enzyme_display_name: Dehydrodolichyl diphosphate synthase complex subunit NUS1

column_label: Table 1 WT hcis-PT row lists Km IPP [uM]=11.1 (+/-1.3); converted to 0.0111 mM.

raw_value_unit_evidence: Km raw_value=11.1 (+/-1.3) raw_unit=uM for isopentenyl diphosphate

row_label: hcis-PT, WT

table_label: Table 1: Kinetic properties of purified hcis-PT and mutants


organism: Homo sapiens

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

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

column_label: Table 1 WT hcis-PT row lists Km FPP [uM]=0.68 (+/-0.14); converted to 0.00068 mM.

raw_value_unit_evidence: Km raw_value=0.68 (+/-0.14) raw_unit=uM for (2E,6E)-farnesyl diphosphate

data_origin: experimental

enzyme: Dehydrodolichyl diphosphate synthase complex subunit NUS1

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

status: verified

source: uniprot


enzyme_display_name: Dehydrodolichyl diphosphate synthase complex subunit DHDDS

substrate_name: isopentenyl diphosphate

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

substrate: isopentenyl diphosphate


enzyme: Dehydrodolichyl diphosphate synthase complex subunit DHDDS


enzyme_display_name: UniProt Q8N5Z0

substrate_name: oxaloacetate

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt Q8N5Z0

substrate: oxaloacetate

source: skid


substrate_name: pyruvate

substrate: pyruvate


substrate_name: hydroxyphenylpyruvate

substrate: hydroxyphenylpyruvate


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


km_display: Not reported


smiles: CCCCC(=O)C(=O)[O-]


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


substrate_name: glyoxylate

substrate: glyoxylate


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


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


substrate_name: Mercaptopyruvate

substrate: Mercaptopyruvate


enzyme_display_name: UniProt Q16773

enzyme: UniProt Q16773


substrate_name: L-kynurenine

substrate: L-kynurenine


substrate_name: L-cysteine

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

substrate: L-cysteine


enzyme_display_name: ornithine aminotransferase

organism: Aspergillus nidulans

source_db: brenda

enzyme: ornithine aminotransferase

source: brenda


substrate_name: L-ornithine

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

substrate: L-ornithine


enzyme_display_name: UniProt P04181

proof_lines:
Raw SKiD Env: Temp=15°C, pH=8
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P04181


enzyme_display_name: UniProt S8EY38

organism: Toxoplasma gondii

enzyme: UniProt S8EY38


substrate_name: acetylornithine

substrate: acetylornithine


enzyme_display_name: Geranylfarnesyl diphosphate synthase, chloroplastic

organism: Leucosceptrum canum

substrate_name: dimethylallyl diphosphate (in the presence of isopentenyl diphosphate)

verification_status: unverified

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

proof_lines: kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl

status: unverified


substrate_name: geranyl diphosphate (in the presence of isopentenyl diphosphate)

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

enzyme: Geranylfarnesyl diphosphate synthase, chloroplastic


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


enzyme_display_name: 4-hydroxybenzoate geranyltransferase

organism: Lithospermum erythrorhizon

substrate_name: geranyl diphosphate

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

enzyme: 4-hydroxybenzoate geranyltransferase

substrate: geranyl diphosphate


enzyme_display_name: Solanesyl diphosphate synthase 1, chloroplastic

organism: Arabidopsis thaliana

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

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


substrate_name: geranylgeranyl diphosphate (in the presence of 100 uM of isopentenyl diphosphate)

enzyme: Solanesyl diphosphate synthase 1, chloroplastic


substrate_name: isopentenyl diphosphate (in the presence of 20 uM of farnesyl diphosphate)


enzyme_display_name: flaviolin linalyltransferase

organism: Streptomyces virginiae

substrate_name: flaviolin

sequence_source: multiple

proof_lines: kcat is 0.013 min(-1) for flaviolin. kcat is 0.14 min(-1) for 4-hydroxybenzoate.

source_databases_merged: brenda uniprot

enzyme: flaviolin linalyltransferase

substrate: flaviolin


column_label: Primary prose labels GPP Km 2.1 uM under the flaviolin condition.

raw_value_unit_evidence: GPP Km 2.1 uM using flaviolin 0.25 mM

row_label: GPP with flaviolin as aromatic substrate

table_label: Section 3.4 Biochemical properties of Fnq26


organism: Streptomyces anulatus

substrate_name: dimethylallyl diphosphate

column_label: PubMed abstract prose, metric label Km, substrate dimethylallyl diphosphate, raw value 116 uM.

normalized_value_unit_evidence: 116 uM = 0.116 mM, matching the expected export Km 0.116 mM.

raw_value_unit_evidence: PubMed abstract reports the Km value for dimethylallyl diphosphate as 116 uM.

row_label: PpzP / dimethylallyl diphosphate

table_label: PubMed abstract prose for PMID 19339241

substrate: dimethylallyl diphosphate


enzyme_display_name: UniProt Q84II6

organism: Janthinobacterium sp. J3

enzyme: UniProt Q84II6


enzyme_display_name: UniProt Q8RTL4

organism: Comamonas sp.

substrate_name: nitrobenzene

enzyme: UniProt Q8RTL4

substrate: nitrobenzene


enzyme_display_name: 2,4-dinitrotoluene dioxygenase

organism: Burkholderia sp.

smiles: O=O

enzyme: 2,4-dinitrotoluene dioxygenase


enzyme_display_name: UniProt Q71RI9

organism: Mus musculus

substrate_name: L-glutamine

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

enzyme: UniProt Q71RI9

substrate: L-glutamine


enzyme_display_name: UniProt P17169

organism: Escherichia coli

substrate_name: D-fructose 6-phosphate

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.2
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=37°C, pH=7.5

enzyme: UniProt P17169

substrate: D-fructose 6-phosphate


substrate_name: L-gamma-glutamyl-p-nitroanilide

substrate: L-gamma-glutamyl-p-nitroanilide


enzyme_display_name: UniProt P80147

organism: Sus scrofa

substrate_name: (R,S)-4-amino-3-fluorobutanoic acid

smiles: C(C(CN)F)C(=O)O

enzyme: UniProt P80147

substrate: (R,S)-4-amino-3-fluorobutanoic acid


substrate_name: gamma-aminobutanoic acid

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

substrate: gamma-aminobutanoic acid


substrate_name: L-Aspartate

source_db: oed

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

substrate: L-Aspartate

source: oed


enzyme_display_name: 4-aminobutyrate transaminase

substrate_name: 4-Aminobutanoate; 2-Oxoglutarate

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

enzyme: 4-aminobutyrate transaminase

substrate: 4-Aminobutanoate; 2-Oxoglutarate


smiles: NCCCC(=O)O


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

mutation_type: substitution


organism: Malus domestica


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E211S to reconstruct the assayed variant sequence.

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


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I50Q/G295Y to reconstruct the assayed variant sequence.

column_label: Table 2; row I50Q/G295Y; columns kcat, kcat/KGABA, and KGABA; raw kcat=0.028 +/- 0.001 s^-1, kcat/KGABA=5.9 +/- 0.3 M^-1 s^-1, KGABA=4.7 +/- 0.2 mM; normalized kcat=0.028 s^-1, Km=4.7 mM, kcat/Km=0.0059 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=0.028 s^-1; Km=4.7 mM; kcat/Km=0.0059 s^-1*mM^-1 from printed kcat/KGABA

row_label: I50Q/G295Y / GABA (4-aminobutanoate)

table_label: Table 2. GABA/R-ketoglutarate transamination analysis of wild-type GABA-AT and its mutants

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V241A to reconstruct the assayed variant sequence.

column_label: Table 2; row V241A; columns kcat, kcat/KGABA, and KGABA; raw kcat=1.93 +/- 0.08 s^-1, kcat/KGABA=64 +/- 6 M^-1 s^-1, KGABA=30 +/- 2 mM; normalized kcat=1.93 s^-1, Km=30.0 mM, kcat/Km=0.064 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=1.93 s^-1; Km=30.0 mM; kcat/Km=0.064 s^-1*mM^-1 from printed kcat/KGABA

row_label: V241A / GABA (4-aminobutanoate)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E211S/I50H/V80T to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat=0.106 s^-1; Km=146.0 mM; kcat/Km=0.00073 s^-1*mM^-1 from printed kcat/KGABA

row_label: E211S/I50H/V80T / GABA (4-aminobutanoate)


column_label: Table 2; row wild type; columns kcat, kcat/KGABA, and KGABA; raw kcat=47.4 +/- 1.0 s^-1, kcat/KGABA=8172 +/- 590 M^-1 s^-1, KGABA=5.8 +/- 0.4 mM; normalized kcat=47.4 s^-1, Km=5.8 mM, kcat/Km=8.172 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=47.4 s^-1; Km=5.8 mM; kcat/Km=8.172 s^-1*mM^-1 from printed kcat/KGABA

row_label: wild type / GABA (4-aminobutanoate)


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: glyoxylate

smiles: O=CC(=O)O

substrate: glyoxylate


organism: Rattus norvegicus

substrate_name: L-Glutamine; D-Fructose 6-phosphate

substrate: L-Glutamine; D-Fructose 6-phosphate


organism: Corynebacterium glutamicum


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P22256 and applied mutation signature V241A to reconstruct the assayed variant sequence.

column_label: Table 2, enzyme row 'V241A'; column 'kcat (s-1)' = 1.93; column 'KKG (mM)' = 0.13; the row's remaining cells are column 'kcat/KGABA (M-1 s-1)' = 64 and column 'KGABA (mM)' = 30, and the 'KiKG (mM)' column prints no cell for this row; Table 2 carries no kcat/KKG column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.93 s-1; already in s^-1, no unit conversion applies; the paper value is 1.93 s^(-1). Km: printed Table 2 KKG cell 0.13 mM; already in mM, no unit conversion applies; the paper value is 0.13 mM. kcat/Km: Table 2's only efficiency column is kcat/KGABA, so the paper value 14.846153846153845 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.93 / 0.13 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'V241A': kcat = 1.93 s-1; KKG = 0.13 mM; Table 2 prints no kcat/KKG cell for this row.

row_label: Table 2, enzyme row 'V241A'

table_label: Table 2: GABA/R-Ketoglutarate Transamination Analysis of Wild-Type GABA-AT and Its Mutants (Biochemistry 2005, 44(8):2982-2992)


substrate_name: 2-Oxoglutarate; 4-Aminobutanoate

substrate: 2-Oxoglutarate; 4-Aminobutanoate


column_label: Table 2, enzyme row 'wild type'; column 'kcat (s-1)' = 47.4; column 'KKG (mM)' = 1.07; the row's remaining cells are column 'kcat/KGABA (M-1 s-1)' = 8172, column 'KGABA (mM)' = 5.8 and column 'KiKG (mM)' = 10.2; Table 2 carries no kcat/KKG column.

normalized_value_unit_evidence: kcat: printed Table 2 cell 47.4 s-1; already in s^-1, no unit conversion applies; the paper value is 47.4 s^(-1). Km: printed Table 2 KKG cell 1.07 mM; already in mM, no unit conversion applies; the paper value is 1.07 mM. kcat/Km: Table 2's only efficiency column is kcat/KGABA, so the paper value 44.299065420560744 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 47.4 / 1.07 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, enzyme row 'wild type': kcat = 47.4 s-1; KKG = 1.07 mM; Table 2 prints no kcat/KKG cell for this row.

row_label: Table 2, enzyme row 'wild type'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I50Q to reconstruct the assayed variant sequence.

column_label: Table 2; row I50Q; columns kcat, kcat/KGABA, and KGABA; raw kcat=13.5 +/- 0.3 s^-1, kcat/KGABA=199 +/- 18 M^-1 s^-1, KGABA=68 +/- 6 mM; normalized kcat=13.5 s^-1, Km=68.0 mM, kcat/Km=0.199 s^-1*mM^-1.

normalized_value_unit_evidence: kcat=13.5 s^-1; Km=68.0 mM; kcat/Km=0.199 s^-1*mM^-1 from printed kcat/KGABA

row_label: I50Q / GABA (4-aminobutanoate)


enzyme_display_name: nitroarene dioxygenase

organism: Acidovorax sp.

enzyme: nitroarene dioxygenase


enzyme_display_name: glutamine---pyruvate transaminase

substrate_name: L-Glutamine; Glyoxylate

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

enzyme: glutamine---pyruvate transaminase

substrate: L-Glutamine; Glyoxylate


enzyme_display_name: glutamine-pyruvate transaminase

substrate_name: L-methionine

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

enzyme: glutamine-pyruvate transaminase

substrate: L-methionine


substrate_name: L-methionine (SR)-sulfoxide

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

substrate: L-methionine (SR)-sulfoxide


smiles: CSCCC(=O)C(=O)[O-]


organism: Pseudomonas aeruginosa


substrate_name: putrescine

smiles: C(CCN)CN

substrate: putrescine


substrate_name: L-ornithine

substrate: L-ornithine


proof_lines: with glyoxylate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C

proof_lines: with pyruvate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C


proof_lines: in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C


proof_lines: with L-alanine as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C


substrate_name: L-alanine

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

proof_lines: with 4-oxobutanoate as cosubstrate, in 50 mM TABS (pH 9), 1.5 mM dithiothreitol, 0.625 mM EDTA, 0.1 mM pyridoxal 5'-phosphate, 10% (v/v) glycerol, at 30°C

substrate: L-alanine


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Nicotiana tabacum


enzyme_display_name: carbazole 1,9a-dioxygenase

enzyme: carbazole 1,9a-dioxygenase


organism: Schistocerca gregaria


enzyme_display_name: D-amino-acid transaminase

organism: Bradyrhizobium japonicum

enzyme: D-amino-acid transaminase


substrate_name: D-alanine

substrate: D-alanine


organism: Lathyrus oleraceus


substrate_name: Naphthalene

substrate: Naphthalene


enzyme_display_name: steroid 9alpha-monooxygenase

organism: Mycolicibacterium fortuitum

substrate_name: NADH

assay_conditions_summary: cofactor NADH

enzyme: steroid 9alpha-monooxygenase

substrate: NADH


enzyme_display_name: salicylate 1-monooxygenase

organism: Solanum lycopersicum

substrate_name: salicylate

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

enzyme: salicylate 1-monooxygenase

substrate: salicylate


substrate_name: L-glutamine

substrate: L-glutamine


enzyme_display_name: beta-alanine-pyruvate transaminase

organism: Bacillus cereus

substrate_name: beta-Alanine

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

enzyme: beta-alanine-pyruvate transaminase

substrate: beta-Alanine


organism: Mycolicibacterium smegmatis


organism: Streptomyces sp.

column_label: Table 1. Steady-state kinetic parameters of Fur7; row 1,3-DHN / GPP; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.00013 normalized_unit=s^-1; Km normalized_value=0.32 normalized_unit=mM; kcat/Km normalized_value=0.00040625 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.13 +/- 0.05 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.32 +/- 0.02 raw_unit=mM; kcat/Km raw_value=0.41 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.00013/0.32 raw_unit=s^-1*mM^-1

row_label: 1,3-DHN / GPP


column_label: Table 1. Steady-state kinetic parameters of Fur7; row compound 4 (2-methoxy-3-methylflaviolin) / GPP; Table 1 first row printed as Fur-P1; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.00066 normalized_unit=s^-1; Km normalized_value=0.054 normalized_unit=mM; kcat/Km normalized_value=0.0122222222222222 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.66 +/- 0.02 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.054 +/- 0.005 raw_unit=mM; kcat/Km raw_value=12 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.00066/0.054 raw_unit=s^-1*mM^-1


substrate_name: flaviolin

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / GPP; column(s) kcat x 10^3; Aromatic substrate Km; kcat/Km computed from exact table kcat and Km cells plus rounded M^-1 s^-1 table value

normalized_value_unit_evidence: kcat normalized_value=0.028 normalized_unit=s^-1; Km normalized_value=0.048 normalized_unit=mM; kcat/Km normalized_value=0.583333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=28 +/- 3 in kcat x 10^3 s^-1 raw_unit=s^-1; Km raw_value=0.048 +/- 0.002 raw_unit=mM; kcat/Km raw_value=580 M^-1 s^-1 raw_unit=s^-1*mM^-1; kcat/Km computed_from_table_kcat_km=0.028/0.048 raw_unit=s^-1*mM^-1

row_label: Flaviolin 1 / GPP

substrate: flaviolin


substrate_name: geranyl diphosphate

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / GPP; column(s) Prenyl donor Km for GPP

raw_value_unit_evidence: Km raw_value=0.059 +/- 0.010 raw_unit=mM

substrate: geranyl diphosphate


substrate_name: dimethylallyl diphosphate

column_label: Table 1. Steady-state kinetic parameters of Fur7; row Flaviolin 1 / DMAPP; column(s) Prenyl donor Km for DMAPP

raw_value_unit_evidence: Km raw_value=0.72 +/- 0.06 raw_unit=mM

row_label: Flaviolin 1 / DMAPP

substrate: dimethylallyl diphosphate


organism: Bacillus sp. (in: firmicutes)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Y31A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; cofactor NADH

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row Y31A, kcat column, value 0.5 s^-1.

raw_value_unit_evidence: Table 1 row Y31A, column kcat: 0.5 s^-1.

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E32A to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32A, kcat column, value 1.3 s^-1.

raw_value_unit_evidence: Table 2 row E32A, column kcat: 1.3 s^-1.

table_label: Table 2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E32Q to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32Q, kcat column, value 13.4 s^-1.

raw_value_unit_evidence: Table 2 row E32Q, column kcat: 13.4 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K35A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row K35A, kcat column, value 84.3 s^-1.

raw_value_unit_evidence: Table 1 row K35A, column kcat: 84.3 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E32D to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32D, kcat column 85.6 s^-1, Km D-alanine column 1.2 mM, kcat/Km D-alanine column 6.8 x 10^4 M^-1 s^-1.

raw_value_unit_evidence: Table 2 row E32D: kcat 85.6 s^-1; Km D-alanine 1.2 mM; kcat/Km D-alanine 6.8 x 10^4 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V33A to reconstruct the assayed variant sequence.

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row V33A, kcat column, value 145.1 s^-1.

raw_value_unit_evidence: Table 1 row V33A, column kcat: 145.1 s^-1.


column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32Q, Km alpha-KG column, value 1.4 mM.

normalized_value_unit_evidence: km=1.4 mM

raw_value_unit_evidence: Table 2 row E32Q, column Km alpha-KG: 1.4 mM.


column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32A, Km alpha-KG column, value 1.8 mM.

normalized_value_unit_evidence: km=1.8 mM

raw_value_unit_evidence: Table 2 row E32A, column Km alpha-KG: 1.8 mM.


column_label: PMID 8977094 PDF text lines 145-153; Table 2 row E32D, Km alpha-KG column, value 2.1 mM.

normalized_value_unit_evidence: km=2.1 mM

raw_value_unit_evidence: Table 2 row E32D, column Km alpha-KG: 2.1 mM.


column_label: PMID 8977094 PDF text lines 141-153; Table 1 row Y31A, Km alpha-ketoglutarate column, value 10.1 mM.

raw_value_unit_evidence: Table 1 row Y31A, column Km alpha-ketoglutarate: 10.1 mM.


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

column_label: PMID 8977094 PDF text lines 141-153; Table 1 row V33A, Km alpha-ketoisovalerate column, value 15.5 mM.

raw_value_unit_evidence: Table 1 row V33A, column Km alpha-ketoisovalerate: 15.5 mM.


column_label: PMID 8977094 PDF text lines 141-153; Table 1 row K35A, Km alpha-ketoisovalerate column, value 32.2 mM.

raw_value_unit_evidence: Table 1 row K35A, column Km alpha-ketoisovalerate: 32.2 mM.


column_label: PMID 8977094 PDF text lines 141-153; Table 1 row K35A, Km alpha-ketoglutarate column, value 35.6 mM.

raw_value_unit_evidence: Table 1 row K35A, column Km alpha-ketoglutarate: 35.6 mM.


enzyme_display_name: Nonaprenyl diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP

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

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

enzyme: Nonaprenyl diphosphate synthase

substrate: IPP


substrate_name: GPP

smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

assay_conditions_summary: pH 7; buffer 50 mM sodium phosphate pH 7

column_label: Table 1 row Rv0562; GPP KM column; value 2.3 +/- 0.8 uM.

normalized_value_unit_evidence: 2.3 uM normalizes to 0.0023 mM.

raw_value_unit_evidence: Table 1 row Rv0562 reports GPP KM 2.3 +/- 0.8 uM.

row_label: Rv0562 / GPP

table_label: Table 1: Kinetic analysis of confirmed GGPP synthases

substrate: GPP


substrate_name: FPP

column_label: Table 1 row Rv0562; FPP KM column; value 11 +/- 3 uM.

normalized_value_unit_evidence: 11 uM normalizes to 0.011 mM.

raw_value_unit_evidence: Table 1 row Rv0562 reports FPP KM 11 +/- 3 uM.

row_label: Rv0562 / FPP

substrate: FPP


substrate_name: DMAPP

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

column_label: Table 1 row Rv0562; DMAPP KM column; value 5 +/- 2 uM.

normalized_value_unit_evidence: 5 uM normalizes to 0.005 mM.

raw_value_unit_evidence: Table 1 row Rv0562 reports DMAPP KM 5 +/- 2 uM.

row_label: Rv0562 / DMAPP

substrate: DMAPP


enzyme_display_name: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

organism: Arabidopsis thaliana

substrate_name: geranylgeranyl diphosphate

assay_conditions_summary: pH 8

column_label: Table 2 columns Enzyme, Substrate, Counter-substrate, Km list At-SPS2 / GGPP / 100 microM IPP / 0.565 +/- 0.178.

normalized_value_unit_evidence: Paper-normalized metrics: Km 0.000565 mM.

raw_value_unit_evidence: Table 2 row At-SPS2 GGPP: Km 0.565 +/- 0.178 microM; kcat not determined.

row_label: At-SPS2 / GGPP / 100 microM IPP

table_label: Table 2. Kinetic Parameters of At-SPS2 and At-SPS2-delta

substrate: geranylgeranyl diphosphate


substrate_name: farnesyl diphosphate

column_label: Table 2 columns Enzyme, Substrate, Counter-substrate, Km list At-SPS2 / FPP / 500 microM IPP / 5.12 +/- 0.57.

normalized_value_unit_evidence: Paper-normalized metrics: Km 0.00512 mM.

raw_value_unit_evidence: Table 2 row At-SPS2 FPP: Km 5.12 +/- 0.57 microM; kcat not determined.

row_label: At-SPS2 / FPP / 500 microM IPP

enzyme: all-trans-nonaprenyl diphosphate synthase [geranylgeranyl-diphosphate specific]

substrate: farnesyl diphosphate


substrate_name: isopentenyl diphosphate

proof_lines: pH 8.0, 30°C, cosubstrate: geranylgeranyl diphosphate, His6-tagged At-SPS2 fusion protein

proof_lines: pH 8.0, 30°C, cosubstrate: farnesyl diphosphate, His6-tagged At-SPS2 fusion protein

proof_lines: kcat is 3.77 sec(-1) with farnesyl diphosphate as substrate (in the presence of 500 uM of isopentenyl diphosphate). kcat is 2.33 sec(-1) with geranylgeranyl diphosphate as substrate (in the presence of 100 uM of isopentenyl diphosphate). kc

substrate: isopentenyl diphosphate


organism: Metapseudomonas resinovorans

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: CarAd activity, electron acceptor 2,6-dichlorophenolindophenol, pH 7.5, 30°C


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

organism: Homo sapiens

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

proof_lines: 3.6 kcat is sec(-1) with L-glutamine as substrate (PubMed:32019926, PubMed:35229715). 1.7 kcat is sec(-1) with D-fructose 6-phosphate as substrate (PubMed:32019926, PubMed:35229715).


substrate_name: D-fructose 6-phosphate

enzyme: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 1

substrate: D-fructose 6-phosphate


enzyme_display_name: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2

proof_lines: 3.7 kcat is sec(-1) with L-glutamine as substrate (PubMed:35229715). 1.8 kcat is sec(-1) with D-fructose 6-phosphate as substrate (PubMed:35229715).


enzyme: Glutamine--fructose-6-phosphate aminotransferase [isomerizing] 2


organism: Pseudomonas sp.

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


enzyme_display_name: Polyamine aminopropyltransferase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: agmatine (at pH 9 and 37 degrees Celsius)

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

smiles: C(CCN=C(N)N)CN

assay_conditions_summary: pH 9

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de

enzyme: Polyamine aminopropyltransferase


enzyme_display_name: Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase

substrate_name: D-alanine

column_label: PMC Supplementary Figure 1 caption reports pyruvate-formation kinetic parameters with KM = 7.3 +/- 1.06 mM.

raw_value_unit_evidence: Km raw_value=7.3 +/- 1.06 raw_unit=mM for pyruvate formation from the D-Ala-side DAAT assay

row_label: Supplementary Figure 1 panel B pyruvate formation / Rv0812 DAAT activity

table_label: PMID 33950161 PMC Supplementary Figure 1 caption

substrate: D-alanine


substrate_name: D-glutamate

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

column_label: PMC Supplementary Figure 1 caption reports D-Glu consumption kinetic parameters with KM = 0.24 +/- 0.05 mM.

raw_value_unit_evidence: Km raw_value=0.24 +/- 0.05 raw_unit=mM for D-Glu consumption

row_label: Supplementary Figure 1 panel C D-Glu consumption / Rv0812 DAAT activity

enzyme: Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase

substrate: D-glutamate


enzyme_display_name: Fluorinase

organism: Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1)

substrate_name: S-adenosyl-L-methionine

enzyme: Fluorinase

substrate: S-adenosyl-L-methionine


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase

organism: Solanum habrochaites

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

proof_lines: pH 7.8, 30°C, 0.035 mM isopentenyl diphosphate

proof_lines: pH 7.8, 30°C, 0.18 mM isopentenyl diphosphate

proof_lines: pH 7.8, 30°C, 0.21 mM isopentenyl diphosphate

source_databases_merged: brenda skid uniprot

enzyme: (2Z,6Z)-farnesyl diphosphate synthase


organism: Streptomyces sp

substrate_name: S-adenosyl-L-methionine (for fluorinase activity)

proof_lines: kcat is 0.262 min(-1) for fluorinase activity (PubMed:24449539). kcat is 0.22 min(-1) for fluorinase activity (PubMed:27739177). kcat is 0.017 min(-1) for SAM hydrolase activity (PubMed:36996195). kcat is 0.008 min(-1) for chlorinase activi


organism: Achromobacter denitrificans

substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt P22256

organism: Escherichia coli

proof_lines: kcat is 47.4 sec(-1) with 4-aminobutanoate as substrate (at 25 degrees Celsius and pH 7.8).

source_databases_merged: skid uniprot

enzyme: UniProt P22256


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


enzyme_display_name: deoxyhypusine monooxygenase

substrate_name: 6-N-[(R)-4-amino-2-hydroxybutyl]-L-lysine of human translation initiation factor 5A

enzyme: deoxyhypusine monooxygenase


organism: Streptomyces sp. (strain KO-3988)


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

substrate_name: sym-nor-spermidine (at 78 degrees Celsius and at pH 7.5)

smiles: C(CN)CNCCCN


enzyme_display_name: norspermine synthase

organism: Thermus thermophilus

enzyme: norspermine synthase


enzyme_display_name: Decaprenyl diphosphate synthase

substrate_name: NPP (at pH 7.9 and 37 degrees Celsius)

column_label: Official PMC HTML Table 2 row NPP column Km=29 uM.

normalized_value_unit_evidence: Km 0.029 mM for NPP; this is the only required metric for the row.

raw_value_unit_evidence: Km 29 uM for NPP.

row_label: NPP

table_label: Table 2. Kinetic parameters for Rv2361c.

enzyme: Decaprenyl diphosphate synthase

substrate: NPP (at pH 7.9 and 37 degrees Celsius)


enzyme_display_name: 4-aminobutyrate aminotransferase GabT

organism: Escherichia coli (strain K12)

substrate_name: 5-aminopentanoate (measured for a coupled GabT/GabD reaction)

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

enzyme: 4-aminobutyrate aminotransferase GabT


enzyme_display_name: 4-hydroxybenzoate geranyltransferase

organism: Lithospermum erythrorhizon

substrate_name: Geranyl diphosphate; 4-Hydroxybenzoate

enzyme: 4-hydroxybenzoate geranyltransferase

substrate: Geranyl diphosphate; 4-Hydroxybenzoate


substrate_name: 4-Hydroxybenzoate; Geranyl diphosphate

substrate: 4-Hydroxybenzoate; Geranyl diphosphate


enzyme_display_name: adenosyl-chloride synthase

organism: Salinispora tropica

substrate_name: Cl-; S-Adenosyl-L-methionine

enzyme: adenosyl-chloride synthase

substrate: Cl-; S-Adenosyl-L-methionine


organism: Bos taurus

substrate_name: D-Fructose 6-phosphate; L-Glutamine

substrate: D-Fructose 6-phosphate; L-Glutamine


substrate_name: L-Glutamine; D-Fructose 6-phosphate

substrate: L-Glutamine; D-Fructose 6-phosphate


enzyme_display_name: 4-aminobutyrate transaminase

organism: Sus scrofa

substrate_name: 4-Aminobutanoate; 2-Oxoglutarate

enzyme: 4-aminobutyrate transaminase

substrate: 4-Aminobutanoate; 2-Oxoglutarate


enzyme_display_name: D-amino-acid transaminase

organism: Arabidopsis thaliana

substrate_name: D-Alanine; 2-Oxoglutarate

enzyme: D-amino-acid transaminase

substrate: D-Alanine; 2-Oxoglutarate


organism: Bacillus sp.

substrate_name: 2-Oxoglutarate; D-Alanine

substrate: 2-Oxoglutarate; D-Alanine


organism: Lysinibacillus sphaericus


organism: Rattus norvegicus


substrate_name: N-succinyldiaminopimelate

substrate: N-succinyldiaminopimelate


enzyme_display_name: Alanine--glyoxylate aminotransferase 2, mitochondrial

substrate_name: D-beta-aminoisobutyrate

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

substrate: D-beta-aminoisobutyrate


substrate_name: 2-Oxoglutarate; D-Glutamate

substrate: 2-Oxoglutarate; D-Glutamate


organism: Homo sapiens

smiles: NCCCC(=O)O


substrate_name: 2-Oxoglutarate; 4-Aminobutanoate

substrate: 2-Oxoglutarate; 4-Aminobutanoate


enzyme_display_name: geranylfarnesyl diphosphate synthase

organism: Leucosceptrum canum

substrate_name: isopentenyl diphosphate

proof_lines: kcat is 16.9x10(-6) sec(-1) with dimethylallyl diphosphate as substrate (in the presence of isopentenyl diphosphate) (PubMed:26941091). kcat is 8.2x10(-6) sec(-1) with isopentenyl diphosphate as substrate (in the presence of geranylgeranyl

enzyme: geranylfarnesyl diphosphate synthase

substrate: isopentenyl diphosphate


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


substrate_name: Isopentenyl diphosphate

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

substrate: Isopentenyl diphosphate


substrate_name: trans,trans-Farnesyl diphosphate; Isopentenyl diphosphate

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


organism: Plasmodium falciparum

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase, chloroplastic

organism: Solanum habrochaites

substrate_name: nerylpyrophosphate in the presence of 180 uM isopentenyl diphosphate

proof_lines: isopentenyl diphosphate acts as activator of its own catalysis.


enzyme_display_name: 4,4'-diapophytoene synthase

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

enzyme: 4,4'-diapophytoene synthase


organism: Vigna radiata var. radiata


enzyme_display_name: beta-alanine-pyruvate transaminase

organism: Achromobacter denitrificans

substrate_name: L-beta-amino-n-butyric acid

enzyme: beta-alanine-pyruvate transaminase

substrate: L-beta-amino-n-butyric acid


enzyme_display_name: 4-aminobutyrate aminotransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: 4-aminobutyrate aminotransferase


enzyme_display_name: Bifunctional aminodeoxychorismate lyase / D-amino acid transaminase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: aminodeoxychorismate

proof_lines: kcat is 1.9 sec(-1) with aminodeoxychorismate as substrate. kcat is 1.46 sec(-1) with D-alanine as substrate. kcat is 0.25 sec(-1) with D-glutamate as substrate.

substrate: aminodeoxychorismate


organism: Salinispora tropica CNB-440

substrate_name: Iodide

assay_conditions_summary: pH 7.9; 310.15 K; buffer 50 mM phosphate

column_label: Official PMC Table 1 row I- (Forward reaction): kcat 0.3 +/- 0.1 min^-1 | Km 260 +/- 20 mM | kcat/Km 0.00115 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.005 normalized_unit=s^-1; Km normalized_value=260.0 normalized_unit=mM; kcat/Km ratio normalized_value=0.00001923076923076923 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.000019166666666666667 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row I-: kcat raw_value=0.3 +/- 0.1 raw_unit=min^-1; Km raw_value=260 +/- 20 raw_unit=mM; kcat/Km raw_value=0.00115 raw_unit=mM^-1 min^-1.

row_label: I-

table_label: Table 1. Apparent kinetic constants of SalL wild type and relative activity of point mutants

substrate: Iodide


substrate_name: bromide

column_label: Official PMC Table 1 row Br- (Forward reaction): kcat 0.8 +/- 0.1 min^-1 | Km 150 +/- 15 mM | kcat/Km 0.0053 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.013333333333333334 normalized_unit=s^-1; Km normalized_value=150.0 normalized_unit=mM; kcat/Km ratio normalized_value=0.00008888888888888889 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.00008833333333333333 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row Br-: kcat raw_value=0.8 +/- 0.1 raw_unit=min^-1; Km raw_value=150 +/- 15 raw_unit=mM; kcat/Km raw_value=0.0053 raw_unit=mM^-1 min^-1.

row_label: Br-

substrate: bromide


substrate_name: S-adenosyl-L-methionine

column_label: Official PMC Table 1 row SAM (Forward reaction): kcat 0.9 +/- 0.1 min^-1 | Km (1 +/- 0.2) x 10^-3 mM | kcat/Km 900 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.015 normalized_unit=s^-1; Km normalized_value=0.001 normalized_unit=mM; kcat/Km ratio normalized_value=15.0 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=15.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row SAM: kcat raw_value=0.9 +/- 0.1 raw_unit=min^-1; Km raw_value=(1 +/- 0.2) x 10^-3 raw_unit=mM; kcat/Km raw_value=900 raw_unit=mM^-1 min^-1.

row_label: SAM

substrate: S-adenosyl-L-methionine


substrate_name: chloride

column_label: Official PMC Table 1 row Cl- (Forward reaction): kcat 0.9 +/- 0.1 min^-1 | Km 45 +/- 5 mM | kcat/Km 0.02 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.015 normalized_unit=s^-1; Km normalized_value=45.0 normalized_unit=mM; kcat/Km ratio normalized_value=0.0003333333333333333 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=0.0003333333333333333 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Forward reaction row Cl-: kcat raw_value=0.9 +/- 0.1 raw_unit=min^-1; Km raw_value=45 +/- 5 raw_unit=mM; kcat/Km raw_value=0.02 raw_unit=mM^-1 min^-1.

row_label: Cl-

substrate: chloride


substrate_name: L-methionine

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

column_label: Official PMC Table 1 row L-Met (Reverse reaction): kcat 12 +/- 1 min^-1 | Km 2.6 +/- 0.2 mM | kcat/Km 4.6 mM^-1 min^-1.

raw_value_unit_evidence: Table 1 Reverse reaction row L-Met: kcat raw_value=12 +/- 1 raw_unit=min^-1; Km raw_value=2.6 +/- 0.2 raw_unit=mM; kcat/Km raw_value=4.6 raw_unit=mM^-1 min^-1.

row_label: L-Met

source_databases_merged: brenda skid

substrate: L-methionine


column_label: Official PMC Table 1 row 5'-ClDA (Reverse reaction): kcat 12 +/- 1 min^-1 | Km (2 +/- 1) x 10^-4 mM | kcat/Km 60,000 mM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.2 normalized_unit=s^-1; Km normalized_value=0.0002 normalized_unit=mM; kcat/Km ratio normalized_value=1000.0 normalized_unit=s^-1*mM^-1; printed kcat/Km column normalized_value=1000.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Reverse reaction row 5'-ClDA: kcat raw_value=12 +/- 1 raw_unit=min^-1; Km raw_value=(2 +/- 1) x 10^-4 raw_unit=mM; kcat/Km raw_value=60,000 raw_unit=mM^-1 min^-1.


proof_lines: in 50 mM phosphate buffer (pH 7.9) at 37°C


enzyme_display_name: UniProt P9WNP7

organism: Mycobacterium tuberculosis

substrate_name: NADH

enzyme: UniProt P9WNP7

substrate: NADH


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase

enzyme: 3-hydroxyacyl-CoA dehydrogenase


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G116F to reconstruct the assayed variant sequence.


organism: Caenorhabditis elegans

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R204A/Y209A to reconstruct the assayed variant sequence.


organism: Metallosphaera sedula


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


enzyme_display_name: glyoxylate reductase

organism: Arabidopsis thaliana

substrate_name: glyoxylate

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

assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADPH

proof_lines: mutant T335A, cosubstrate NADPH, pH 6.2, 25°C

proof_lines: mutant T335A, cosubstrate NADH, pH 6.2, 25°C

enzyme: glyoxylate reductase

substrate: glyoxylate


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

proof_lines: wild-type, cosubstrate NADPH, pH 6.2, 25°C

proof_lines: wild-type, cosubstrate NADH, pH 6.2, 25°C


substrate_name: NADPH

substrate: NADPH


proof_lines: mutant T335D, cosubstrate NADPH, pH 6.2, 25°C

proof_lines: mutant T335D, cosubstrate NADH, pH 6.2, 25°C


assay_conditions_summary: pH 6.2; 298.15 K; cofactor NADH


assay_conditions_summary: cofactor CoA

proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxyoctanoyl-CoA


proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxyhexanoyl-CoA


assay_conditions_summary: cofactor NAD+


proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxybutyryl-CoA


proof_lines: mitochondrial enzyme, oxidation of (S)-3-hydroxydecanoyl-CoA


assay_conditions_summary: cofactor NADPH


substrate_name: acetoacetyl-pantetheine

substrate: acetoacetyl-pantetheine


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Mycolicibacterium smegmatis


substrate_name: acetoacetyl-N-acetyl-cysteamine

substrate: acetoacetyl-N-acetyl-cysteamine


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

organism: Leptosphaeria maculans

substrate_name: cyclohex-1-en-1-ylmethyl diphosphate

normalized_value_unit_evidence: kcat normalized_value=0.0055 normalized_unit=s^-1; Km normalized_value=0.13 normalized_unit=mM; kcat/Km normalized_value=0.04166666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.33 raw_unit=min^-1; Km raw_value=0.13 raw_unit=mM; kcat/Km raw_value=2.5 raw_unit=mM^-1*min^-1

row_label: A4 / cyclohex-1-en-1-ylmethyl diphosphate

table_label: Table 1. Kinetic parameters for SirD with L-Tyr and alkyl-PP analogues

enzyme: 4-O-dimethylallyl-L-tyrosine synthase

substrate: cyclohex-1-en-1-ylmethyl diphosphate


substrate_name: dimethylallyl diphosphate

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

normalized_value_unit_evidence: kcat normalized_value=0.6833333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.23 normalized_unit=mM; kcat/Km normalized_value=2.966666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=41 raw_unit=min^-1; Km raw_value=0.23 raw_unit=mM; kcat/Km raw_value=178 raw_unit=mM^-1*min^-1

row_label: A1 / dimethylallyl diphosphate

substrate: dimethylallyl diphosphate


substrate_name: 2-cyclohexylideneethyl diphosphate

normalized_value_unit_evidence: kcat normalized_value=0.05833333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.21 normalized_unit=mM; kcat/Km normalized_value=0.2666666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.5 raw_unit=min^-1; Km raw_value=0.21 raw_unit=mM; kcat/Km raw_value=16 raw_unit=mM^-1*min^-1

row_label: A5 / 2-cyclohexylideneethyl diphosphate

substrate: 2-cyclohexylideneethyl diphosphate


normalized_value_unit_evidence: kcat normalized_value=0.003666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.17 normalized_unit=mM; kcat/Km normalized_value=0.02166666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.22 raw_unit=min^-1; Km raw_value=0.17 raw_unit=mM; kcat/Km raw_value=1.3 raw_unit=mM^-1*min^-1

row_label: A19 / (2E)-2-methylpenta-2,4-dien-1-yl diphosphate


substrate_name: (2E)-3-methylpent-2-en-1-yl diphosphate

smiles: CC/C(C)=C/COP(=O)(O)OP(=O)(O)O

column_label: Table 1 row A2; raw cells kcat 18 min^-1, KM 0.2 mM, kcat/KM 90 mM^-1 min^-1; normalized cells 0.3 s^-1, 0.2 mM, 1.5 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; Km normalized_value=0.2 normalized_unit=mM; kcat/Km normalized_value=1.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=18 raw_unit=min^-1; Km raw_value=0.2 raw_unit=mM; kcat/Km raw_value=90 raw_unit=mM^-1*min^-1

row_label: A2 / (2E)-3-methylpent-2-en-1-yl diphosphate

substrate: (2E)-3-methylpent-2-en-1-yl diphosphate


normalized_value_unit_evidence: kcat normalized_value=0.01233333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.12 normalized_unit=mM; kcat/Km normalized_value=0.1016666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.74 raw_unit=min^-1; Km raw_value=0.12 raw_unit=mM; kcat/Km raw_value=6.1 raw_unit=mM^-1*min^-1

row_label: A20 / (2E,4Z)-2-methylhexa-2,4-dien-1-yl diphosphate


smiles: CC(C)=C/C=C/COP(=O)(O)OP(=O)(O)O

normalized_value_unit_evidence: kcat normalized_value=0.001666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.73 normalized_unit=mM; kcat/Km normalized_value=0.002333333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.1 raw_unit=min^-1; Km raw_value=0.73 raw_unit=mM; kcat/Km raw_value=0.14 raw_unit=mM^-1*min^-1

row_label: A18 / (2E)-5-methylhexa-2,4-dien-1-yl diphosphate


substrate_name: (2E)-but-2-en-1-yl diphosphate

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

substrate: (2E)-but-2-en-1-yl diphosphate


substrate_name: (2E)-penta-2,4-dien-1-yl diphosphate

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

normalized_value_unit_evidence: kcat normalized_value=0.0008333333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.26 normalized_unit=mM; kcat/Km normalized_value=0.003333333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.05 raw_unit=min^-1; Km raw_value=0.26 raw_unit=mM; kcat/Km raw_value=0.2 raw_unit=mM^-1*min^-1

row_label: A17 / (2E)-penta-2,4-dien-1-yl diphosphate

substrate: (2E)-penta-2,4-dien-1-yl diphosphate


substrate_name: (2Z)-3-chlorobut-2-en-1-yl diphosphate

smiles: C/C(Cl)=C/COP(=O)(O)OP(=O)(O)O

normalized_value_unit_evidence: kcat normalized_value=0.0006666666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.05 normalized_unit=mM; kcat/Km normalized_value=0.01666666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.04 raw_unit=min^-1; Km raw_value=0.05 raw_unit=mM; kcat/Km raw_value=1 raw_unit=mM^-1*min^-1

row_label: A11 / (2Z)-3-chlorobut-2-en-1-yl diphosphate

substrate: (2Z)-3-chlorobut-2-en-1-yl diphosphate


organism: Bos taurus


enzyme_display_name: acetoacetyl-CoA reductase

organism: Methylorubrum rhodesianum

proof_lines:
cofactor NADPH
cofactor NADH

enzyme: acetoacetyl-CoA reductase


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


proof_lines: recombinant mutant R204A/Y209A, pH 7.0, 25°C

proof_lines: recombinant mutants R204A and Y209A, pH 7.0, 25°C


proof_lines: recombinant wild-type enzyme, pH 7.0, 25°C


organism: Clostridium acetobutylicum

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


organism: Candida tropicalis

mutation_signature: Δ2

mutation_type: deletion


organism: Homo sapiens

assay_conditions_summary: pH 8; cofactor CoA

proof_lines:
isozyme SCHAD II, at pH 8.0
isozyme SCHAD II, at pH 7.0
enzyme from brain, pH 7.0


proof_lines:
isozyme SCHAD I, at pH 8.5
isozyme SCHAD II, at pH 9.3
enzyme from brain


assay_conditions_summary: pH 8.5; cofactor CoA

proof_lines:
isozyme SCHAD I, at pH 8.5
isozyme SCHAD I, at pH 8.0
isozyme SCHAD II, at pH 8.0


assay_conditions_summary: pH 7; cofactor NAD+

proof_lines: enzyme from brain, substrate 17beta-estradiol


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


assay_conditions_summary: pH 9.5; 303.15 K; cofactor CoA


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


organism: Rattus norvegicus

assay_conditions_summary: pH 5; cofactor CoA

proof_lines: pH 5.0, recombinant His-tagged mutant S137C


proof_lines: pH 5.0, recombinant His-tagged mutant S137T


proof_lines: pH 5.0, recombinant His-tagged mutant S137A


proof_lines: pH 5.0, recombinant His-tagged wild-type enzyme


organism: Sus scrofa


assay_conditions_summary: pH 7; cofactor CoA


assay_conditions_summary: cofactor NADH


organism: Zoogloea ramigera

substrate_name: butyrylacetyl-CoA

substrate: butyrylacetyl-CoA


assay_conditions_summary: cofactor CoA


organism: Cupriavidus necator

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

proof_lines:
enzyme Had, at pH 8.0 and 30°C
enzyme PaaH1, at pH 8.0 and 30°C


proof_lines:
enzyme PaaH1, at pH 8.0 and 30°C
enzyme Had, at pH 8.0 and 30°C


substrate_name: androsterone

substrate: androsterone


organism: Digitalis purpurea

substrate_name: NADH

substrate: NADH


assay_conditions_summary: cofactor NADPH


assay_conditions_summary: pH 7.8; 295.15 K; cofactor NADPH

proof_lines: pH 7.8, 22°C, recombinant His6-tagged enzyme


substrate_name: S-acetoacetyl-N-acetylcysteamine

substrate: S-acetoacetyl-N-acetylcysteamine


organism: Spinacia oleracea

proof_lines: NADPH, cytosolic enzyme type with preference for hydroxypyruvate as substrate

proof_lines: NADH, peroxisomal enzyme type with preference for hydroxypyruvate and NADH as substrates


substrate_name: Hydroxypyruvate

proof_lines: NADPH, cytosolic enzyme type with preference for hydroxypyruvate and NADPH as substrates

substrate: Hydroxypyruvate


organism: Digitalis lanata


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


enzyme_display_name: (R)-3-hydroxyacid-ester dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: ethyl 3-oxohexanoate

smiles: CCCC(=O)CC(=O)OCC

enzyme: (R)-3-hydroxyacid-ester dehydrogenase

substrate: ethyl 3-oxohexanoate


substrate_name: ethyl 3-oxobutanoate

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

substrate: ethyl 3-oxobutanoate


proof_lines:
in presence of NADH
in presence of NADPH


substrate_name: Unknown

substrate: Unknown


substrate_name: acetoacetyl-pantetheine

substrate: acetoacetyl-pantetheine


substrate_name: acetoacetyl-N-acetylcysteamine

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

substrate: acetoacetyl-N-acetylcysteamine


organism: Azotobacter vinelandii

substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


substrate_name: NADPH

substrate: NADPH


substrate_name: glyoxylate

substrate: glyoxylate


organism: Streptomyces coelicolor


proof_lines:
cofactor NADPH
cofactor NADH


proof_lines: pH 6.5, 30°C, recombinant enzyme in presence of 0.1 mM acetyl-CoA


organism: Escherichia coli


organism: Metallosphaera sedula

assay_conditions_summary: pH 8; 343.15 K; cofactor CoA


substrate_name: NAD+

assay_conditions_summary: pH 8; 338.15 K; cofactor NAD+

substrate: NAD+


organism: Unknown

substrate_name: SPC_39_Cell; SPC_38_Cell; SPC_2019_Cell

substrate: SPC_39_Cell; SPC_38_Cell; SPC_2019_Cell


organism: Pigeon


substrate_name: beta-ketopalmitoyl-CoA

substrate: beta-ketopalmitoyl-CoA


enzyme_display_name: 4-pyridoxic acid dehydrogenase

organism: Pseudomonas sp. MA-1

proof_lines: electron acceptor phenazine methosulfate, pH 8.0, 25°C

proof_lines: electron acceptor 2,6-dichloroindophenol, pH 8.0, 25°C

enzyme: 4-pyridoxic acid dehydrogenase


enzyme_display_name: serine 3-dehydrogenase (NADP+)

substrate_name: L-serine

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

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

enzyme: serine 3-dehydrogenase (NADP+)

substrate: L-serine


substrate_name: L-allo-threonine

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

substrate: L-allo-threonine


substrate_name: NADP+

substrate: NADP+


substrate_name: Glyoxylate

substrate: Glyoxylate


organism: Zea mays

substrate_name: NADPH; H+; Glyoxylate

substrate: NADPH; H+; Glyoxylate


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: pH 7.4, 37°C recombinant His-tagged enzyme


organism: Mesorhizobium loti

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication


organism: Saccharolobus solfataricus

substrate_name: NADH

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADH

proof_lines: pH 7.5, 70°C, recombinant enzyme and native enzyme from xylose-grown cell extract

substrate: NADH


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 5

proof_lines:
mutant E149Q, pH 8.0, 30°C
mutant E149Q, pH 5.0, 30°C


assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor NADH


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)


substrate_name: NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: Acetoacetyl-CoA reductase

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

substrate_name: acetoacetyl-CoA

enzyme: Acetoacetyl-CoA reductase


substrate_name: NADPH


substrate_name: tetramyristoyl cardiolipin

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetoacetyl-CoA (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 4.3 sec(-1) with beta-ketododecanoyl-CoA as substrate. kcat is 3.5 sec(-1) with beta-ketooctanoyl-CoA as substrate. kcat is 1.9 sec(-1) with acetoacetyl-CoA as substrate. kcat is 2.6 sec(-1) with NADPH as substrate (PubMed:11932442)


substrate_name: NADPH (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor NADPH


substrate_name: H+; Glyoxylate; NADH

assay_conditions_summary: cofactor NAD+

substrate: H+; Glyoxylate; NADH


organism: Thermococcus litoralis

substrate_name: NADH; Glyoxylate; H+

substrate: NADH; Glyoxylate; H+


enzyme_display_name: UniProt P34439

organism: Caenorhabditis elegans

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

enzyme: UniProt P34439


organism: Drosophila melanogaster

substrate_name: NAD (in the presence of (3S)-3-hydroxybutanoyl-CoA, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: Fatty acid oxidation complex subunit alpha

organism: Escherichia coli (strain K12)

substrate_name: L-3-hydroxy-4-trans-decenoyl-CoA (for enoyl-CoA hydratase activity)

assay_conditions_summary: cofactor CoA


enzyme_display_name: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial

substrate_name: acetoacetyl-CoA at pH 5.0

assay_conditions_summary: pH 5; cofactor CoA

substrate: acetoacetyl-CoA at pH 5.0


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

proof_lines: kcat is 1.14 sec(-1) with acetoacetyl-CoA as substrate. kcat is 5.72 sec(-1) with beta-keto-octanoyl-CoA as substrate.

substrate: acetoacetyl-CoA


organism: Sus scrofa

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 1, row 3-Hydroxybutyryl-CoA, column Apparent Km (uM): 7.2. Shared footnote a states pH 8 forward-direction measurements with L-3-hydroxyacyl-CoA as variable substrate, several fixed NAD+ concentrations, CoASH, and 3-ketoacyl-CoA thiolase.

raw_value_unit_evidence: Apparent Km 7.2 uM.

table_label: Table 1. Kinetic Parameters of Pig Heart 3-Hydroxyacyl-CoA Dehydrogenase

enzyme: Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial


organism: Methylorubrum rhodesianum

substrate_name: L-beta-hydroxybutyryl-CoA

substrate: L-beta-hydroxybutyryl-CoA


organism: Vitis vinifera

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: UniProt Q0KEY8

organism: Cupriavidus necator

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: UniProt Q0KEY8


substrate_name: 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


organism: Mycobacterium smegmatis

substrate_name: H+; NADPH; Acetoacetyl-CoA

assay_conditions_summary: cofactor NADPH

substrate: H+; NADPH; Acetoacetyl-CoA


substrate_name: beta-ketododecanoyl-CoA (at 25 degrees Celsius and at pH 7.0)


organism: Escherichia coli

substrate_name: trans,trans-Farnesyl diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D215A to reconstruct the assayed variant sequence.

substrate: trans,trans-Farnesyl diphosphate


organism: Aspergillus niger

proof_lines:
TyrPT
tyrosine derivatives
Aspergillus niger


proof_lines:
4- and 5-methyl-DL-tryptophan
L-tryptophan
TyrPT


substrate_name: alpha-methyl-L-tyrosine

substrate: alpha-methyl-L-tyrosine


substrate_name: dimethylallyl diphosphate

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

column_label: Table 4 (Comparison of kinetic parameters of TyrPT with those of SirD published previously) prints one compound-label column followed by two column groups, SirD and TyrPT, each with the heads KM (mM), kcat (s-1) and kcat/KM (s-1 M-1). The cited cell set is the TyrPT column group of compound row DMAPPc: KM (mM) = 0.71; kcat (s-1) = 0.69; kcat/KM (s-1 M-1) = 972. The SirD column group of the same row belongs to the Leptosphaeria maculans enzyme SirD and was adopted from previous publications, as the table's own footnote states, so it is not read for this catalog row.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.69 s-1; the TyrPT kcat column of this table is already per second, so no unit conversion applies and the paper value is 0.69 s^(-1). Km: printed Table 4 cell 0.71 mM; the KM column is already in millimolar, so no unit conversion applies and the paper value is 0.71 mM. kcat/Km: printed Table 4 cell 972 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 972 / 1000 = 0.972 s^-1 mM^-1, and the exact quotient of the two printed component cells of the same row is 0.69 / 0.71 = 0.9718309859154929 s^-1 mM^-1, which is the value the catalog holds.

raw_value_unit_evidence: Table 4, TyrPT columns, compound row DMAPPc (substrate dimethylallyl diphosphate): KM = 0.71 mM; kcat = 0.69 s-1; printed kcat/KM = 972 s-1 M-1.

table_label: Table 4: Comparison of kinetic parameters of TyrPT with those of SirD published previously (Appl Microbiol Biotechnol 2014, 98(24):10119-10129)

substrate: dimethylallyl diphosphate


column_label: Table 4 (Comparison of kinetic parameters of TyrPT with those of SirD published previously) prints one compound-label column followed by two column groups, SirD and TyrPT, each with the heads KM (mM), kcat (s-1) and kcat/KM (s-1 M-1). The cited cell set is the TyrPT column group of compound row 6a: KM (mM) = 0.19; kcat (s-1) = 0.27; kcat/KM (s-1 M-1) = 1,421. The SirD column group of the same row belongs to the Leptosphaeria maculans enzyme SirD and was adopted from previous publications, as the table's own footnote states, so it is not read for this catalog row.

normalized_value_unit_evidence: kcat: printed Table 4 cell 0.27 s-1; the TyrPT kcat column of this table is already per second, so no unit conversion applies and the paper value is 0.27 s^(-1). Km: printed Table 4 cell 0.19 mM; the KM column is already in millimolar, so no unit conversion applies and the paper value is 0.19 mM. kcat/Km: printed Table 4 cell 1,421 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1421 / 1000 = 1.421 s^-1 mM^-1, and the exact quotient of the two printed component cells of the same row is 0.27 / 0.19 = 1.4210526315789473 s^-1 mM^-1, which is the value the catalog holds.

raw_value_unit_evidence: Table 4, TyrPT columns, compound row 6a (substrate 3,4-dihydroxy-L-phenylalanine): KM = 0.19 mM; kcat = 0.27 s-1; printed kcat/KM = 1,421 s-1 M-1.

row_label: Table 4, TyrPT columns, compound row 6a


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: D-Tyrosine

substrate: D-Tyrosine


substrate_name: Isopentenyl diphosphate

substrate: Isopentenyl diphosphate


enzyme_display_name: Alanine--glyoxylate aminotransferase 2, mitochondrial

organism: Rattus norvegicus

substrate_name: N(omega),N('omega)-dimethyl-L-arginine (with pyruvate as cosubstrate)


substrate_name: N(omega),N(omega)-dimethyl-L-arginine (with pyruvate as cosubstrate)

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

column_label: Table IV row N^G,N^G-Dimethyl-L-arginine:pyruvate; amino acid Km (mM) column = 9.7 +/- 1.2.

raw_value_unit_evidence: Km raw_value=9.7 +/- 1.2 raw_unit=mM

table_label: Table IV, Kinetic properties of dimethylarginine:pyruvate aminotransferase

enzyme: Alanine--glyoxylate aminotransferase 2, mitochondrial


substrate_name: N(omega)-methyl-L-arginine (with pyruvate as cosubstrate)

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

column_label: Table IV row N^G-Monomethyl-L-arginine:pyruvate; amino acid Km (mM) column = 8.0 +/- 0.9.

raw_value_unit_evidence: Km raw_value=8.0 +/- 0.9 raw_unit=mM


substrate_name: L-ornithine (with pyruvate as cosubstrate)

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

column_label: Table IV row L-Ornithine:pyruvate; amino acid Km (mM) column = 70.0 +/- 1.2.

raw_value_unit_evidence: Km raw_value=70.0 +/- 1.2 raw_unit=mM


substrate_name: L-alanine (with glyoxylate as cosubstrate)

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

column_label: Kinetic Properties prose states: in the transamination between L-alanine and glyoxylate, Km values for L-alanine and glyoxylate were 7.8 and 2.9 mM, respectively.

raw_value_unit_evidence: Km raw_value=7.8 raw_unit=mM

row_label: L-alanine in the L-alanine/glyoxylate substrate pair

table_label: Kinetic Properties prose, page 20940


substrate_name: pyruvate (with L-ornithine as cosubstrate)

column_label: Table IV row L-Ornithine:pyruvate; keto acid Km (mM) column = 4.1 +/- 0.5.

raw_value_unit_evidence: Km raw_value=4.1 +/- 0.5 raw_unit=mM


substrate_name: glyoxylate (with L-alanine as cosubstrate)

raw_value_unit_evidence: Km raw_value=2.9 raw_unit=mM

row_label: glyoxylate in the L-alanine/glyoxylate substrate pair


enzyme_display_name: UniProt P9WFF7

organism: Mycobacterium tuberculosis

substrate_name: isopentenyl diphosphate

column_label: Table 2; substrate column IPP; row Kcat (min^-1) raw value 4.8; row Km (uM) raw value 89; row Kcat/Km raw value 5.4 x 10^4 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=0.08 normalized_unit=s^-1; Km normalized_value=0.089 normalized_unit=mM; kcat/Km normalized_value=0.9 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.8 raw_unit=min^-1; Km raw_value=89 raw_unit=uM; kcat/Km raw_value=5.4 x 10^4 raw_unit=M^-1*min^-1

row_label: IPP

table_label: Table 2. Calculated kinetic parameters of Rv2361c

enzyme: UniProt P9WFF7

substrate: isopentenyl diphosphate


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

column_label: Table 2; substrate column E,Z-FPP; row Kcat (min^-1) raw value 690; row Km (uM) raw value 290; row Kcat/Km raw value 2.4 x 10^6 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=11.5 normalized_unit=s^-1; Km normalized_value=0.29 normalized_unit=mM; kcat/Km normalized_value=40 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=690 raw_unit=min^-1; Km raw_value=290 raw_unit=uM; kcat/Km raw_value=2.4 x 10^6 raw_unit=M^-1*min^-1

row_label: E,Z-FPP

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


substrate_name: geranyl diphosphate

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

column_label: Table 2; substrate column GPP; row Kcat (min^-1) raw value 3.6; row Km (uM) raw value 490; row Kcat/Km raw value 7.4 x 10^3 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=0.06 normalized_unit=s^-1; Km normalized_value=0.49 normalized_unit=mM; kcat/Km normalized_value=0.1233333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=3.6 raw_unit=min^-1; Km raw_value=490 raw_unit=uM; kcat/Km raw_value=7.4 x 10^3 raw_unit=M^-1*min^-1

row_label: GPP

substrate: geranyl diphosphate


substrate_name: geranylgeranyl diphosphate

column_label: Table 2; substrate column GGPP; row Kcat (min^-1) raw value 1.8; row Km (uM) raw value 40; row Kcat/Km raw value 4.3 x 10^5 with unit M^-1*min^-1 from Kcat/Km using Km in M

normalized_value_unit_evidence: kcat normalized_value=0.03 normalized_unit=s^-1; Km normalized_value=0.04 normalized_unit=mM; kcat/Km normalized_value=7.166666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.8 raw_unit=min^-1; Km raw_value=40 raw_unit=uM; kcat/Km raw_value=4.3 x 10^5 raw_unit=M^-1*min^-1

row_label: GGPP

substrate: geranylgeranyl diphosphate


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


substrate_name: neryl diphosphate

smiles: CC(C)=CCC/C(C)=C\COP(=O)(O)OP(=O)(O)O

column_label: Official PMC HTML Table 2 row NPP columns Km=29 uM, Kcat=3.1 min^-1, Kcat/Km=1.1 x 10^5.

row_label: NPP

substrate: neryl diphosphate


substrate_name: D-Fructose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V605L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: D-Fructose 6-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W74L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: L-Glutamine

sequence_variant_note: Mutation signature A602L matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: L-Glutamine


organism: Arabidopsis thaliana

smiles: NCCCC(=O)O

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column Km mM, raw cell 0.34+/-0.02, normalized 0.34 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column kcat/Km s^-1 mM^-1, raw cell 31, normalized 31 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km normalized_value=31 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.34+/-0.02 raw_unit=mM raw_cell=0.34+/-0.02; kcat/Km raw_value=31 raw_unit=s^-1*mM^-1 raw_cell=31


column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (4-oxobutanoate; succinate semialdehyde) / fixed substrate alanine, column kcat s^-1, raw cell 10.8, normalized 10.8 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (4-oxobutanoate; succinate semialdehyde) / fixed substrate alanine, column Km mM, raw cell 0.014+/-0.002, normalized 0.014 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (4-oxobutanoate; succinate semialdehyde) / fixed substrate alanine, column kcat/Km s^-1 mM^-1, raw cell 770, normalized 770 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.8 normalized_unit=s^-1; Km normalized_value=0.014 normalized_unit=mM; kcat/Km normalized_value=770 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.8 raw_unit=s^-1 raw_cell=10.8; Km raw_value=0.014+/-0.002 raw_unit=mM raw_cell=0.014+/-0.002; kcat/Km raw_value=770 raw_unit=s^-1*mM^-1 raw_cell=770


substrate_name: glyoxylate

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate glyoxylate / fixed substrate GABA, column kcat s^-1, raw cell 9.7, normalized 9.7 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate glyoxylate / fixed substrate GABA, column Km mM, raw cell 0.11+/-0.01, normalized 0.11 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate glyoxylate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 88, normalized 88 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=9.7 normalized_unit=s^-1; Km normalized_value=0.11 normalized_unit=mM; kcat/Km normalized_value=88 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=9.7 raw_unit=s^-1 raw_cell=9.7; Km raw_value=0.11+/-0.01 raw_unit=mM raw_cell=0.11+/-0.01; kcat/Km raw_value=88 raw_unit=s^-1*mM^-1 raw_cell=88

substrate: glyoxylate


substrate_name: L-alanine

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column kcat s^-1, raw cell 15.4, normalized 15.4 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column Km mM, raw cell 2.4+/-0.3, normalized 2.4 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column kcat/Km s^-1 mM^-1, raw cell 6.4, normalized 6.4 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=15.4 normalized_unit=s^-1; Km normalized_value=2.4 normalized_unit=mM; kcat/Km normalized_value=6.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=15.4 raw_unit=s^-1 raw_cell=15.4; Km raw_value=2.4+/-0.3 raw_unit=mM raw_cell=2.4+/-0.3; kcat/Km raw_value=6.4 raw_unit=s^-1*mM^-1 raw_cell=6.4

substrate: L-alanine


substrate_name: pyruvate

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column Km mM, raw cell 0.14+/-0.01, normalized 0.14 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 76, normalized 76 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=76 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.14+/-0.01 raw_unit=mM raw_cell=0.14+/-0.01; kcat/Km raw_value=76 raw_unit=s^-1*mM^-1 raw_cell=76

substrate: pyruvate


enzyme_display_name: Serine 3-dehydrogenase

organism: Agrobacterium tumefaciens

substrate_name: L-serine

enzyme: Serine 3-dehydrogenase

substrate: L-serine


substrate_name: L-glycerate

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

column_label: Kinetic prose; ordered analytes D-serine, L-glycerate, D-glycerate; ordered Km values 44, 54, 56 mM; L-glycerate maps to 54 mM.

normalized_value_unit_evidence: L-glycerate Km = 54 mM.

raw_value_unit_evidence: Primary Kinetic prose: Km for D-serine, L-glycerate, and D-glycerate were 44, 54, and 56 mM, respectively.

row_label: D-serine, L-glycerate, and D-glycerate Km sentence; L-glycerate

table_label: Kinetic prose, journal page 155

substrate: L-glycerate


substrate_name: D-glycerate

column_label: Kinetic prose; ordered analytes D-serine, L-glycerate, D-glycerate; ordered Km values 44, 54, 56 mM; D-glycerate maps to 56 mM.

normalized_value_unit_evidence: D-glycerate Km = 56 mM.

row_label: D-serine, L-glycerate, and D-glycerate Km sentence; D-glycerate

substrate: D-glycerate


substrate_name: NADP(+)

assay_conditions_summary: cofactor NADP+

substrate: NADP(+)


organism: Leptosphaeria maculans

substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-Tyr (at pH 7.5 and 37 degrees Celsius)


substrate_name: DMAPP (at pH 7.5 and 37 degrees Celsius)

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


substrate_name: L-tryptophan (at pH 7.5 and 37 degrees Celsius)


enzyme_display_name: 4-hydroxybenzoate geranyltransferase 1

organism: Lithospermum erythrorhizon

column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 10.3 and 53.8 uM for 4HB, respectively; current accession Q8W405 is LePGT-1.

raw_value_unit_evidence: LePGT-1 Km for 4HB = 10.3 uM.

row_label: Recombinant LePGT-1 (Q8W405)

table_label: Results prose, PDF page 3 / JBC page 6243

enzyme: 4-hydroxybenzoate geranyltransferase 1


smiles: CC(=CCCC(=CCOP(=O)(O)OP(=O)(O)O)C)C

column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 5.1 and 45.9 uM for GPP, respectively; current accession Q8W405 is LePGT-1.

raw_value_unit_evidence: LePGT-1 Km for GPP = 5.1 uM.


enzyme_display_name: 4-hydroxybenzoate geranyltransferase 2

column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 10.3 and 53.8 uM for 4HB, respectively; current accession Q8W404 is LePGT-2.

raw_value_unit_evidence: LePGT-2 Km for 4HB = 53.8 uM.

row_label: Recombinant LePGT-2 (Q8W404)

enzyme: 4-hydroxybenzoate geranyltransferase 2


column_label: Results prose gives LePGT-1 and LePGT-2 Km values of 5.1 and 45.9 uM for GPP, respectively; current accession Q8W404 is LePGT-2.

raw_value_unit_evidence: LePGT-2 Km for GPP = 45.9 uM.


enzyme_display_name: carbazole 1,9a-dioxygenase

organism: Janthinobacterium sp. J3

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I262V to reconstruct the assayed variant sequence.

enzyme: carbazole 1,9a-dioxygenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q282N to reconstruct the assayed variant sequence.


enzyme_display_name: 4-aminobutyrate aminotransferase PuuE

substrate_name: SSA (at pH 7.8 and at 30 degrees Celsius)

enzyme: 4-aminobutyrate aminotransferase PuuE


substrate_name: GABA (at pH 7.8 and at 30 degrees Celsius)

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


substrate_name: KG (at pH 7.8 and at 30 degrees Celsius)

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


substrate_name: L-glutamate (at pH 7.8 and at 30 degrees Celsius)

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


substrate_name: D-aspartate

substrate: D-aspartate


substrate_name: D-alanine

substrate: D-alanine


substrate_name: D-glutamate

substrate: D-glutamate


enzyme_display_name: glyoxylate reductase

organism: Thermococcus litoralis

substrate_name: NADH

assay_conditions_summary: pH 6.5; cofactor NADH

column_label: Wiley full-text Abstract prose reports Km values for glyoxylate, hydroxypyruvate, and NADH in that order as 0.73, 1.3, and 0.067 mM; NADH maps to the third value.

raw_value_unit_evidence: NADH Km 0.067 mM

row_label: NADH

table_label: Wiley full-text Abstract prose

enzyme: glyoxylate reductase

substrate: NADH


substrate_name: glyoxylate

column_label: Wiley full-text Abstract prose reports Km values for glyoxylate, hydroxypyruvate, and NADH in that order as 0.73, 1.3, and 0.067 mM; glyoxylate maps to the first value.

raw_value_unit_evidence: glyoxylate Km 0.73 mM

row_label: glyoxylate


substrate_name: hydroxypyruvate

column_label: Wiley full-text Abstract prose reports Km values for glyoxylate, hydroxypyruvate, and NADH in that order as 0.73, 1.3, and 0.067 mM; hydroxypyruvate maps to the second value.

raw_value_unit_evidence: hydroxypyruvate Km 1.3 mM

row_label: hydroxypyruvate

substrate: hydroxypyruvate


organism: Escherichia coli (strain K12)

substrate_name: crotonyl-CoA

enzyme: Fatty acid oxidation complex subunit alpha

substrate: crotonyl-CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


assay_conditions_summary: cofactor NADH


enzyme_display_name: Polyamine aminopropyltransferase

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

substrate_name: S-adenosylmethioninamine (at 78 degrees Celsius and at pH 7.5)

enzyme: Polyamine aminopropyltransferase


substrate_name: 1,3-diaminopropane (at 78 degrees Celsius and at pH 7.5)

smiles: C(CN)CN

column_label: Abstract lists 1,3-diaminopropane (Km = 1675 microM) among recognized amine acceptor substrates.

raw_value_unit_evidence: Km raw_value=1675 microM raw_unit=microM

row_label: Propylamine transferase / 1,3-diaminopropane amine acceptor

table_label: PubMed XML abstract PMID 3096734


substrate_name: putrescine (at 78 degrees Celsius and at pH 7.5)

smiles: C(CCN)CN

column_label: Abstract lists putrescine (Km = 3850 microM) among recognized amine acceptor substrates.

raw_value_unit_evidence: Km raw_value=3850 microM raw_unit=microM

row_label: Propylamine transferase / putrescine amine acceptor


enzyme_display_name: (2Z,6Z)-farnesyl diphosphate synthase

organism: Solanum habrochaites

substrate_name: dimethylallyl diphosphate

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

proof_lines: very short-chain polyisoprenoid products

enzyme: (2Z,6Z)-farnesyl diphosphate synthase

substrate: dimethylallyl diphosphate


substrate_name: isopentenyl diphosphate

substrate: isopentenyl diphosphate


substrate_name: neryl diphosphate

substrate: neryl diphosphate


organism: Cereibacter sphaeroides

substrate_name: geranyl diphosphate

column_label: Table 2, GPP column, kcat/KM/KM rows: 4 min^-1; 18.5 +/- 3.5 microM; 0.21 min^-1 microM^-1.

raw_value_unit_evidence: Table 2 GPP: kcat = 4 min^-1; KM = 18.5 +/- 3.5 microM; printed kcat/KM = 0.21 min^-1 microM^-1.

table_label: Table 2: Calculated kinetic parameters of Rsdds

substrate: geranyl diphosphate


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

column_label: Springer abstract/prose sentence for FPP kinetic parameters; metric labels Vmax, KM, kcat, and kcat/KM are explicit.

raw_value_unit_evidence: Springer abstract reports Vmax 264.6 pmol/min, KM 13.1 uM, kcat 8.8 1/min, and kcat/KM 0.67 for FPP.

row_label: omega,E,E-farnesyl diphosphate (FPP), most appropriate substrate

table_label: Springer abstract/prose preview

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


column_label: Table 2, IPP column, kcat/KM/KM rows: 8.6 min^-1; 13.8 +/- 4.6 microM; 0.62 min^-1 microM^-1.

raw_value_unit_evidence: Table 2 IPP: kcat = 8.6 min^-1; KM = 13.8 +/- 4.6 microM; printed kcat/KM = 0.62 min^-1 microM^-1.


organism: Trypanosoma cruzi


substrate_name: geranylgeranyl diphosphate

substrate: geranylgeranyl diphosphate


enzyme_display_name: salicylate 1-monooxygenase

organism: Sphingomonas sp.

substrate_name: salicylate

assay_conditions_summary: pH 7

enzyme: salicylate 1-monooxygenase

substrate: salicylate


substrate_name: anthranilate

substrate: anthranilate


enzyme_display_name: Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1

proof_lines: AIM1 beta-oxidation Arabidopsis


enzyme_display_name: Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2

proof_lines: beta-oxidation Arabidopsis AIM1


enzyme_display_name: D-alanine aminotransferase

organism: Bacillus sp. (strain YM-1)

substrate_name: alpha-ketoglutarate

enzyme: D-alanine aminotransferase

substrate: alpha-ketoglutarate


substrate_name: alpha-ketobutyrate

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

substrate: alpha-ketobutyrate


substrate_name: alpha-ketovalerate

substrate: alpha-ketovalerate


organism: Homo sapiens

column_label: Table 2, Acetoacetyl-CoA block, Km row, Normal column reports 11.9 uM; normalized value is 0.0119 mM.

raw_value_unit_evidence: Km raw_value=11.9 raw_unit=uM

row_label: Normal column; Acetoacetyl-CoA block; Km row

table_label: Table 2. Kinetic properties of expressed M/SCHAD proteins


substrate_name: NADH

column_label: Table 2, NADH block, Km row, Normal column reports 24.2 uM; normalized value is 0.0242 mM.

raw_value_unit_evidence: Km raw_value=24.2 raw_unit=uM

row_label: Normal column; NADH block; Km row


organism: Streptomyces anulatus

substrate_name: 5,10-dihydrophenazine 1-carboxylate

substrate: 5,10-dihydrophenazine 1-carboxylate


organism: Sus scrofa

column_label: Table 1, row 3-Hydroxydecanoyl-CoA, column Apparent Km (uM): 2.9. Row carries footnote b, From Ref. (19); shared footnote a states pH 8 forward-direction measurements with L-3-hydroxyacyl-CoA as variable substrate, several fixed NAD+ concentrations, CoASH, and 3-ketoacyl-CoA thiolase.

raw_value_unit_evidence: Apparent Km 2.9 uM.

row_label: 3-Hydroxydecanoyl-CoA (footnote b: From Ref. (19))


column_label: Table 1, row 3-Hydroxyhexadecanoyl-CoA, column Apparent Km (uM): 3.0. Shared footnote a states pH 8 forward-direction measurements with L-3-hydroxyacyl-CoA as variable substrate, several fixed NAD+ concentrations, CoASH, and 3-ketoacyl-CoA thiolase.

raw_value_unit_evidence: Apparent Km 3.0 uM.


enzyme_display_name: 4-O-dimethylallyl-L-tyrosine synthase

substrate_name: benzyl diphosphate

enzyme: 4-O-dimethylallyl-L-tyrosine synthase

substrate: benzyl diphosphate


substrate_name: 2-pentenyl diphosphate

smiles: CC/C=C/COP(=O)(O)OP(=O)(O)O

substrate: 2-pentenyl diphosphate


organism: Plasmodium falciparum


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


organism: Vigna radiata var. radiata

substrate_name: L-glutamine

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

column_label: The abstract reports Km values of 3.8 mM for D-fructose 6-phosphate and 0.5 mM for L-glutamine.

raw_value_unit_evidence: Km raw_value=0.5 mM raw_unit=mM

row_label: Prose segment: L-glutamine Km

table_label: PubMed PMID 16658095 abstract

substrate: L-glutamine


substrate_name: D-fructose 6-phosphate

raw_value_unit_evidence: Km raw_value=3.8 mM raw_unit=mM

row_label: Prose segment: D-fructose 6-phosphate Km

substrate: D-fructose 6-phosphate


organism: Arabidopsis thaliana


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: N-acetylornithine (at pH 9.5 and 25 degrees Celsius)

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


substrate_name: ornithine (at pH 9.5 and 25 degrees Celsius)

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


organism: Pseudomonas sp.

assay_conditions_summary: pH 8


organism: Ovis aries


enzyme_display_name: 4-aminobutyrate aminotransferase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: 4-aminobutyrate aminotransferase


organism: Rattus norvegicus


substrate_name: beta-alanine

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

substrate: beta-alanine


enzyme_display_name: D-amino-acid transaminase

organism: Bacillus sp.

substrate_name: D-Alanine

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.

enzyme: D-amino-acid transaminase

substrate: D-Alanine


enzyme_display_name: 2,4-dinitrotoluene dioxygenase

organism: Burkholderia sp.

proof_lines:
2,4-DNT degradation
2,4-dinitrotoluene dioxygenase
Burkholderia

enzyme: 2,4-dinitrotoluene dioxygenase


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase

organism: Euglena gracilis

substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 6.5; cofactor CoA

enzyme: 3-hydroxyacyl-CoA dehydrogenase

substrate: acetoacetyl-CoA


organism: Leptosphaeria maculans

substrate_name: L-tryptophan

substrate: L-tryptophan


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

substrate_name: spermidine (at 78 degrees Celsius and at pH 7.5)

smiles: C(CCNCCCN)CN


substrate_name: 3-ethylpent-2-en-1-yl diphosphate

smiles: CCC(=CCOP(=O)(O)OP(=O)(O)O)CC

substrate: 3-ethylpent-2-en-1-yl diphosphate


enzyme_display_name: norspermine synthase

organism: Thermus thermophilus

proof_lines: Crystal Structures and Enzymatic Properties of a Triamine/Agmatine Aminopropyltransferase from Thermus thermophilus

enzyme: norspermine synthase


enzyme_display_name: Ophiobolin F synthase oblA

organism: Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107)

substrate_name: geranylgeranyl diphosphate

enzyme: Ophiobolin F synthase oblA


enzyme_display_name: Decaprenyl diphosphate synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: IPP (at pH 7.9 and 37 degrees Celsius)

column_label: PubMed abstract metric sentence gives Km for isopentenyl diphosphate as 89 microM, normalized to 0.089 mM

normalized_value_unit_evidence: PubMed abstract Km normalized_value=0.089 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: The Km value for isopentenyl diphosphate is 89 microM

row_label: Rv2361c isopentenyl diphosphate Km sentence

table_label: PubMed abstract

enzyme: Decaprenyl diphosphate synthase

substrate: IPP (at pH 7.9 and 37 degrees Celsius)


organism: Neurospora crassa


enzyme_display_name: Alanine--glyoxylate aminotransferase 2, mitochondrial

column_label: The paper's Km Values paragraph reports beta-alanine, 1.4 mM, among amino-donor Km values at pH 7.3.

raw_value_unit_evidence: Km raw_value=1.4 raw_unit=mM

row_label: beta-alanine as amino donor

table_label: Properties section. Km Values paragraph following Table III substrate-specificity context


enzyme_display_name: glutamine--pyruvate transaminase

organism: Mus musculus

enzyme: glutamine--pyruvate transaminase


enzyme_display_name: 4,4'-diapophytoene synthase

organism: Staphylococcus aureus

substrate_name: trans,trans-Farnesyl diphosphate

column_label: PMID 16269684 Table 2, DAP from FPP row, Vmax column 3.2 uM/h and FPP Km column 1.2 uM.

raw_value_unit_evidence: Table 2 reports DAP from FPP Vmax = 3.2 uM/h and FPP Km = 1.2 uM.

row_label: DAP from FPP

table_label: Table 2

enzyme: 4,4'-diapophytoene synthase

substrate: trans,trans-Farnesyl diphosphate


enzyme_display_name: UniProt Q988B8

organism: Mesorhizobium loti

substrate_name: L-glutamate

enzyme: UniProt Q988B8

substrate: L-glutamate


substrate_name: pyridoxamine 5'-phosphate

substrate: pyridoxamine 5'-phosphate


enzyme_display_name: pyridoxamine--pyruvate transaminase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/Y35H/V70K to reconstruct the assayed variant sequence.

enzyme: pyridoxamine--pyruvate transaminase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/Y35H/V70K/E212G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V70K with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V70R/F247C to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y35H/V70K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y35H/V70R/F247C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/V70K to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M2T/V70K/E212G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V70K/E212G with inferred residue-numbering offset +24 to reconstruct the assayed variant sequence.


substrate_name: L-Alanine

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

substrate: L-Alanine


organism: Escherichia coli (strain K12)

substrate_name: N-acetylornithine

substrate: N-acetylornithine


organism: Vitis vinifera

substrate_name: 2-keto-L-gulonate (in presence of NADPH)


substrate_name: hydroxypyruvate (in presence of NADPH)

substrate: hydroxypyruvate (in presence of NADPH)


substrate_name: glyoxylate (in presence of NADPH)

substrate: glyoxylate (in presence of NADPH)


substrate_name: pyruvate (in presence of NADPH)

substrate: pyruvate (in presence of NADPH)


enzyme_display_name: tryptophan-phenylpyruvate transaminase

organism: Pseudomonas sp.

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

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

enzyme: tryptophan-phenylpyruvate transaminase


smiles: CCCCC(=O)C(=O)[O-]


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: L-leucine

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

substrate: L-leucine


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-tryptophan


substrate_name: L-norleucine

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

substrate: L-norleucine


substrate_name: L-valine

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

substrate: L-valine


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-alanine

substrate: L-alanine


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor CoA

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH


substrate_name: 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

proof_lines:
Drosophila 17beta-HSD10
isoursodeoxycholate
bile-acid substrate class


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH

proof_lines:
Drosophila 17beta-HSD10
hydroxyacyl-CoA dehydrogenase
acetoacetyl-CoA


substrate_name: NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)

proof_lines:
Drosophila 17beta-HSD10
C21 steroids
aldosterone


enzyme_display_name: pyridoxamine-pyruvate transaminase

enzyme: pyridoxamine-pyruvate transaminase


substrate_name: pyridoxal

substrate: pyridoxal


substrate_name: pyridoxamine

proof_lines: with 3-hydroxy-4-aminomethylpyridine, pH 8.9, 25°C

substrate: pyridoxamine


proof_lines: with omega-methylpyridoxal, pH 8.9, 25°C


enzyme_display_name: UniProt P9WQ77

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WQ77


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: (2-aminoethyl)phosphonate (at 25 degrees Celsius, pH 8.5)

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


substrate_name: pyruvate (at 25 degrees Celsius, pH 8.5)


substrate_name: 2-phosphonoacetaldehyde (at 25 degrees Celsius, pH 8.5)


substrate_name: L-alanine (at 25 degrees Celsius, pH 8.5)


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


substrate_name: pyruvate


enzyme_display_name: UniProt Q72LL6

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

enzyme: UniProt Q72LL6


enzyme_display_name: branched-chain-amino-acid transaminase

organism: Enterobacter sp.

substrate_name: trimethylpyruvate

enzyme: branched-chain-amino-acid transaminase

substrate: trimethylpyruvate


substrate_name: 3-methyl-2-oxovaleric acid

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

substrate: 3-methyl-2-oxovaleric acid


substrate_name: 3-methyl-2-oxobutyric acid

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

substrate: 3-methyl-2-oxobutyric acid


substrate_name: 4-methyl-2-oxovaleric acid

substrate: 4-methyl-2-oxovaleric acid


organism: [Brevibacterium] flavum


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: prephenate

substrate: prephenate


substrate_name: L-glutamate

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

substrate: L-glutamate


enzyme_display_name: UniProt D0LR31

organism: Haliangium ochraceum

substrate_name: L-norvaline

enzyme: UniProt D0LR31


substrate_name: L-isoleucine

substrate: L-isoleucine


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-valine


enzyme_display_name: UniProt D1CCW1

organism: Thermobaculum terrenum

enzyme: UniProt D1CCW1


enzyme_display_name: UniProt O15382

organism: Homo sapiens

enzyme: UniProt O15382


enzyme_display_name: UniProt P0AB80

organism: Escherichia coli

enzyme: UniProt P0AB80


proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=37°C, pH=8


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


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


enzyme_display_name: UniProt O86428

organism: Pseudomonas aeruginosa

enzyme: UniProt O86428


enzyme_display_name: UniProt P9WQ75

enzyme: UniProt P9WQ75


organism: Nicotiana tabacum

substrate_name: pyridoxamine


organism: Oryctolagus cuniculus

substrate_name: Oxaloacetate; Pyridoxamine

substrate: Oxaloacetate; Pyridoxamine


enzyme_display_name: pyridoxamine-oxaloacetate transaminase

substrate_name: oxaloacetate

enzyme: pyridoxamine-oxaloacetate transaminase

substrate: oxaloacetate


proof_lines: with omega-methylpyridoxamine, pH 8.9, 25°C


enzyme_display_name: UniProt P21549

substrate_name: L-cysteine

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

enzyme: UniProt P21549

substrate: L-cysteine


enzyme_display_name: alanine--glyoxylate transaminase

substrate_name: glyoxylate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I56N to reconstruct the assayed variant sequence.

smiles: O=CC(=O)O

enzyme: alanine--glyoxylate transaminase

substrate: glyoxylate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P11R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P11R/I56N to reconstruct the assayed variant sequence.


substrate_name: L-alanine


organism: Sus scrofa

substrate_name: Pyridoxamine; Oxaloacetate

substrate: Pyridoxamine; Oxaloacetate


organism: Rattus norvegicus

proof_lines: somewhat higher at very high levels of pyridoxamine, 14 mM


organism: Mesorhizobium loti

substrate_name: pyridoxamine 5'-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E68G with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9

substrate: pyridoxamine 5'-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E68A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R336A to reconstruct the assayed variant sequence.


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt P23721

enzyme: UniProt P23721


substrate_name: L-homoserine

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

substrate: L-homoserine


enzyme_display_name: UniProt Q59196

organism: Niallia circulans

proof_lines:
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=-----, pH=9

enzyme: UniProt Q59196


enzyme_display_name: UniProt Q60I38

organism: Entamoeba histolytica

enzyme: UniProt Q60I38


substrate_name: O-phospho-L-serine

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8.5

substrate: O-phospho-L-serine


enzyme_display_name: UniProt A0A0A7I435

organism: Bifidobacterium catenulatum subsp. kashiwanohense

enzyme: UniProt A0A0A7I435


substrate_name: taurine

substrate: taurine


enzyme_display_name: UniProt A0A1D8PMC5

organism: Candida albicans

enzyme: UniProt A0A1D8PMC5


substrate_name: L-tryptophan

substrate: L-tryptophan


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


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: alpha-aminoadipate

substrate: alpha-aminoadipate


enzyme_display_name: pyridoxamine-pyruvate transaminase

substrate_name: L-glutamate

enzyme: pyridoxamine-pyruvate transaminase

substrate: L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70K with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35H/V70K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/Y35H/V70K/E212G to reconstruct the assayed variant sequence.

proof_lines: M2T/Y35H/V70K/E212G mutant protein, pH 9.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/Y35H/V70K to reconstruct the assayed variant sequence.

proof_lines: M2T/Y35H/V70K mutant protein, pH 9.0, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/V70K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70R/F247C to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70K/E212G with inferred residue-numbering offset +24 to reconstruct the assayed variant sequence.