6′)-Ih / isepamicin

substrate: isepamicin


substrate_name: kanamycin B

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / kanamycin B; organism mapping Acinetobacter baumannii

normalized_value_unit_evidence: Normalized evidence: kcat=0.06 s^-1; km/S0.5=0.012 mM; kcat_over_km=5 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / kanamycin B; kcat 0.060 s^-1; S0.5 12.0 ± 1.1 μM (normalized km 0.012 mM); kcat/S0.5 5.00 x10^3 M^-1 s^-1 (normalized kcat_over_km 5 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / kanamycin B

substrate: kanamycin B


substrate_name: neomycin C

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / neomycin C; organism mapping Acinetobacter baumannii; kcat_over_km paper=7.59 s^-1 mM^-1; export=7.594936708860758 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.06 s^-1; km/S0.5=0.0079 mM; kcat_over_km=7.59 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / neomycin C; kcat 0.060 s^-1; S0.5 7.9 ± 1.0 μM (normalized km 0.0079 mM); kcat/S0.5 7.59 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.59 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ih / neomycin C

substrate: neomycin C


substrate_name: ribostamycin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / ribostamycin; organism mapping Acinetobacter baumannii; kcat paper=0.044 s^-1; export=0.04 s^-1; kcat_over_km paper=7.1 s^-1 mM^-1; export=6.451612903225807 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.044 s^-1; km/S0.5=0.0062 mM; kcat_over_km=7.1 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / ribostamycin; kcat 0.044 s^-1; S0.5 6.2 ± 1.5 μM (normalized km 0.0062 mM); kcat/S0.5 7.10 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.1 s^-1 mM^-1).

row_label: AAC(6′)-Ih / ribostamycin

substrate: ribostamycin


substrate_name: sisomicin

column_label: Table 1, AAC(6′)-Ih sisomicin row, exact Hill-equation cells kcat 0.051 s^-1; S0.5 10.5 ± 0.8 μM; kcat/S0.5 4.86 × 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat=0.051 s^(-1); S0.5=0.0105 mM in the current km slot; independently printed kcat/S0.5=4.86 s^(-1)*mM^(-1).

raw_value_unit_evidence: AAC(6′)-Ih / Acinetobacter baumannii / sisomicin source-bound cells: kcat 0.051 s^-1; S0.5 10.5 ± 0.8 μM; catalytic efficiency reported as kcat/S0.5 4.86 × 10^3 M^-1 s^-1.

row_label: AAC(6′)-Ih / sisomicin

table_label: Table 1. Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation.

substrate: sisomicin


substrate_name: tobramicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ih / tobramicin; organism mapping Acinetobacter baumannii; kcat_over_km paper=7.59 s^-1 mM^-1; export=7.586206896551724 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.022 s^-1; km/S0.5=0.0029 mM; kcat_over_km=7.59 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ih / tobramicin; kcat 0.022 s^-1; S0.5 2.9 ± 1.0 μM (normalized km 0.0029 mM); kcat/S0.5 7.59 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.59 s^-1 mM^-1).

row_label: AAC(6′)-Ih / tobramicin

substrate: tobramicin


organism: Serratia marcescens

substrate_name: acetyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: acetyl-CoA


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / AMK.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; AMK

table_label: Table 1, steady-state kinetic characterization of ANT(3\)-Ii/AAC(6')-IId"


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / GEN.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; GEN


substrate_name: kanamycin

substrate: kanamycin


substrate_name: neomycin

column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / NEO.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; NEO

substrate: neomycin


substrate_name: netilmicin

column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / NET.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; NET

substrate: netilmicin


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / RIB.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; RIB


column_label: Table 1 columns Activity, Substrate, Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); row matched by NHis6-tagged AAC(6')-IId / SIS.

row_label: NHis6-tagged AAC(6')-IId; acetyltransferase; SIS


substrate_name: tobramycin

substrate: tobramycin


enzyme_display_name: aminoglycoside N(3)-acetyltransferase

organism: Pseudomonas aeruginosa

substrate_name: kanamycin A

enzyme: aminoglycoside N(3)-acetyltransferase

substrate: kanamycin A


substrate_name: sisomycin

substrate: sisomycin


substrate_name: myristoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature K107E/K252E to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Lys107Glu/Lys252Glu'; column 'Km (uM)' = 51; column 'kcat (s-1)' = 1.33; column 'kcat/Km (s-1.M-1)' = 25,848; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.33 s^-1; already in s^-1, so no unit conversion applies; the exported value is 1.33 s^(-1). Km: printed Table 1 cell 51 uM; 51 / 1000 = 0.051 mM; the exported value is 0.051 mM. kcat/Km: printed Table 1 cell 25,848 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 25,848 / 1000 = 25.848 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Lys107Glu/Lys252Glu': Km = 51 uM; kcat = 1.33 s^-1; printed kcat/Km = 25,848 s^-1.M^-1.

table_label: Table 1: Catalytic parameters for HsNMT1 and related mutants using MyrCoA (Nature Communications 2020, 11:1132)

substrate: myristoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature V181A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Val181Ala'; column 'Km (uM)' = 20; column 'kcat (s-1)' = 0.36; column 'kcat/Km (s-1.M-1)' = 18,541; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.36 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.36 s^(-1). Km: printed Table 1 cell 20 uM; 20 / 1000 = 0.02 mM; the exported value is 0.02 mM. kcat/Km: printed Table 1 cell 18,541 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18,541 / 1000 = 18.541 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Val181Ala': Km = 20 uM; kcat = 0.36 s^-1; printed kcat/Km = 18,541 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Val181Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature V181L to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Val181Leu'; column 'Km (uM)' = 54; column 'kcat (s-1)' = 0.33; column 'kcat/Km (s-1.M-1)' = 6172; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.33 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.33 s^(-1). Km: printed Table 1 cell 54 uM; 54 / 1000 = 0.054 mM; the exported value is 0.054 mM. kcat/Km: printed Table 1 cell 6172 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6172 / 1000 = 6.172 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Val181Leu': Km = 54 uM; kcat = 0.33 s^-1; printed kcat/Km = 6172 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Val181Leu'


column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Wild-type'; column 'Km (uM)' = 18; column 'kcat (s-1)' = 0.41; column 'kcat/Km (s-1.M-1)' = 23,502; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.41 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.41 s^(-1). Km: printed Table 1 cell 18 uM; 18 / 1000 = 0.018 mM; the exported value is 0.018 mM. kcat/Km: printed Table 1 cell 23,502 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 23,502 / 1000 = 23.502 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Wild-type': Km = 18 uM; kcat = 0.41 s^-1; printed kcat/Km = 23,502 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Wild-type'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature Y180A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Tyr180Ala'; column 'Km (uM)' = 765; column 'kcat (s-1)' = 0.16; column 'kcat/Km (s-1.M-1)' = 206; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.16 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.16 s^(-1). Km: printed Table 1 cell 765 uM; 765 / 1000 = 0.765 mM; the exported value is 0.765 mM. kcat/Km: printed Table 1 cell 206 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 206 / 1000 = 0.206 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Tyr180Ala': Km = 765 uM; kcat = 0.16 s^-1; printed kcat/Km = 206 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Tyr180Ala'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature Y180F/N246A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Tyr180Phe/Asn246Ala'; column 'Km (uM)' = 33; column 'kcat (s-1)' = 0.68; column 'kcat/Km (s-1.M-1)' = 20,924; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.68 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.68 s^(-1). Km: printed Table 1 cell 33 uM; 33 / 1000 = 0.033 mM; the exported value is 0.033 mM. kcat/Km: printed Table 1 cell 20,924 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 20,924 / 1000 = 20.924 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Tyr180Phe/Asn246Ala': Km = 33 uM; kcat = 0.68 s^-1; printed kcat/Km = 20,924 s^-1.M^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P30419 and applied mutation signature Y192A to reconstruct the assayed variant sequence.

column_label: Table 1 (Catalytic parameters for HsNMT1 and related mutants using MyrCoA), HsNMT1 variant row 'Tyr192Ala'; column 'Km (uM)' = 187; column 'kcat (s-1)' = 0.93; column 'kcat/Km (s-1.M-1)' = 4960; column 'Relative kcat/Km' is a percentage of the wild-type efficiency and carries no unit.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.93 s^-1; already in s^-1, so no unit conversion applies; the exported value is 0.93 s^(-1). Km: printed Table 1 cell 187 uM; 187 / 1000 = 0.187 mM; the exported value is 0.187 mM. kcat/Km: printed Table 1 cell 4960 s^-1.M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4960 / 1000 = 4.96 s^-1 mM^-1, which is the value this record proposes for kcat_over_km.

raw_value_unit_evidence: Table 1, HsNMT1 variant row 'Tyr192Ala': Km = 187 uM; kcat = 0.93 s^-1; printed kcat/Km = 4960 s^-1.M^-1.

row_label: Table 1, HsNMT1 variant row 'Tyr192Ala'


organism: Acinetobacter haemolyticus

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

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / 2'-N-ethylnetilmicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=5.3 s^-1 mM^-1; export=5.300546448087432 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.097 s^-1; km/S0.5=0.0183 mM; kcat_over_km=5.3 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / 2'-N-ethylnetilmicin; kcat 0.097 s^-1; S0.5 18.3 ± 1.5 μM (normalized km 0.0183 mM); kcat/S0.5 5.30 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.3 s^-1 mM^-1).

row_label: AAC(6′)-Ig / 2'-N-ethylnetilmicin


substrate_name: amikacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / amikacin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=7.44 s^-1 mM^-1; export=7.437641723356009 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.328 s^-1; km/S0.5=0.0441 mM; kcat_over_km=7.44 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / amikacin; kcat 0.328 s^-1; S0.5 44.1 ± 5.6 μM (normalized km 0.0441 mM); kcat/S0.5 7.44 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.44 s^-1 mM^-1).

row_label: AAC(6′)-Ig / amikacin

substrate: amikacin


substrate_name: arbekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / arbekacin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=5.54 s^-1 mM^-1; export=5.539568345323741 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.077 s^-1; km/S0.5=0.0139 mM; kcat_over_km=5.54 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / arbekacin; kcat 0.077 s^-1; S0.5 13.9 ± 1.1 μM (normalized km 0.0139 mM); kcat/S0.5 5.54 x10^3 M^-1 s^-1 (normalized kcat_over_km 5.54 s^-1 mM^-1).

row_label: AAC(6′)-Ig / arbekacin

substrate: arbekacin


substrate_name: butirosin A

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / butirosin A; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=6.18 s^-1 mM^-1; export=6.184971098265896 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.107 s^-1; km/S0.5=0.0173 mM; kcat_over_km=6.18 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / butirosin A; kcat 0.107 s^-1; S0.5 17.3 ± 2.8 μM (normalized km 0.0173 mM); kcat/S0.5 6.18 x10^3 M^-1 s^-1 (normalized kcat_over_km 6.18 s^-1 mM^-1); note: kcat cell carries footnote f.

row_label: AAC(6′)-Ig / butirosin A

substrate: butirosin A


substrate_name: dibekacin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / dibekacin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=4.9 s^-1 mM^-1; export=4.903474903474904 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.127 s^-1; km/S0.5=0.0259 mM; kcat_over_km=4.9 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / dibekacin; kcat 0.127 s^-1; S0.5 25.9 ± 2.5 μM (normalized km 0.0259 mM); kcat/S0.5 4.90 x10^3 M^-1 s^-1 (normalized kcat_over_km 4.9 s^-1 mM^-1).

row_label: AAC(6′)-Ig / dibekacin

substrate: dibekacin


substrate_name: gentamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / gentamicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=3.13 s^-1 mM^-1; export=3.125 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.055 s^-1; km/S0.5=0.0176 mM; kcat_over_km=3.13 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / gentamicin; kcat 0.055 s^-1; S0.5 17.6 ± 2.7 μM (normalized km 0.0176 mM); kcat/S0.5 3.13 x10^3 M^-1 s^-1 (normalized kcat_over_km 3.13 s^-1 mM^-1); note: substrate row label carries footnote d.

row_label: AAC(6′)-Ig / gentamicin

substrate: gentamicin


substrate_name: isepamicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / isepamicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=7.49 s^-1 mM^-1; export=7.490384615384616 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.779 s^-1; km/S0.5=0.104 mM; kcat_over_km=7.49 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / isepamicin; kcat 0.779 s^-1; S0.5 104 ± 15 μM (normalized km 0.104 mM); kcat/S0.5 7.49 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.49 s^-1 mM^-1).

row_label: AAC(6′)-Ig / isepamicin

substrate: isepamicin


substrate_name: kanamycin B

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / kanamycin B; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=6.24 s^-1 mM^-1; export=6.241379310344827 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.181 s^-1; km/S0.5=0.029 mM; kcat_over_km=6.24 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / kanamycin B; kcat 0.181 s^-1; S0.5 29.0 ± 3.4 μM (normalized km 0.029 mM); kcat/S0.5 6.24 x10^3 M^-1 s^-1 (normalized kcat_over_km 6.24 s^-1 mM^-1).

row_label: AAC(6′)-Ig / kanamycin B

substrate: kanamycin B


substrate_name: neomycin C

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / neomycin C; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=7.7 s^-1 mM^-1; export=7.702702702702703 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.057 s^-1; km/S0.5=0.0074 mM; kcat_over_km=7.7 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / neomycin C; kcat 0.057 s^-1; S0.5 7.4 ± 0.5 μM (normalized km 0.0074 mM); kcat/S0.5 7.70 x10^3 M^-1 s^-1 (normalized kcat_over_km 7.7 s^-1 mM^-1).

row_label: AAC(6′)-Ig / neomycin C

substrate: neomycin C


substrate_name: ribostamycin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / ribostamycin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=6.1 s^-1 mM^-1; export=6.101694915254237 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.072 s^-1; km/S0.5=0.0118 mM; kcat_over_km=6.1 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / ribostamycin; kcat 0.072 s^-1; S0.5 11.8 ± 1.7 μM (normalized km 0.0118 mM); kcat/S0.5 6.10 x10^3 M^-1 s^-1 (normalized kcat_over_km 6.1 s^-1 mM^-1).

row_label: AAC(6′)-Ig / ribostamycin

substrate: ribostamycin


substrate_name: sisomicin

column_label: Table 1, AAC(6′)-Ig sisomicin row, exact Hill-equation cells kcat 0.130 s^-1; S0.5 16.8 ± 2.0 μM; kcat/S0.5 7.74 × 10^3 M^-1 s^-1.

normalized_value_unit_evidence: kcat=0.130 s^(-1); S0.5=0.0168 mM in the current km slot; independently printed kcat/S0.5=7.74 s^(-1)*mM^(-1).

raw_value_unit_evidence: AAC(6′)-Ig / Acinetobacter haemolyticus / sisomicin source-bound cells: kcat 0.130 s^-1; S0.5 16.8 ± 2.0 μM; catalytic efficiency reported as kcat/S0.5 7.74 × 10^3 M^-1 s^-1.

row_label: AAC(6′)-Ig / sisomicin

substrate: sisomicin


substrate_name: tobramicin

column_label: ACS Infectious Diseases 2016 Table 1, Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row label AAC(6′)-Ig / tobramicin; organism mapping Acinetobacter haemolyticus; kcat_over_km paper=3.86 s^-1 mM^-1; export=3.863636363636364 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.085 s^-1; km/S0.5=0.022 mM; kcat_over_km=3.86 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic Parameters and MIC Values of AAC(6′)-Ig and AAC(6′)-Ih for Aminoglycoside Acetylation; row AAC(6′)-Ig / tobramicin; kcat 0.085 s^-1; S0.5 22.0 ± 2.9 μM (normalized km 0.022 mM); kcat/S0.5 3.86 x10^3 M^-1 s^-1 (normalized kcat_over_km 3.86 s^-1 mM^-1).

row_label: AAC(6′)-Ig / tobramicin

substrate: tobramicin


organism: Fragaria x ananassa

substrate_name: methanol

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Methanol; columns Km (mM), Kcat, Kcat/Km; cells 4.05, 18.5, 4.5

row_label: Methanol

substrate: methanol


substrate_name: octanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Octanol; columns Km (mM), Kcat, Kcat/Km; cells 2.23, 466, 208

row_label: Octanol

substrate: octanol


substrate_name: pentanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Pentanol; columns Km (mM), Kcat, Kcat/Km; cells 5.78, 407, 71

raw_value_unit_evidence: Pentanol: Km=5.78 mM; kcat=407 s^-1; kcat/Km=71 s^-1 mM^-1

row_label: Pentanol

substrate: pentanol


substrate_name: propanol

column_label: Table 4. Kinetic parameters of semi-purified recombinant FaAAT2 for different alcohols at variable concentrations in combination with acetyl-CoA; row Propanol; columns Km (mM), Kcat, Kcat/Km; cells 2.4, 17.5, 7.2

raw_value_unit_evidence: Propanol: Km=2.4 mM; kcat=17.5 s^-1; kcat/Km=7.2 s^-1 mM^-1

row_label: Propanol

substrate: propanol


enzyme_display_name: deacetylvindoline O-acetyltransferase

organism: Catharanthus roseus

substrate_name: vindoline

enzyme: deacetylvindoline O-acetyltransferase

substrate: vindoline


organism: Methylorubrum extorquens

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

column_label: Abstract/prose reports apparent Km for H4MPT = 30 uM.

raw_value_unit_evidence: 30 uM

table_label: Abstract/prose apparent Km values


substrate_name: formylmethanofuran

column_label: Abstract/prose reports apparent Km for formylMFR = 50 uM.

raw_value_unit_evidence: 50 uM

row_label: formylMFR

substrate: formylmethanofuran


enzyme_display_name: Alcohol O-acetyltransferase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: butyryl-CoA (for thioesterase activity)

assay_conditions_summary: buffer in vitro; cofactor CoA

column_label: Main text states KM was 25+/-1 uM for butyryl-CoA; Supplementary Table 1 row Butyryl reports KM 25+/-1 under wild-type Atf1p.

raw_value_unit_evidence: KM 25+/-1 uM for butyryl-CoA; supplement row Butyryl under Atf1p wild-type

row_label: Atf1p wild-type; Butyryl

table_label: Supplementary Table 1. Kinetic data from coupled enzyme assays; main text Biochemical assays of Atf1p.

enzyme: Alcohol O-acetyltransferase 1

substrate: butyryl-CoA (for thioesterase activity)


substrate_name: hexanoyl-CoA (for thioesterase activity)

column_label: Main text states KM was 12+/-3 uM for hexanoyl-CoA; Supplementary Table 1 row Hexanoyl reports KM 12+/-3 under wild-type Atf1p.

raw_value_unit_evidence: KM 12+/-3 uM for hexanoyl-CoA; supplement row Hexanoyl under Atf1p wild-type

row_label: Atf1p wild-type; Hexanoyl


substrate_name: octanoyl-CoA (for thioesterase activity)

column_label: Main text states KM was 3+/-1 uM for octanoyl-CoA; Supplementary Table 1 row Octanoyl reports KM 3+/-1 under wild-type Atf1p.

raw_value_unit_evidence: KM 3+/-1 uM for octanoyl-CoA; supplement row Octanoyl under Atf1p wild-type

row_label: Atf1p wild-type; Octanoyl


organism: Rattus norvegicus

substrate_name: S-acetyl-CoA

column_label: Primary PDF page 520 Properties prose gives S-Acetyl coenzyme A apparent Km 26 uM; converted to 0.026 mM.

normalized_value_unit_evidence: apparent Km 0.026 mM

raw_value_unit_evidence: Page 520 prose: S-Acetyl coenzyme A serves as acetyl donor with an apparent Km of 26 uM (Vm = 420 nmol min^-1) in an otherwise standard assay system

table_label: ScienceDirect PDF page 520 Properties prose

substrate: S-acetyl-CoA


substrate_name: S-butyl-L-cysteine

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

column_label: Primary PDF page 519 Table II row S-Butyl-L-cysteine has Ks (uM) value 63; converted to 0.063 mM.

normalized_value_unit_evidence: apparent Km/Ks 0.063 mM

raw_value_unit_evidence: Table II row S-Butyl-L-cysteine, column Ks (uM): 63; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Butyl-L-cysteine

table_label: ScienceDirect PDF page 519 Table II, Substrate Specificity of Cysteine S-Conjugate N-Acetyltransferase

substrate: S-butyl-L-cysteine


substrate_name: S-Benzyl-L-cysteine

column_label: Primary PDF page 519 Table II row S-Benzyl-L-cysteine has Ks (uM) value 140; converted to 0.14 mM.

normalized_value_unit_evidence: apparent Km/Ks 0.14 mM

raw_value_unit_evidence: Table II row S-Benzyl-L-cysteine, column Ks (uM): 140; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: S-propyl-L-cysteine

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

column_label: Primary PDF page 519 Table II row S-Propyl-L-cysteine has Ks (uM) value 670; converted to 0.67 mM.

normalized_value_unit_evidence: apparent Km/Ks 0.67 mM

raw_value_unit_evidence: Table II row S-Propyl-L-cysteine, column Ks (uM): 670; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Propyl-L-cysteine

substrate: S-propyl-L-cysteine


substrate_name: O-benzyl-L-serine

column_label: Primary PDF page 519 Table II row O-benzyl-L-serine has Ks (uM) value 2600; converted to 2.6 mM.

normalized_value_unit_evidence: apparent Km/Ks 2.6 mM

raw_value_unit_evidence: Table II row O-benzyl-L-serine, column Ks (uM): 2600; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: O-benzyl-L-serine

substrate: O-benzyl-L-serine


substrate_name: S-ethyl-L-cysteine

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

column_label: Primary PDF page 519 Table II row S-Ethyl-L-cysteine has Ks (uM) value 7100; converted to 7.1 mM.

normalized_value_unit_evidence: apparent Km/Ks 7.1 mM

raw_value_unit_evidence: Table II row S-Ethyl-L-cysteine, column Ks (uM): 7100; footnote c defines apparent Km and Vm at 0.8 mM CoASAc under standard assay conditions

row_label: S-Ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: N-formylmethanofuran

column_label: The abstract reports Km for CHO-MFR was 50 microM at the optimal salt concentration and 65 degrees C.

raw_value_unit_evidence: Km raw_value=50 microM raw_unit=microM

row_label: Prose segment: CHO-MFR Km

table_label: PubMed PMID 1483480 abstract

substrate: N-formylmethanofuran


column_label: The abstract reports Km for H4MPT was 100 microM at the optimal salt concentration and 65 degrees C.

raw_value_unit_evidence: Km raw_value=100 microM raw_unit=microM

row_label: Prose segment: H4MPT Km


substrate_name: N-furfurylformamide

verification_status: disputed

substrate: N-furfurylformamide

status: disputed


organism: Raphanus sativus

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


organism: Corynebacterium striatum

substrate_name: acetyl-CoA

assay_conditions_summary: pH 6; 310.15 K; cofactor CoA

substrate: acetyl-CoA


substrate_name: dibekacin

substrate: dibekacin


substrate_name: kanamycin B

substrate: kanamycin B