organism: Arabidopsis thaliana


enzyme_display_name: phycobiliprotein cysteine-84 phycobilin lyase

organism: Anabaena sp.

source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature R147Q to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'R147Q'; column 'Km (uM)' = 2.29; column 'kcat x 10^5 (s-1)' = 1.69; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.74.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.69 in the column headed kcat x 10^5 (s-1), so the constant is 1.69 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000169 s^(-1); the exported value is 0.0000169 s^(-1). Km: printed Table 1 cell 2.29 uM; 2.29 / 1000 = 0.00229 mM; the paper value is 0.00229 mM; the exported value is 0.00229 mM. kcat/Km: printed Table 1 cell 0.74 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.74 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.74 x 10^-5 x 1000 = 0.0074 s^-1 mM^-1; the paper value is 0.0074 s^(-1)*mM^(-1); the exported value is 0.007379912663755459 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'R147Q': Km = 2.29 uM; kcat = 1.69 x 10^-5 s^-1; printed kcat/Km = 0.74 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'R147Q'

data_origin: experimental

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature H80L to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'H80L'; column 'Km (uM)' = 1.70; column 'kcat x 10^5 (s-1)' = 2.46; column 'kcat/Km x 10^5 (s-1 uM-1)' = 1.47.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.46 in the column headed kcat x 10^5 (s-1), so the constant is 2.46 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000246 s^(-1); the exported value is 0.0000246 s^(-1). Km: printed Table 1 cell 1.70 uM; 1.70 / 1000 = 0.0017 mM; the paper value is 0.0017 mM; the exported value is 0.0017 mM. kcat/Km: printed Table 1 cell 1.47 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 1.47 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.47 x 10^-5 x 1000 = 0.0147 s^-1 mM^-1; the paper value is 0.0147 s^(-1)*mM^(-1); the exported value is 0.014470588235294119 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'H80L': Km = 1.70 uM; kcat = 2.46 x 10^-5 s^-1; printed kcat/Km = 1.47 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'H80L'

enzyme: phycobiliprotein cysteine-84 phycobilin lyase


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature H21T/H22V to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'H21T/H22V'; column 'Km (uM)' = 1.34; column 'kcat x 10^5 (s-1)' = 0.95; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.71.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.95 in the column headed kcat x 10^5 (s-1), so the constant is 0.95 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000095 s^(-1); the exported value is 0.0000095 s^(-1). Km: printed Table 1 cell 1.34 uM; 1.34 / 1000 = 0.00134 mM; the paper value is 0.00134 mM; the exported value is 0.00134 mM. kcat/Km: printed Table 1 cell 0.71 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.71 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.71 x 10^-5 x 1000 = 0.0071 s^-1 mM^-1; the paper value is 0.0071 s^(-1)*mM^(-1); the exported value is 0.0070895522388059705 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'H21T/H22V': Km = 1.34 uM; kcat = 0.95 x 10^-5 s^-1; printed kcat/Km = 0.71 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'H21T/H22V'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W69M with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'Wild type'; column 'Km (uM)' = 1.14; column 'kcat x 10^5 (s-1)' = 2.50; column 'kcat/Km x 10^5 (s-1 uM-1)' = 2.19.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.50 in the column headed kcat x 10^5 (s-1), so the constant is 2.50 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.000025 s^(-1); the exported value is 0.000025 s^(-1). Km: printed Table 1 cell 1.14 uM; 1.14 / 1000 = 0.00114 mM; the paper value is 0.00114 mM; the exported value is 0.00114 mM. kcat/Km: printed Table 1 cell 2.19 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 2.19 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.19 x 10^-5 x 1000 = 0.0219 s^-1 mM^-1; the paper value is 0.0219 s^(-1)*mM^(-1); the exported value is 0.02192982456140351 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'Wild type': Km = 1.14 uM; kcat = 2.50 x 10^-5 s^-1; printed kcat/Km = 2.19 x 10^-5 s^-1 uM^-1.

row_label: Table 1, row 'Wild type'


enzyme_display_name: hercynylcysteine S-oxide lyase

organism: Mycolicibacterium smegmatis

source_db: brenda

kcat_over_km_display: Not reported

assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: hercynylcysteine S-oxide lyase

source: brenda


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.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature R18V to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'R18V'; column 'Km (uM)' = 2.54; column 'kcat x 10^5 (s-1)' = 0.73; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.29.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.73 in the column headed kcat x 10^5 (s-1), so the constant is 0.73 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000073 s^(-1); the exported value is 0.0000073 s^(-1). Km: printed Table 1 cell 2.54 uM; 2.54 / 1000 = 0.00254 mM; the paper value is 0.00254 mM; the exported value is 0.00254 mM. kcat/Km: printed Table 1 cell 0.29 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.29 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.29 x 10^-5 x 1000 = 0.0029 s^-1 mM^-1; the paper value is 0.0029 s^(-1)*mM^(-1); the exported value is 0.002874015748031496 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'R18V': Km = 2.54 uM; kcat = 0.73 x 10^-5 s^-1; printed kcat/Km = 0.29 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'R18V'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature C63T to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'C63T'; column 'Km (uM)' = 1.55; column 'kcat x 10^5 (s-1)' = 2.81; column 'kcat/Km x 10^5 (s-1 uM-1)' = 1.81.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.81 in the column headed kcat x 10^5 (s-1), so the constant is 2.81 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000281 s^(-1); the exported value is 0.000028 s^(-1). Km: printed Table 1 cell 1.55 uM; 1.55 / 1000 = 0.00155 mM; the paper value is 0.00155 mM; the exported value is 0.00155 mM. kcat/Km: printed Table 1 cell 1.81 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 1.81 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.81 x 10^-5 x 1000 = 0.0181 s^-1 mM^-1; the paper value is 0.0181 s^(-1)*mM^(-1); the exported value is 0.01806451612903226 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'C63T': Km = 1.55 uM; kcat = 2.81 x 10^-5 s^-1; printed kcat/Km = 1.81 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'C63T'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature R169L to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'R169L'; column 'Km (uM)' = 1.39; column 'kcat x 10^5 (s-1)' = 1.80; column 'kcat/Km x 10^5 (s-1 uM-1)' = 1.29.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.80 in the column headed kcat x 10^5 (s-1), so the constant is 1.80 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.000018 s^(-1); the exported value is 0.000018 s^(-1). Km: printed Table 1 cell 1.39 uM; 1.39 / 1000 = 0.00139 mM; the paper value is 0.00139 mM; the exported value is 0.00139 mM. kcat/Km: printed Table 1 cell 1.29 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 1.29 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.29 x 10^-5 x 1000 = 0.0129 s^-1 mM^-1; the paper value is 0.0129 s^(-1)*mM^(-1); the exported value is 0.012949640287769786 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'R169L': Km = 1.39 uM; kcat = 1.80 x 10^-5 s^-1; printed kcat/Km = 1.29 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'R169L'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature W75S to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'W75S'; column 'Km (uM)' = 1.44; column 'kcat x 10^5 (s-1)' = 1.06; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.74.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.06 in the column headed kcat x 10^5 (s-1), so the constant is 1.06 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000106 s^(-1); the exported value is 0.0000106 s^(-1). Km: printed Table 1 cell 1.44 uM; 1.44 / 1000 = 0.00144 mM; the paper value is 0.00144 mM; the exported value is 0.00144 mM. kcat/Km: printed Table 1 cell 0.74 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.74 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.74 x 10^-5 x 1000 = 0.0074 s^-1 mM^-1; the paper value is 0.0074 s^(-1)*mM^(-1); the exported value is 0.007361111111111111 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'W75S': Km = 1.44 uM; kcat = 1.06 x 10^-5 s^-1; printed kcat/Km = 0.74 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'W75S'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8YZ70 and applied mutation signature H22V to reconstruct the assayed variant sequence.

column_label: Table 1: Relative activities and enzyme kinetic constants of wild-type and mutant lyase, CpcS1, and the amount of chromophore bound to lyase (J. Biol. Chem. 2009, 284(52):36405-36414), enzyme-form row 'H22V'; column 'Km (uM)' = 1.38; column 'kcat x 10^5 (s-1)' = 1.19; column 'kcat/Km x 10^5 (s-1 uM-1)' = 0.86.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.19 in the column headed kcat x 10^5 (s-1), so the constant is 1.19 x 10^-5 s^-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 0.0000119 s^(-1); the exported value is 0.0000119 s^(-1). Km: printed Table 1 cell 1.38 uM; 1.38 / 1000 = 0.00138 mM; the paper value is 0.00138 mM; the exported value is 0.00138 mM. kcat/Km: printed Table 1 cell 0.86 in the column headed kcat/Km x 10^5 (s-1 uM-1), so the constant is 0.86 x 10^-5 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.86 x 10^-5 x 1000 = 0.0086 s^-1 mM^-1; the paper value is 0.0086 s^(-1)*mM^(-1); the exported value is 0.008623188405797101 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme-form row 'H22V': Km = 1.38 uM; kcat = 1.19 x 10^-5 s^-1; printed kcat/Km = 0.86 x 10^-5 s^-1 uM^-1.

row_label: Table 1, mutant row 'H22V'


enzyme_display_name: cysteine-S-conjugate beta-lyase

organism: Escherichia coli

substrate_name: L-cystathionine

verification_status: unverified

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

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

enzyme: cysteine-S-conjugate beta-lyase

substrate: L-cystathionine

status: unverified


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

proof_lines: pH 8.5, 25°C, recombinant wild-type enzyme


substrate_name: Unknown

kcat_display: Not reported

km_display: Not reported

ki_unit: mM

substrate: Unknown


enzyme_display_name: D-cysteine desulfhydrase

substrate_name: DL-selenocystine

smiles: C(C(C(=O)O)N)[Se][Se]CC(C(=O)O)N

proof_lines: 30°C, pH 8.0, based on the concentration of the D-isomer, Escherichia coli

enzyme: D-cysteine desulfhydrase

substrate: DL-selenocystine


substrate_name: DL-lanthionine

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

substrate: DL-lanthionine


substrate_name: S-phenyl-D-cysteine

substrate: S-phenyl-D-cysteine


substrate_name: S-n-propyl-D-cysteine

substrate: S-n-propyl-D-cysteine


substrate_name: S-n-butyl-D-cysteine

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

substrate: S-n-butyl-D-cysteine


substrate_name: D-Cystine

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

substrate: D-Cystine


substrate_name: S-benzyl-D-cysteine

substrate: S-benzyl-D-cysteine


substrate_name: D-allocystathionine

substrate: D-allocystathionine


substrate_name: S-methyl-D-cysteine

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

substrate: S-methyl-D-cysteine


substrate_name: S-carboxymethyl-D-cysteine

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

substrate: S-carboxymethyl-D-cysteine


enzyme_display_name: protoporphyrin ferrochelatase

organism: Rattus norvegicus

substrate_name: protoporphyrin IX

proof_lines: wild type enzyme, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C

proof_lines: wild type enzyme, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C

enzyme: protoporphyrin ferrochelatase

substrate: protoporphyrin IX


proof_lines: mutant enzyme F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C

proof_lines: mutant enzyme F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


proof_lines: mutant enzyme S143T/F323L, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C

proof_lines: mutant enzyme S143T/F323L, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


proof_lines: mutant enzyme S143T, with Ni2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C

proof_lines: mutant enzyme S143T, with Fe2+ as cosubstrate, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


proof_lines: wild type enzyme, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


proof_lines: mutant enzyme S143T, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


proof_lines: mutant enzyme S143T/F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


proof_lines: mutant enzyme F323L, 0.1 M Tris-acetate, pH 8.0, 0.5 M NaCl, 0.1% (v/v) Tween 80, at 30°C


enzyme_display_name: methionine gamma-lyase

organism: Pseudomonas putida

substrate_name: L-methionine

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

enzyme: methionine gamma-lyase

substrate: L-methionine


substrate_name: L-cysteine

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

substrate: L-cysteine


substrate_name: DL-homocysteine

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

substrate: DL-homocysteine


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


organism: Homo sapiens

substrate_name: mesoporphyrin IX

proof_lines: mutant Q139L, heterodimer, room temperature

proof_lines: mutant Q139L, homodimer, room temperature

substrate: mesoporphyrin IX


proof_lines: mutant F260L, heterodimer, room temperature

proof_lines: mutant F260L, homodimer, room temperature


proof_lines: mutant Y191H, homodimer, room temperature

proof_lines: mutant Y191H, heterodimer, room temperature


proof_lines: mutant S264L, heterodimer, room temperature


organism: Citrobacter freundii

substrate_name: L-Vinylglycine

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

substrate: L-Vinylglycine


substrate_name: O-acetyl-DL-homoserine

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

substrate: O-acetyl-DL-homoserine


substrate_name: L-methionine sulfone

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

substrate: L-methionine sulfone


substrate_name: L-methionine sulfoxide

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

proof_lines: pH and temperature not specified in the publication

substrate: L-methionine sulfoxide


substrate_name: L-alanine

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

substrate: L-alanine


substrate_name: L-norvaline

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

substrate: L-norvaline


organism: Porphyromonas gingivalis

substrate_name: D-methionine

proof_lines:
at pH 7.5 and 37°C
pH 8.0, 30°C, recombinant enzyme
pH 7.5, 37°C

substrate: D-methionine


substrate_name: L-homoserine lactone

substrate: L-homoserine lactone


substrate_name: L-homoserine

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

substrate: L-homoserine


substrate_name: L-ethionine

substrate: L-ethionine


proof_lines:
at pH 7.5 and 37°C
pH 7.5, 37°C


substrate_name: S-ethyl-L-homocysteine

substrate: S-ethyl-L-homocysteine


substrate_name: S-ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: S-Benzyl-L-cysteine

substrate: S-Benzyl-L-cysteine


substrate_name: DL-homoserine

substrate: DL-homoserine


substrate_name: L-Gly(vinyl)

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

substrate: L-Gly(vinyl)


substrate_name: L-cysteine

proof_lines:
30°C, pH 8.0
recombinant enzyme

substrate: L-cysteine


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


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


enzyme_display_name: leukotriene-C4 synthase

substrate_name: leukotriene A4 methyl ester

proof_lines:
mutant R104A, pH 7.0, 22°C
mutant R104A, pH 8.0, 22°C
mutant R104A, pH 9.0, 22°C

enzyme: leukotriene-C4 synthase

substrate: leukotriene A4 methyl ester


proof_lines:
mutant R31A, pH 8.0, 22°C
mutant R31A, pH 7.0, 22°C
mutant R31A, pH 9.0, 22°C


substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

proof_lines:
mutant R31A, pH 9.0, 22°C
mutant R31A, pH 7.0, 22°C
mutant R31A, pH 8.0, 22°C

substrate: glutathione


proof_lines:
wild-type, pH 7.0, 22°C
wild-type, pH 8.0, 22°C
wild-type, pH 9.0, 22°C


proof_lines:
wild-type, pH 9.0, 22°C
wild-type, pH 7.0, 22°C
wild-type, pH 8.0, 22°C


organism: Clostridium tetani


substrate_name: L-methionine

substrate: L-methionine


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)


organism: Clostridium sporogenes


enzyme_display_name: S-ribosylhomocysteine lyase

organism: Vibrio harveyi

enzyme: S-ribosylhomocysteine lyase


substrate_name: S-ribosylhomocysteine

substrate: S-ribosylhomocysteine


enzyme_display_name: dichloromethane dehalogenase

organism: Methylorubrum rhodesianum

substrate_name: Dichloromethane

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

smiles: C(Cl)Cl

enzyme: dichloromethane dehalogenase

substrate: Dichloromethane


enzyme_display_name: S-carboxymethylcysteine synthase

substrate_name: thioglycolate

sequence_source: multiple

source_databases_merged: brenda uniprot

enzyme: S-carboxymethylcysteine synthase

substrate: thioglycolate


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


enzyme_display_name: UniProt P9WQ35

organism: Mycobacterium tuberculosis

substrate_name: ATP

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P9WQ35

substrate: ATP

source: skid


enzyme_display_name: UniProt A0A1Y2HEJ3

organism: Catenaria anguillulae

substrate_name: GTP

enzyme: UniProt A0A1Y2HEJ3

substrate: GTP


enzyme_display_name: UniProt Q02108

enzyme: UniProt Q02108


organism: Neurospora crassa

substrate_name: S-(Hercyn-2-yl)-L-cysteine S-oxide

kcat_over_km_origin: calculated

substrate: S-(Hercyn-2-yl)-L-cysteine S-oxide


substrate_name: porphyrin

substrate: porphyrin


substrate_name: L-cystathionine

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

substrate: L-cystathionine


substrate_name: L-cystine

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

substrate: L-cystine


substrate_name: L-djenkolate

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

substrate: L-djenkolate


substrate_name: L-meso-lanthionine

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

substrate: L-meso-lanthionine


substrate_name: L-homolanthionine

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

substrate: L-homolanthionine


enzyme_display_name: L-3-cyanoalanine synthase

organism: Arabidopsis thaliana

enzyme: L-3-cyanoalanine synthase


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


substrate_name: KCN

substrate: KCN


substrate_name: L-cysteine

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

substrate: L-cysteine


enzyme_display_name: adenylate cyclase

organism: Synechocystis sp.

mutation_signature: truncated Cya1

mutation_type: truncation

assay_conditions_summary: pH 7.5; 300.15 K; cofactor ATP

enzyme: adenylate cyclase


mutation_signature: truncated Cya1 / 50 mM NaHCO3 truncated Cya1

proof_lines: truncated Cya1, pH 7.5, 27°C, 50 mM NaHCO3


enzyme_display_name: 3-chloro-D-alanine dehydrochlorinase

substrate_name: D-cysteine

enzyme: 3-chloro-D-alanine dehydrochlorinase

substrate: D-cysteine


substrate_name: L-ethionine

substrate: L-ethionine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


substrate_name: S-ethyl-L-cysteine

substrate: S-ethyl-L-cysteine


substrate_name: L-methionine sulfone

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

substrate: L-methionine sulfone


substrate_name: L-Vinylglycine

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

substrate: L-Vinylglycine


organism: Alternaria solani

substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


organism: Haloactinopolyspora alba

assay_conditions_summary: pH 10; 313.15 K; cofactor ATP


substrate_name: NaHS

substrate: NaHS


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: beta-Chloro-D-alanine

proof_lines: recombinant His6-tagged enzyme, pH and temperature not specified in the publication

substrate: beta-Chloro-D-alanine


organism: Nocardia erythropolis


organism: Ruditapes philippinarum


organism: Rattus norvegicus

proof_lines: after activation of soluble AC with the stimulatory G protein alpha protein and GTP-gamma-S in the presence of Mn2+

proof_lines: after activation of soluble AC with the stimulatory G protein alpha protein and GTP-gamma-S in the presence of Mg2+


proof_lines:
in the presence of Cl-
in the presence of HCO3-
native Cya1, pH 7.5, 27°C


enzyme_display_name: UniProt Q9CAK8

enzyme: UniProt Q9CAK8


organism: Synechocystis sp. PCC 6803


organism: Pseudomonas putida

smiles: S


organism: Thermobifida halotolerans

assay_conditions_summary: pH 10; 318.15 K; cofactor ATP


enzyme_display_name: guanylate cyclase

substrate_name: GTP

proof_lines: pH 7.5, 22°C, wild-type enzyme, mutant enzyme E497K/C566D

proof_lines: pH 7.5, 22°C, wild-type enzyme, wild-type enzyme

enzyme: guanylate cyclase

substrate: GTP


organism: Mammalia

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: recombinant form VC1-IIC2, 30°C, pH 7.4, 10 mM Mn2+, 0.1 mM forskolin, stimulatory G protein alpha subunits guanosine 5'-(gamma-thio)triphosphate

proof_lines: recombinant form VC1-IIC2, 30°C, pH 7.4, 10 mM MnCl, 0.1 mM forskolin


organism: Ambystoma tigrinum


organism: Escherichia coli


organism: Niallia circulans

substrate_name: Dichloromethane

substrate: Dichloromethane


organism: Homo sapiens

proof_lines: in 10 mM MnCl2, 100 mM KCl, 25 mM HEPES/NaOH, pH 7.4, at 30°C

proof_lines: in the presence of 1 mM ATP, isozyme GC-A, in 25 mM HEPES (pH 7.4), 50 mM NaCl, 0.1% (w/v) bovine serum albumin, 0.5 mM isobutylmethyl xanthine, 1 mM EDTA, 0.5 mM microcystin and 5 mM MgCl2, at 37°C

proof_lines: in the presence of 1 mM ATP, isozyme GC-B, in 25 mM HEPES (pH 7.4), 50 mM NaCl, 0.1% (w/v) bovine serum albumin, 0.5 mM isobutylmethyl xanthine, 1 mM EDTA, 0.5 mM microcystin and 5 mM MgCl2, at 37°C


organism: Leishmania donovani

proof_lines:
purified enzyme
recombinant enzyme


organism: Mus musculus

proof_lines: nonstimulated isozyme RetGC1, in 30 mM MOPS-KOH (pH 7.2), 60 mM KCl, 4 mM NaCl, 1 mM dithiothreitol, 2 mM Ca2+/EGTA buffer, at 30°C

proof_lines: nonstimulated isozyme RetGC2, in 30 mM MOPS-KOH (pH 7.2), 60 mM KCl, 4 mM NaCl, 1 mM dithiothreitol, 2 mM Ca2+/EGTA buffer, at 30°C

proof_lines: isozyme RetGC1, stimulated by guanylyl cyclase activating protein 2, in 30 mM MOPS-KOH (pH 7.2), 60 mM KCl, 4 mM NaCl, 1 mM dithiothreitol, 2 mM Ca2+/EGTA buffer, at 30°C


organism: Yersinia pestis

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP


enzyme_display_name: cytidylate cyclase

substrate_name: CTP

enzyme: cytidylate cyclase

substrate: CTP


organism: Ipomoea nil


organism: Bacillus anthracis

proof_lines: in the presence of 5 mM Mg2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C

proof_lines: in the presence of 5 mM Mn2+, in 75 mM HEPES-NaOH, pH 7.4, at 37°C


substrate_name: Unknown

substrate: Unknown


organism: Bordetella pertussis


proof_lines:
in 75 mM HEPES-NaOH, pH 7.4, at 37°C
in 75 mM HEPES-NaOH, pH 7.4,at 37°C


proof_lines: mutant VC1-A406P+IIC2-I1006V, 30°C, pH 7.4, 10 mM MnCl, 0.1 mM forskolin


proof_lines: mutant VC1-A409P+IIC2, 30°C, pH 7.4, 10 mM MnCl, 0.1 mM forskolin


proof_lines: mutant VC1+IIC2-I1006V, 30°C, pH 7.4, 10 mM MnCl, 0.1 mM forskolin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S506E with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant S506E, temperature not specified in the publication, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S506A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant S506A, temperature not specified in the publication, pH not specified in the publication


enzyme_display_name: pancreatic ribonuclease

organism: Gallus gallus

substrate_name: tRNA

assay_conditions_summary: pH 7

enzyme: pancreatic ribonuclease

substrate: tRNA


enzyme_display_name: ribonuclease T2

substrate_name: RNA

enzyme: ribonuclease T2

substrate: RNA


organism: Magallana gigas

substrate_name: UpG

substrate: UpG


substrate_name: GpG

substrate: GpG


substrate_name: ApG

substrate: ApG


substrate_name: CpG

substrate: CpG


organism: Blastocladiella emersonii

proof_lines: pH 7.5, 22°C, wild-type enzyme, wild-type enzyme


organism: Methylophilus sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V18I with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.


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

proof_lines:
pH 8.5, wild-type
30°C, pH 8.5, wild-type
pH 8.2, wild-type


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -15, so it is treated as a source-provided variant sequence.


organism: Momordica charantia

substrate_name: CpU

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N71T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: CpU


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R74S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V72L with inferred residue-numbering offset +1 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.

proof_lines:
wild-type enzyme, pH 6.5, 37°C
wild-type enzyme


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.


source_db: uniprot

proof_lines: kcat is 745 min(-1) with CpU as substrate.

source: uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K87A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.


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


organism: Methylorubrum rhodesianum

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


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


organism: Oncorhynchus keta

substrate_name: GpC

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

substrate: GpC


organism: Rhizopus niveus


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y6A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y6F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: Dibromomethane

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

smiles: C(Br)Br

substrate: Dibromomethane


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +14, so it is treated as a source-provided variant sequence.


proof_lines:
30°C, pH 8.5, wild-type
pH 8.2, wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F1078S with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

assay_conditions_summary: 303.15 K; cofactor ATP


substrate_name: UpC

substrate: UpC


substrate_name: ApU

substrate: ApU


enzyme_display_name: hercynylcysteine S-oxide lyase

organism: Mycolicibacterium smegmatis

substrate_name: S-(hercyn-2-yl)-L-cysteine S-oxide

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: hercynylcysteine S-oxide lyase

substrate: S-(hercyn-2-yl)-L-cysteine S-oxide


enzyme_display_name: cyclic pyranopterin monophosphate synthase

organism: Escherichia coli

proof_lines: His-tagged wild-type, pH not specified in the publication, temperature not specified in the publication


organism: Anabaena sp.

substrate_name: ATP

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

proof_lines: 37°C, pH 7.5, recombinant cyaB1 AC, in the presence of 2 mM Mn2+ and 0.1 mM cAMP

proof_lines: recombinant CyaB1-maltose binding protein fusion

substrate: ATP


organism: Homo sapiens

substrate_name: GTP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V902L to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant V902L enzyme in presence or absence of activator GCAP2

proof_lines: pH and temperature not specified in the publication, mutant V902L enzyme in presence of activator GCAP1

proof_lines: pH and temperature not specified in the publication, mutant V902L enzyme in presence of activator GCAP2

substrate: GTP


enzyme_display_name: FAD-AMP lyase (cyclizing)

organism: Rattus norvegicus

substrate_name: GDP-alpha-L-fucose with manganese

enzyme: FAD-AMP lyase (cyclizing)

substrate: GDP-alpha-L-fucose with manganese


organism: Aotus trivirgatus

substrate_name: yeast tRNA (in the presence of 40 mM sodium phosphate at pH 7.0)


substrate_name: cyclic 2',3'-cytidine monophosphate

substrate: cyclic 2',3'-cytidine monophosphate


organism: Macaca fascicularis

substrate: yeast tRNA (in the presence of 40 mM sodium phosphate at pH 7.0)


organism: Pongo pygmaeus


organism: Arabidopsis thaliana

substrate_name: Ser/Thr peptide 1 for the protein serine-threonine kinase activity


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W117Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Bacillus anthracis

substrate_name: Unknown

proof_lines: forward reaction, 2 microM free Ca2+, pH 7.2, 30°C

proof_lines: forward reaction, 0.1 microM free Ca2+, pH 7.2, 30°C

proof_lines: reverse reaction, 0.1 microM free Ca2+, pH 7.2, 30°C

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H351F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H351N to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; cofactor ATP


verification_status: verified

column_label: Abstract reports the isolated intermediate was converted to cPMP by MoaC or its human homologue MOCS1B with high specificities, Km < 0.060 microM and 0.79+/-0.24 microM for MoaC and MOCS1B, respectively.

raw_value_unit_evidence: Km raw_value=0.79+/-0.24 microM raw_unit=microM

row_label: human MOCS1B / cyclic dihydroguanosine triphosphate intermediate

table_label: PubMed XML abstract PMID 23627491

enzyme: cyclic pyranopterin monophosphate synthase

status: verified


organism: Lithobates pipiens

assay_conditions_summary: pH 6


mutation_signature: but the preserved evidence still stops at an abstract-only paper context and unstructured notes. Promoting it would overstate what the source actually proves.

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

smiles: C(Cl)I


substrate_name: Diiodomethane

smiles: C(I)I

substrate: Diiodomethane


substrate_name: Dichloromethane

smiles: C(Cl)Cl

substrate: Dichloromethane


organism: Dictyostelium discoideum

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


organism: Euglena gracilis


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


substrate_name: pNP-decanoate

proof_lines: kcat is 140 min(-1) for lipolytic activity. kcat is 355 min(-1) for N-terminal lipolytic domain and lipolytic activity.

substrate: pNP-decanoate


organism: Escherichia coli (strain K12)

substrate_name: CDP-ME2P (at pH 7.4)

proof_lines: kcat is 61 min(-1) for CDP-ME2P (at pH 7.4).

substrate: CDP-ME2P (at pH 7.4)


proof_lines:
22°C, pH 8.0
guanylyl cyclase GCA
soluble guanylyl cyclase sGC


organism: Bos taurus

substrate_name: cytidine-2',3'-cyclic monophosphate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N34A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

substrate: cytidine-2',3'-cyclic monophosphate


substrate_name: poly(A)-poly(U)

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R39A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

substrate: poly(A)-poly(U)


organism: Rhizopus niveus

substrate_name: CpC

substrate: CpC


enzyme_display_name: ribonuclease U2

organism: Ustilago sphaerogena

substrate_name: RNA containing adenosine 3'-(methyl phosphate)

proof_lines:
37°C, pH 4.5, recombinant enzyme
37°C, pH 4.5, fungal enzyme

enzyme: ribonuclease U2


organism: Plasmodium falciparum (isolate HB3)


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature H77A to reconstruct the assayed variant sequence.

proof_lines: mutant H77A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K51A to reconstruct the assayed variant sequence.

proof_lines: mutant K51A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E112A to reconstruct the assayed variant sequence.

proof_lines: mutant E112A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature E114A to reconstruct the assayed variant sequence.

proof_lines: mutant E114A, pH not specified in the publication, temperature not specified in the publication


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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
kcat is 0.56 min(-1).

source_databases_merged: skid uniprot


substrate_name: 2',3'-Cyclic CMP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F46L with inferred residue-numbering offset +26 to reconstruct the assayed variant sequence.

substrate: 2',3'-Cyclic CMP


enzyme_display_name: dichloromethane dehalogenase

organism: Methylophilus sp.

enzyme: dichloromethane dehalogenase


organism: Glutamicibacter nicotianae

substrate_name: deoxycAMP

column_label: Page 1971 prose states the Km values for cyclic AMP and cyclic dAMP are 14 mM and 13 mM respectively.

raw_value_unit_evidence: Km for cyclic dAMP = 13 mM

row_label: reverse reaction; substrate cyclic dAMP

table_label: Page 1971 Catalytic Properties prose; Table IV condition context

substrate: deoxycAMP


organism: Homo sapiens

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


organism: Rattus norvegicus

substrate_name: ATP (in the presence of 5.74 mM free Mg(2+) and 1 muM exogenous calmodulin) (isoform 1)


substrate_name: CDP-ME2P (at pH 8 and at 37 degrees Celsius)


substrate_name: ATP

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 7.2, 2 microM free Ca2+
30°C, pH 7.2, 0.1 microM free Ca2+


substrate_name: FAD with manganese

assay_conditions_summary: pH 7.5; cofactor FAD

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: FAD; column label: Mn2+-dependent activities / Km (uM); raw value 8.8 uM; normalized value 0.0088 mM.

normalized_value_unit_evidence: Km=0.0088 mM after converting 8.8 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row FAD; Mn2+-dependent Km column = 8.8 uM.

row_label: FAD row / Mn2+-dependent activities Km column

substrate: FAD with manganese


substrate_name: ADP-glucose with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: ADP-glucose; column label: Mn2+-dependent activities / Km (uM); raw value 12.5 uM; normalized value 0.0125 mM.

normalized_value_unit_evidence: Km=0.0125 mM after converting 12.5 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row ADP-glucose; Mn2+-dependent Km column = 12.5 uM.

row_label: ADP-glucose row / Mn2+-dependent activities Km column

substrate: ADP-glucose with manganese


substrate_name: UDP-glucose with manganese

assay_conditions_summary: cofactor FAD

substrate: UDP-glucose with manganese


substrate_name: UDP-xylose with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: UDP-xylose; column label: Mn2+-dependent activities / Km (uM); raw value 714 uM; normalized value 0.714 mM.

normalized_value_unit_evidence: Km=0.714 mM after converting 714 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row UDP-xylose; Mn2+-dependent Km column = 714 uM.

row_label: UDP-xylose row / Mn2+-dependent activities Km column

substrate: UDP-xylose with manganese


substrate_name: UDP-glucuronate with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: UDP-glucuronate; column label: Mn2+-dependent activities / Km (uM); raw value 107 uM; normalized value 0.107 mM.

normalized_value_unit_evidence: Km=0.107 mM after converting 107 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row UDP-glucuronate; Mn2+-dependent Km column = 107 uM.

row_label: UDP-glucuronate row / Mn2+-dependent activities Km column

substrate: UDP-glucuronate with manganese


substrate_name: UDP-galacturonate with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: UDP-galacturonate; column label: Mn2+-dependent activities / Km (uM); raw value 108 uM; normalized value 0.108 mM.

normalized_value_unit_evidence: Km=0.108 mM after converting 108 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row UDP-galacturonate; Mn2+-dependent Km column = 108 uM.

row_label: UDP-galacturonate row / Mn2+-dependent activities Km column

substrate: UDP-galacturonate with manganese


substrate_name: CDP-glucose with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: CDP-glucose; column label: Mn2+-dependent activities / Km (uM); raw value 416 uM; normalized value 0.416 mM.

normalized_value_unit_evidence: Km=0.416 mM after converting 416 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row CDP-glucose; Mn2+-dependent Km column = 416 uM.

row_label: CDP-glucose row / Mn2+-dependent activities Km column

substrate: CDP-glucose with manganese


substrate_name: CDP-glycerol with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: CDP-glycerol; column label: Mn2+-dependent activities / Km (uM); raw value 795 uM; normalized value 0.795 mM.

normalized_value_unit_evidence: Km=0.795 mM after converting 795 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row CDP-glycerol; Mn2+-dependent Km column = 795 uM.

row_label: CDP-glycerol row / Mn2+-dependent activities Km column

substrate: CDP-glycerol with manganese


substrate_name: GDP-glucose with manganese

column_label: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row label: GDP-glucose; column label: Mn2+-dependent activities / Km (uM); raw value 784 uM; normalized value 0.784 mM.

normalized_value_unit_evidence: Km=0.784 mM after converting 784 uM to mM.

raw_value_unit_evidence: Table 4. Kinetic Parameters of FAD-AMP Lyase with Different Substrates; row GDP-glucose; Mn2+-dependent Km column = 784 uM.

row_label: GDP-glucose row / Mn2+-dependent activities Km column

substrate: GDP-glucose with manganese


substrate_name: adenylimidodiphosphate

substrate: adenylimidodiphosphate


substrate_name: dATP

substrate: dATP


substrate_name: diphosphate

substrate: diphosphate


substrate_name: cAMP

raw_value_unit_evidence: Km for cyclic AMP = 14 mM

row_label: reverse reaction; substrate cyclic AMP

substrate: cAMP


organism: Hyphomicrobium sp. DM2

substrate_name: Dichloromethane

substrate: Dichloromethane


organism: Sus scrofa

substrate_name: D-glyceraldehyde

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

column_label: Abstract reports D-glyceraldehyde, dihydroxyacetone, and glycolaldehyde acted as substrates with Kms of 11, <5, and 260 microM, respectively.

raw_value_unit_evidence: Km raw_value=11 microM raw_unit=microM

row_label: Porcine kidney triokinase / D-glyceraldehyde

table_label: PubMed XML abstract PMID 7831203

substrate: D-glyceraldehyde


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


smiles: C(F)Cl


substrate_name: chloroethane

smiles: CCCl

substrate: chloroethane


substrate_name: Bromomethane

smiles: CBr

substrate: Bromomethane


substrate_name: Iodoethane

smiles: CCI

substrate: Iodoethane


substrate_name: Diiodomethane

substrate: Diiodomethane


substrate_name: Dibromomethane

substrate: Dibromomethane


substrate_name: Bromoethane

smiles: CCBr

raw_value_unit_evidence: KM raw_value=330 +/- 40 raw_unit=uM

row_label: CH3CH2Br / bromoethane

table_label: ACS Biochemistry Table 2 - Steady State Kinetic Parameters of DM11 toward Monohaloethane Substrates

substrate: Bromoethane


substrate_name: ATP

assay_conditions_summary: pH 7.5; cofactor ATP

column_label: Table 1: Kinetic parameters of hTKFC and mutants row DHA kinase (ATP) activity / Wild type: Km raw_value=43.2 +/- 7.9 raw_unit=uM, table unit label=10^6 Km (M), hTKFC form=Wild type. Km normalized_value=0.0432 normalized_unit=mM after uM-to-mM conversion; CatLog value=0.0432 mM.

row_label: DHA kinase (ATP) activity / Wild type

substrate: ATP


substrate_name: FAD

column_label: Table 1: Kinetic parameters of hTKFC and mutants row Cyclizing lyase (FAD) activity / Wild type: Km raw_value=7.0 +/- 2.5 raw_unit=uM, table unit label=10^6 Km (M), hTKFC form=Wild type. Km normalized_value=0.007 normalized_unit=mM after uM-to-mM conversion; CatLog value=0.007 mM.

substrate: FAD


substrate_name: ADP-glucose

assay_conditions_summary: pH 7.5; cofactor ADP

column_label: Table 1: Kinetic parameters of hTKFC and mutants row Cyclizing lyase (ADP-glucose) activity / Wild type: Km raw_value=12.0 +/- 1.0 raw_unit=uM, table unit label=10^6 Km (M), hTKFC form=Wild type. Km normalized_value=0.012 normalized_unit=mM after uM-to-mM conversion; CatLog value=0.012 mM.

substrate: ADP-glucose


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Methylorubrum extorquens

assay_conditions_summary: pH 8

proof_lines:
pH 8
30°C, pH 8.2
pH 8.0 and 30°C


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


substrate_name: glyceraldehyde

substrate: glyceraldehyde


organism: Arabidopsis thaliana


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


enzyme_display_name: phycoerythrocyanin alpha-cysteine-84 phycoviolobilin lyase/isomerase

organism: Mastigocladus laminosus

substrate_name: phycocyanobilin

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

substrate: phycocyanobilin


enzyme: phycoerythrocyanin alpha-cysteine-84 phycoviolobilin lyase/isomerase


organism: Yersinia pestis

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


substrate_name: 2',3'-Cyclic CMP

sequence_variant_note: Mutation signature F46A matches the mutant residue at offset +0 and the reference residue at offset +26; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: 2',3'-Cyclic CMP


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -12, so it is treated as a source-provided variant sequence.


organism: Anabaena sp.

assay_conditions_summary: pH 8.5; 318.15 K; cofactor ATP

column_label: Results prose, cyaB1 with bicarbonate, Km(ATP) = 33.8 +/- 2.8 uM and kcat = 7.0 min^-1; not a table cell. The efficiency is a labeled derived ratio from these same row values, not claimed as directly printed.

normalized_value_unit_evidence: Km 33.8 uM rounds to 0.034 mM; kcat 7.0 min^-1 rounds to 0.117 s^-1; the stored efficiency is transparently derived from the same rounded row values as 0.117/0.034 = 3.441176470588235 s^-1 mM^-1.

raw_value_unit_evidence: Results prose reports Km(ATP) 33.8 +/- 2.8 uM and kcat 7.0 min^-1 with bicarbonate at pH 8.5 and 45 C.

row_label: Wild-type Anabaena cyaB1 catalytic domain residues 595-859 with ATP and bicarbonate

table_label: Results prose, printed page 35036 / PDF page 4


organism: Mycobacterium tuberculosis


organism: Streptomyces bikiniensis


substrate_name: 4-CDP-2-C-methyl-D-erythritol 2-phosphate (at pH 7 and in presence of Mg(2+) with recombinant IspF residues (62-240))


enzyme_display_name: D-tagatose 3-epimerase

organism: Caballeronia fortuita

substrate_name: D-sorbose

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

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

enzyme: D-tagatose 3-epimerase

substrate: D-sorbose


substrate_name: D-psicose

substrate: D-psicose


assay_conditions_summary: cofactor ATP


enzyme_display_name: dTDP-L-rhamnose 4-epimerase

organism: Burkholderia thailandensis

proof_lines: pH 8.2, temperature not specified in the publication

proof_lines: kcat is 0.9 sec(-1) for dTDP-6-deoxy-L-talose.

enzyme: dTDP-L-rhamnose 4-epimerase


organism: Plasmodium falciparum

proof_lines:
pH 7.0, 27°C
Raw SKiD Env: Temp=27°C, pH=7

source_databases_merged: brenda skid


enzyme_display_name: D-psicose 3-epimerase

organism: Clostridium sp.

substrate_name: D-Psicose

enzyme: D-psicose 3-epimerase

substrate: D-Psicose


substrate_name: D-fructose

substrate: D-fructose


organism: Dictyostelium discoideum

substrate_name: GTPgammaS

substrate: GTPgammaS


organism: Caballeronia insecticola


organism: Catenaria anguillulae

sequence_variant_note: Mutation signature E497K/C566D references residue 497, which is outside the resolved sequence length.

assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


substrate_name: GTP

substrate: GTP


organism: Treponema primitia


organism: Cereibacter sphaeroides

proof_lines: recombinant wild-type enzyme, pH 8.5, 35°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R118W with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


organism: Methylomonas sp. (strain DH-1)

substrate_name: L-ribulose

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

proof_lines: kcat is 4923 min(-1) with L-ribulose as substrate. kcat is 4103 min(-1) with D-allulose as substrate.

substrate: L-ribulose


substrate_name: L-allulose

substrate: L-allulose


organism: Enterocloster bolteae (strain ATCC BAA-613 / DSM 15670 / CCUG 46953 / JCM 12243 / WAL 16351)

substrate_name: D-psicose (at pH 7 and 55 degrees Celsius)

proof_lines: kcat is 49 sec(-1) for epimerase activity with D-psicose as substrate (at pH 7 and 55 degrees Celsius). kcat is 4.7 sec(-1) for epimerase activity with D-tagatose as substrate (at pH 7 and 55 degrees Celsius).


organism: Ruminiclostridium cellulolyticum

proof_lines: kcat is 3243.4 min(-1) for epimerase activity with D-psicose as substrate (at pH 8 and 55 degrees Celsius). kcat is 184.8 min(-1) for epimerase activity with D-tagatose as substrate (at pH 8 and 55 degrees Celsius).

source_databases_merged: brenda skid uniprot


organism: Desmospora sp. 8437

protein_accession_database: NCBI Protein

sequence_source: NCBI RefSeq protein WP_009711885.1


enzyme_display_name: L-fucose mutarotase

organism: Escherichia coli

substrate_name: alpha-L-fucopyranose

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: L-fucose mutarotase

substrate: alpha-L-fucopyranose


organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)

substrate_name: Unknown

proof_lines: kcat is 0.34 min(-1) for epimerase activity with D-psicose as substrate. kcat is 3.4 min(-1) for epimerase activity with D-tagatose as substrate. kcat is 8.5 min(-1) for epimerase activity with L-xylulose as substrate. kcat is 13 min(-1) fo

substrate: Unknown


organism: Pseudomonas cichorii


organism: Mesorhizobium loti


substrate_name: L-xylulose

substrate: L-xylulose


organism: Christensenella minuta


organism: [Clostridium] scindens


organism: Homo sapiens

substrate_name: GTP (in absence of RD3)

substrate: GTP (in absence of RD3)


organism: Ruminococcus sp.

proof_lines: pH 8.0, 60°C, recombinant enzyme expressed in Escherichia coli (DPE12)


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)

substrate_name: L-fucose

substrate: L-fucose


organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

substrate_name: D-psicose (at pH 8 and 50 degrees Celsius)

proof_lines: kcat is 2381 min(-1) for epimerase activity with D-psicose as substrate (at pH 8 and 50 degrees Celsius). kcat is 270 min(-1) for epimerase activity with D-tagatose as substrate (at pH 8 and 50 degrees Celsius).


enzyme_display_name: UniProt O75521

enzyme: UniProt O75521


enzyme_display_name: UniProt Q05871

organism: Saccharomyces cerevisiae

enzyme: UniProt Q05871


organism: Mus musculus

substrate_name: GTP (in presence of GUCA1A)

substrate: GTP (in presence of GUCA1A)


organism: Rattus norvegicus


enzyme_display_name: adenylate cyclase

substrate_name: ATP

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

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant Y394A, 10 mM Mg2+

enzyme: adenylate cyclase

substrate: ATP


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant W374A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant W249A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant K136A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant E242A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant K253A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant E185A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant K260A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant S113A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant T189A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant R19A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant S106A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant K332A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, recombinant catalytic domain mutant S103A, 10 mM Mg2+


proof_lines: pH 8.0, 37°C, versus ATP, wild-type catalytic domain Cya2-446


enzyme_display_name: guanylate cyclase

proof_lines: mutant S502A, temperature not specified in the publication, pH not specified in the publication

enzyme: guanylate cyclase


proof_lines: mutant S473A, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S487A, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant T500E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant T513E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S502E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S473E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S487E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant T500A, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S510E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant T513A, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S497E, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S510A, temperature not specified in the publication, pH not specified in the publication


proof_lines: mutant S497A, temperature not specified in the publication, pH not specified in the publication


organism: Enterocloster bolteae

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


substrate_name: D-tagatose

substrate: D-tagatose


enzyme_display_name: aconitate Delta-isomerase

organism: Zea mays

substrate_name: cis-aconitate

proof_lines: at pH 8.0, temperature not specified in the publication

enzyme: aconitate Delta-isomerase

substrate: cis-aconitate


proof_lines: with cis-aconitate as substrate, at pH 8.0, temperature not specified in the publication

proof_lines: with trans-aconitate as substrate, at pH 8.0, temperature not specified in the publication


enzyme_display_name: isopiperitenone Delta-isomerase

organism: Mentha x piperita

substrate_name: isopiperitenone

enzyme: isopiperitenone Delta-isomerase

substrate: isopiperitenone


enzyme_display_name: L-dopachrome isomerase

organism: Sepia officinalis

substrate_name: dopachrome

enzyme: L-dopachrome isomerase

substrate: dopachrome


enzyme_display_name: cholestenol Delta-isomerase

enzyme: cholestenol Delta-isomerase


organism: Ruminiclostridium cellulolyticum

substrate_name: D-fructose


substrate_name: D-Psicose

substrate: D-Psicose


substrate_name: L-Ribulose

assay_conditions_summary: pH 8; 333.15 K; buffer pH 8

column_label: Table 2, row L-Ribulose, M. loti L-RE columns report Km 291 mM, kcat 13 min^-1, kcat/Km 43 M^-1 min^-1.

raw_value_unit_evidence: Table 2 row L-Ribulose: Km = 291 mM; kcat = 13 min^-1; kcat/Km = 43 M^-1 min^-1

row_label: L-Ribulose

table_label: Table 2

substrate: L-Ribulose


column_label: Table 2, row D-Tagatose, M. loti L-RE columns report Km 140 mM, kcat 3.4 min^-1, kcat/Km 30 M^-1 min^-1.

raw_value_unit_evidence: Table 2 row D-Tagatose: Km = 140 mM; kcat = 3.4 min^-1; kcat/Km = 30 M^-1 min^-1

row_label: D-Tagatose


substrate_name: L-Xylulose

column_label: Table 2, row L-Xylulose, M. loti L-RE columns report Km 230 mM, kcat 8.5 min^-1, kcat/Km 37 M^-1 min^-1.

raw_value_unit_evidence: Table 2 row L-Xylulose: Km = 230 mM; kcat = 8.5 min^-1; kcat/Km = 37 M^-1 min^-1

row_label: L-Xylulose

substrate: L-Xylulose


column_label: Table 2, row D-Psicose, M. loti L-RE columns report Km 58 mM, kcat 0.34 min^-1, kcat/Km 5.4 M^-1 min^-1.

raw_value_unit_evidence: Table 2 row D-Psicose: Km = 58 mM; kcat = 0.34 min^-1; kcat/Km = 5.4 M^-1 min^-1

row_label: D-Psicose


enzyme_display_name: prostaglandin-A1 Delta-isomerase

organism: Felis catus

substrate_name: prostaglandin A1

enzyme: prostaglandin-A1 Delta-isomerase

substrate: prostaglandin A1


organism: Pseudomonas putida

proof_lines: Km-value is pH-dependent and increases from 0.18 mM at pH 7.15 to 7.7 mM at pH 9.25

proof_lines: in presence of 20% glycerol, over a 4fold range in enzyme concentration, the Km-value is inversely dependent on the enzyme concentration

proof_lines: in absence of glycerol, over a 4fold range in enzyme concentration, the Km-value is inversely dependent on the enzyme concentration


enzyme_display_name: Delta(3)-Delta(2)-enoyl-CoA isomerase

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

assay_conditions_summary: cofactor CoA

proof_lines: kcat are 270 sec(-1), 25 sec(-1), 20 sec(-1), 200 sec(-1), 180 sec(-1) and 98 sec(-1) for (3Z)-hexenoyl-CoA, (3Z)-octenoyl-CoA, (3Z)-tetradecenoyl-CoA, (3E)-hexenoyl-CoA, (3E)-octenoyl-CoA and (3E)-tetradecenoyl-CoA, respectively.

enzyme: Delta(3)-Delta(2)-enoyl-CoA isomerase


assay_conditions_summary: pH 8; 298.15 K; cofactor CoA

column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Octenoyl-CoA'; column 'Km (uM)' = 120 +/- 12; column 'kcat (s^-1)' = 210 +/- 11; column 'kcat/Km (uM^-1 s^-1)' = 1.8.

normalized_value_unit_evidence: Km: printed TABLE II cell 120 uM; 1 uM is 0.001 mM, so 120 / 1000 = 0.12 mM. kcat: printed TABLE II cell 210 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 1.8 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.8 x 1000 = 1800.0 s^-1 mM^-1. The exported kcat is 210.0 s^(-1) and equals the printed cell. The exported Km is 0.1 mM against the printed cell 0.12 mM. The exported kcat_over_km is 2100.0 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 1800.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '3-trans-Octenoyl-CoA': Km = 120 +/- 12 uM; kcat = 210 +/- 11 s^-1; printed kcat/Km = 1.8 uM^-1 s^-1.

row_label: TABLE II, substrate row '3-trans-Octenoyl-CoA'


column_label: TABLE I: Kinetic parameters of MECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Tetradecenoyl-CoA'; column 'Km (uM)' = 48 +/- 4.7; column 'kcat (s^-1)' = 20 +/- 1.2; column 'kcat/Km (uM^-1 s^-1)' = 0.42.

normalized_value_unit_evidence: Km: printed TABLE I cell 48 uM; 1 uM is 0.001 mM, so 48 / 1000 = 0.048 mM. kcat: printed TABLE I cell 20 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE I cell 0.42 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.42 x 1000 = 420.0 s^-1 mM^-1. Quotient disclosure for this printed row: 20 / 0.048 = 416.6666666666667 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE I uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 20.0 s^(-1) and the exported Km is 0.048 mM.

raw_value_unit_evidence: TABLE I (Kinetic parameters of MECI), substrate row '3-trans-Tetradecenoyl-CoA': Km = 48 +/- 4.7 uM; kcat = 20 +/- 1.2 s^-1; printed kcat/Km = 0.42 uM^-1 s^-1.

row_label: TABLE I, substrate row '3-trans-Tetradecenoyl-CoA'


column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Tetradecenoyl-CoA'; column 'Km (uM)' = 29 +/- 3.8; column 'kcat (s^-1)' = 540 +/- 38; column 'kcat/Km (uM^-1 s^-1)' = 19.

normalized_value_unit_evidence: Km: printed TABLE II cell 29 uM; 1 uM is 0.001 mM, so 29 / 1000 = 0.029 mM. kcat: printed TABLE II cell 540 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 19 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 19 x 1000 = 19000.0 s^-1 mM^-1. The exported kcat is 540.0 s^(-1) and equals the printed cell. The exported Km is 0.021 mM against the printed cell 0.029 mM. The exported kcat_over_km is 25714.285714285714 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 19000.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '3-trans-Tetradecenoyl-CoA': Km = 29 +/- 3.8 uM; kcat = 540 +/- 38 s^-1; printed kcat/Km = 19 uM^-1 s^-1.

row_label: TABLE II, substrate row '3-trans-Tetradecenoyl-CoA'


proof_lines: kcat are 100 sec(-1), 210 sec(-1), 540 sec(-1), 58 sec(-1), 47 sec(-1) and 210 sec(-1) for (3Z)-hexenoyl-CoA, (3Z)-octenoyl-CoA, (3Z)-tetradecenoyl-CoA, (3E)-hexenoyl-CoA, (3E)-octenoyl-CoA and (3E)-tetradecenoyl-CoA, respectively.


organism: Oryctolagus cuniculus

proof_lines:
in absence of rabbit albumin
in presence of rabbit albumin


enzyme_display_name: methylitaconate Delta-isomerase

organism: Eubacterium barkeri

substrate_name: methylitaconate

enzyme: methylitaconate Delta-isomerase

substrate: methylitaconate


organism: Escherichia coli

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


assay_conditions_summary: pH 8.5; 298.15 K; cofactor CoA


column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-cis-Tetradecenoyl-CoA'; column 'Km (uM)' = 21 +/- 5.9; column 'kcat (s^-1)' = 210 +/- 22; column 'kcat/Km (uM^-1 s^-1)' = 10.

normalized_value_unit_evidence: Km: printed TABLE II cell 21 uM; 1 uM is 0.001 mM, so 21 / 1000 = 0.021 mM. kcat: printed TABLE II cell 210 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 10 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 10 x 1000 = 10000.0 s^-1 mM^-1. The exported values are kcat 210.0 s^(-1) and Km 0.020999999999999998 mM, and each one equals the printed cell after conversion. The export carries no kcat_over_km field for this row, so the printed efficiency cell is recorded as evidence only and no ratio is written.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '3-cis-Tetradecenoyl-CoA': Km = 21 +/- 5.9 uM; kcat = 210 +/- 22 s^-1; printed kcat/Km = 10 uM^-1 s^-1.

row_label: TABLE II, substrate row '3-cis-Tetradecenoyl-CoA'


column_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-cis-Tetradecenoyl-CoA'; column 'Km (uM)' = 45 +/- 2.5; column 'kcat (s^-1)' = 2.7 +/- 1.1; column 'kcat/Km (uM^-1 s^-1)' = 0.060.

normalized_value_unit_evidence: Km: printed TABLE III cell 45 uM; 1 uM is 0.001 mM, so 45 / 1000 = 0.045 mM. kcat: printed TABLE III cell 2.7 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.060 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.060 x 1000 = 60.0 s^-1 mM^-1. The exported values are kcat 2.7 s^(-1) and Km 0.045000000000000005 mM, and each one equals the printed cell after conversion. The export carries no kcat_over_km field for this row, so the printed efficiency cell is recorded as evidence only and no ratio is written.

raw_value_unit_evidence: TABLE III (Kinetic parameters of the enoyl-CoA isomerase of MFE1), substrate row '3-cis-Tetradecenoyl-CoA': Km = 45 +/- 2.5 uM; kcat = 2.7 +/- 1.1 s^-1; printed kcat/Km = 0.060 uM^-1 s^-1.

row_label: TABLE III, substrate row '3-cis-Tetradecenoyl-CoA'


column_label: TABLE I: Kinetic parameters of MECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-cis-Tetradecenoyl-CoA'; column 'Km (uM)' = 57 +/- 6; column 'kcat (s^-1)' = 98 +/- 4.8; column 'kcat/Km (uM^-1 s^-1)' = 1.7.

normalized_value_unit_evidence: Km: printed TABLE I cell 57 uM; 1 uM is 0.001 mM, so 57 / 1000 = 0.057 mM. kcat: printed TABLE I cell 98 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE I cell 1.7 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.7 x 1000 = 1700.0 s^-1 mM^-1. The exported values are kcat 98.0 s^(-1) and Km 0.057 mM, and each one equals the printed cell after conversion. The export carries no kcat_over_km field for this row, so the printed efficiency cell is recorded as evidence only and no ratio is written.

raw_value_unit_evidence: TABLE I (Kinetic parameters of MECI), substrate row '3-cis-Tetradecenoyl-CoA': Km = 57 +/- 6 uM; kcat = 98 +/- 4.8 s^-1; printed kcat/Km = 1.7 uM^-1 s^-1.

row_label: TABLE I, substrate row '3-cis-Tetradecenoyl-CoA'


organism: Drosophila melanogaster

substrate_name: dopamine chrome

substrate: dopamine chrome


organism: Escherichia coli (strain K12)

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


organism: Homo sapiens

substrate_name: crotonyl-CoA ((2E)-butenoyl-CoA)

substrate: crotonyl-CoA ((2E)-butenoyl-CoA)


substrate_name: Unknown

substrate: Unknown


organism: Trichinella spiralis


organism: Cavia porcellus


proof_lines: pH and temperature not specified in the publication


organism: Mus musculus


organism: Rattus norvegicus


column_label: TABLE I: Kinetic parameters of MECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Hexenoyl-CoA'; column 'Km (uM)' = 470 +/- 40; column 'kcat (s^-1)' = 270 +/- 16; column 'kcat/Km (uM^-1 s^-1)' = 0.57.

normalized_value_unit_evidence: Km: printed TABLE I cell 470 uM; 1 uM is 0.001 mM, so 470 / 1000 = 0.47 mM. kcat: printed TABLE I cell 270 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE I cell 0.57 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.57 x 1000 = 570.0 s^-1 mM^-1. The exported kcat is 270.0 s^(-1) and equals the printed cell. The exported Km is 0.013 mM against the printed cell 0.47 mM. The exported kcat_over_km is 20769.23076923077 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 570.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE I (Kinetic parameters of MECI), substrate row '3-trans-Hexenoyl-CoA': Km = 470 +/- 40 uM; kcat = 270 +/- 16 s^-1; printed kcat/Km = 0.57 uM^-1 s^-1.

row_label: TABLE I, substrate row '3-trans-Hexenoyl-CoA'


column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Hexenoyl-CoA'; column 'Km (uM)' = 1600 +/- 79; column 'kcat (s^-1)' = 100 +/- 39; column 'kcat/Km (uM^-1 s^-1)' = 0.063.

normalized_value_unit_evidence: Km: printed TABLE II cell 1600 uM; 1 uM is 0.001 mM, so 1600 / 1000 = 1.6 mM. kcat: printed TABLE II cell 100 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 0.063 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.063 x 1000 = 63.0 s^-1 mM^-1. The exported kcat is 100.0 s^(-1) and equals the printed cell. The exported Km is 1.2 mM against the printed cell 1.6 mM. The exported kcat_over_km is 83.33333333333334 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 63.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '3-trans-Hexenoyl-CoA': Km = 1600 +/- 79 uM; kcat = 100 +/- 39 s^-1; printed kcat/Km = 0.063 uM^-1 s^-1.

row_label: TABLE II, substrate row '3-trans-Hexenoyl-CoA'


column_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Hexenoyl-CoA'; column 'Km (uM)' = 38 +/- 1.3; column 'kcat (s^-1)' = 1.8 +/- 0.039; column 'kcat/Km (uM^-1 s^-1)' = 0.047.

normalized_value_unit_evidence: Km: printed TABLE III cell 38 uM; 1 uM is 0.001 mM, so 38 / 1000 = 0.038 mM. kcat: printed TABLE III cell 1.8 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.047 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.047 x 1000 = 47.0 s^-1 mM^-1. The exported kcat is 1.8 s^(-1) and equals the printed cell. The exported Km is 0.031 mM against the printed cell 0.038 mM. The exported kcat_over_km is 58.06451612903226 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 47.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE III (Kinetic parameters of the enoyl-CoA isomerase of MFE1), substrate row '3-trans-Hexenoyl-CoA': Km = 38 +/- 1.3 uM; kcat = 1.8 +/- 0.039 s^-1; printed kcat/Km = 0.047 uM^-1 s^-1.

row_label: TABLE III, substrate row '3-trans-Hexenoyl-CoA'


column_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Octenoyl-CoA'; column 'Km (uM)' = 28 +/- 1.5; column 'kcat (s^-1)' = 2.0 +/- 0.052; column 'kcat/Km (uM^-1 s^-1)' = 0.071.

normalized_value_unit_evidence: Km: printed TABLE III cell 28 uM; 1 uM is 0.001 mM, so 28 / 1000 = 0.028 mM. kcat: printed TABLE III cell 2.0 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.071 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.071 x 1000 = 71.0 s^-1 mM^-1. The exported kcat is 2.4 s^(-1) against the printed cell 2.0 s^-1. The exported Km is 0.028 mM and equals the printed cell. The exported kcat_over_km is 85.71428571428571 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 71.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE III (Kinetic parameters of the enoyl-CoA isomerase of MFE1), substrate row '3-trans-Octenoyl-CoA': Km = 28 +/- 1.5 uM; kcat = 2.0 +/- 0.052 s^-1; printed kcat/Km = 0.071 uM^-1 s^-1.

row_label: TABLE III, substrate row '3-trans-Octenoyl-CoA'


column_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Tetradecenoyl-CoA'; column 'Km (uM)' = 32 +/- 11; column 'kcat (s^-1)' = 1.4 +/- 0.26; column 'kcat/Km (uM^-1 s^-1)' = 0.044.

normalized_value_unit_evidence: Km: printed TABLE III cell 32 uM; 1 uM is 0.001 mM, so 32 / 1000 = 0.032 mM. kcat: printed TABLE III cell 1.4 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.044 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.044 x 1000 = 44.0 s^-1 mM^-1. Quotient disclosure for this printed row: 1.4 / 0.032 = 43.74999999999999 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE III uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 1.4 s^(-1) and the exported Km is 0.032 mM.

raw_value_unit_evidence: TABLE III (Kinetic parameters of the enoyl-CoA isomerase of MFE1), substrate row '3-trans-Tetradecenoyl-CoA': Km = 32 +/- 11 uM; kcat = 1.4 +/- 0.26 s^-1; printed kcat/Km = 0.044 uM^-1 s^-1.

row_label: TABLE III, substrate row '3-trans-Tetradecenoyl-CoA'


column_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '2-trans,5-cis-Octadienoyl-CoA'; column 'Km (uM)' = 4.4 +/- 1.2; column 'kcat (s^-1)' = 11 +/- 0.92; column 'kcat/Km (uM^-1 s^-1)' = 2.5.

normalized_value_unit_evidence: Km: printed TABLE III cell 4.4 uM; 1 uM is 0.001 mM, so 4.4 / 1000 = 0.0044 mM. kcat: printed TABLE III cell 11 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 2.5 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 2.5 x 1000 = 2500.0 s^-1 mM^-1. The exported values are kcat 11.0 s^(-1), Km 0.0044 mM and kcat_over_km 2500.0 s^(-1)*mM^(-1), and each one equals the printed cell after conversion.

raw_value_unit_evidence: TABLE III (Kinetic parameters of the enoyl-CoA isomerase of MFE1), substrate row '2-trans,5-cis-Octadienoyl-CoA': Km = 4.4 +/- 1.2 uM; kcat = 11 +/- 0.92 s^-1; printed kcat/Km = 2.5 uM^-1 s^-1.

row_label: TABLE III, substrate row '2-trans,5-cis-Octadienoyl-CoA'


column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '2-trans,5-cis-Tetradecadienoyl-CoA'; column 'Km (uM)' = 29 +/- 5.9; column 'kcat (s^-1)' = 15 +/- 1.4; column 'kcat/Km (uM^-1 s^-1)' = 0.52.

normalized_value_unit_evidence: Km: printed TABLE II cell 29 uM; 1 uM is 0.001 mM, so 29 / 1000 = 0.029 mM. kcat: printed TABLE II cell 15 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 0.52 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.52 x 1000 = 520.0 s^-1 mM^-1. Quotient disclosure for this printed row: 15 / 0.029 = 517.2413793103448 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE II uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 15.0 s^(-1) and the exported Km is 0.029 mM.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '2-trans,5-cis-Tetradecadienoyl-CoA': Km = 29 +/- 5.9 uM; kcat = 15 +/- 1.4 s^-1; printed kcat/Km = 0.52 uM^-1 s^-1.

row_label: TABLE II, substrate row '2-trans,5-cis-Tetradecadienoyl-CoA'


organism: Pseudomonas sp.

substrate_name: trans-Aconitate

proof_lines: kcat and kcat/KM are 4500 sec(-1) and 760 sec(-1) mM(-1), respectively for cis-aconitic acid. kcat and kcat/KM are 15000 sec(-1) and 190 sec(-1) mM(-1), respectively for trans-aconitic acid.

source_databases_merged: sabio_rk brenda uniprot

substrate: trans-Aconitate


organism: Pseudomonas sp. WU-0701

substrate_name: trans-aconitate

substrate: trans-aconitate


organism: Saccharomyces cerevisiae


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K242C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D149E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K242D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K242F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K242R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K242T to reconstruct the assayed variant sequence.


table_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132)


table_label: TABLE I: Kinetic parameters of MECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132)


normalized_value_unit_evidence: Km: printed TABLE II cell 29 uM; 1 uM is 0.001 mM, so 29 / 1000 = 0.029 mM. kcat: printed TABLE II cell 540 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 19 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 19 x 1000 = 19000.0 s^-1 mM^-1. Quotient disclosure for this printed row: 540 / 0.029 = 18620.689655172413 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE II uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 540.0 s^(-1) and the exported Km is 0.029 mM.

table_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132)


column_label: Table I (PDF page 5 of 6, journal page 9131), substrate row `3-cis-Octenoyl-CoA`: Km (uM) = 150 +/- 24; kcat (s^-1) = 180 +/- 16; kcat/Km (uM^-1 s^-1) = 1.2.

normalized_value_unit_evidence: kcat: printed cell 180 s^-1 -> 180 s^(-1) (unit is already s^-1); the exported value is 180.0 s^(-1). Km: printed cell 150 uM -> 0.15 mM (divide by 1000); the exported value is 0.15 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.2 uM^-1 s^-1 for this substrate line -> 1200.0 s^(-1)*mM^(-1) (multiply by 1000 for uM^-1 to mM^-1); the exported value is 1200.0 s^(-1)*mM^(-1).

row_label: Table I, decoded plain-numeral transcription, substrate row `3-cis-Octenoyl-CoA`

table_label: Table I (PDF page 5 of 6, journal page 9131) 'Kinetic parameters of MECI'


column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-cis-Octenoyl-CoA'; column 'Km (uM)' = 100 +/- 6.8; column 'kcat (s^-1)' = 47 +/- 1.4; column 'kcat/Km (uM^-1 s^-1)' = 0.45.

normalized_value_unit_evidence: Km: printed TABLE II cell 100 uM; 1 uM is 0.001 mM, so 100 / 1000 = 0.1 mM. kcat: printed TABLE II cell 47 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 0.45 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.45 x 1000 = 450.0 s^-1 mM^-1. The exported kcat is 47.0 s^(-1) and equals the printed cell. The exported Km is 0.1 mM and equals the printed cell. The exported kcat_over_km is 470.0 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 450.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '3-cis-Octenoyl-CoA': Km = 100 +/- 6.8 uM; kcat = 47 +/- 1.4 s^-1; printed kcat/Km = 0.45 uM^-1 s^-1.

row_label: TABLE II, substrate row '3-cis-Octenoyl-CoA'


column_label: Table III (PDF page 5 of 6, journal page 9131), substrate row `3-cis-Tetradecenoyl-CoA (footnote a)`: Km (uM) = 45 +/- 2.5; kcat (s^-1) = 2.7 +/- 1.1; kcat/Km (uM^-1 s^-1) = 0.060.

normalized_value_unit_evidence: kcat: printed cell 2.7 s^-1 -> 2.7 s^(-1) (unit is already s^-1); the exported value is 2.7 s^(-1). Km: printed cell 45 uM -> 0.045 mM (divide by 1000); the exported value is 0.045 mM. kcat/Km: the paper PRINTS the kcat/Km cell 0.060 uM^-1 s^-1 for this substrate line -> 60.000 s^(-1)*mM^(-1) (multiply by 1000 for uM^-1 to mM^-1); the exported value is 60.00000000000001 s^(-1)*mM^(-1).

row_label: Table III, decoded plain-numeral transcription, substrate row `3-cis-Tetradecenoyl-CoA (footnote a)`

table_label: Table III (PDF page 5 of 6, journal page 9131) 'Kinetic parameters of the enoyl-CoA isomerase of MFE1'


normalized_value_unit_evidence: Km: printed TABLE I cell 57 uM; 1 uM is 0.001 mM, so 57 / 1000 = 0.057 mM. kcat: printed TABLE I cell 98 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE I cell 1.7 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 1.7 x 1000 = 1700.0 s^-1 mM^-1. Quotient disclosure for this printed row: 98 / 0.057 = 1719.298245614035 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE I uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 98.0 s^(-1) and the exported Km is 0.057 mM.


column_label: Table II (PDF page 5 of 6, journal page 9131), substrate row `3-cis-Tetradecenoyl-CoA`: Km (uM) = 21 +/- 5.9; kcat (s^-1) = 210 +/- 22; kcat/Km (uM^-1 s^-1) = 10.

normalized_value_unit_evidence: kcat: printed cell 210 s^-1 -> 210 s^(-1) (unit is already s^-1); the exported value is 210.0 s^(-1). Km: printed cell 21 uM -> 0.021 mM (divide by 1000); the exported value is 0.021 mM. kcat/Km: the paper PRINTS the kcat/Km cell 10 uM^-1 s^-1 for this substrate line -> 10000 s^(-1)*mM^(-1) (multiply by 1000 for uM^-1 to mM^-1); the exported value is 10000.0 s^(-1)*mM^(-1).

row_label: Table II, decoded plain-numeral transcription, substrate row `3-cis-Tetradecenoyl-CoA`

table_label: Table II (PDF page 5 of 6, journal page 9131) 'Kinetic parameters of ECI'


normalized_value_unit_evidence: Km: printed TABLE III cell 38 uM; 1 uM is 0.001 mM, so 38 / 1000 = 0.038 mM. kcat: printed TABLE III cell 1.8 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.047 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.047 x 1000 = 47.0 s^-1 mM^-1. Quotient disclosure for this printed row: 1.8 / 0.038 = 47.36842105263158 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE III uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 1.8 s^(-1) and the exported Km is 0.038 mM.


normalized_value_unit_evidence: Km: printed TABLE III cell 28 uM; 1 uM is 0.001 mM, so 28 / 1000 = 0.028 mM. kcat: printed TABLE III cell 2.0 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.071 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.071 x 1000 = 71.0 s^-1 mM^-1. Quotient disclosure for this printed row: 2.0 / 0.028 = 71.42857142857143 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE III uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 2.0 s^(-1) and the exported Km is 0.028 mM.


column_label: TABLE I: Kinetic parameters of MECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-trans-Octenoyl-CoA'; column 'Km (uM)' = 190 +/- 36; column 'kcat (s^-1)' = 25 +/- 2.8; column 'kcat/Km (uM^-1 s^-1)' = 0.13.

normalized_value_unit_evidence: Km: printed TABLE I cell 190 uM; 1 uM is 0.001 mM, so 190 / 1000 = 0.19 mM. kcat: printed TABLE I cell 25 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE I cell 0.13 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.13 x 1000 = 130.0 s^-1 mM^-1. Quotient disclosure for this printed row: 25 / 0.19 = 131.57894736842104 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE I uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 25.0 s^(-1) and the exported Km is 0.19 mM.

raw_value_unit_evidence: TABLE I (Kinetic parameters of MECI), substrate row '3-trans-Octenoyl-CoA': Km = 190 +/- 36 uM; kcat = 25 +/- 2.8 s^-1; printed kcat/Km = 0.13 uM^-1 s^-1.

row_label: TABLE I, substrate row '3-trans-Octenoyl-CoA'


column_label: Table III (PDF page 5 of 6, journal page 9131), substrate row `2-trans,5-cis-Octadienoyl-CoA (footnote b)`: Km (uM) = 4.4 +/- 1.2; kcat (s^-1) = 11 +/- 0.92; kcat/Km (uM^-1 s^-1) = 2.5.

normalized_value_unit_evidence: kcat: printed cell 11 s^-1 -> 11 s^(-1) (unit is already s^-1); the exported value is 11.0 s^(-1). Km: printed cell 4.4 uM -> 0.0044 mM (divide by 1000); the exported value is 0.004 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.5 uM^-1 s^-1 for this substrate line -> 2500.0 s^(-1)*mM^(-1) (multiply by 1000 for uM^-1 to mM^-1); the exported value is 2750.0 s^(-1)*mM^(-1).

row_label: Table III, decoded plain-numeral transcription, substrate row `2-trans,5-cis-Octadienoyl-CoA (footnote b)`


column_label: TABLE I: Kinetic parameters of MECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '2-trans,5-cis-Octadienoyl-CoA'; column 'Km (uM)' = 84 +/- 18; column 'kcat (s^-1)' = 45 +/- 4.8; column 'kcat/Km (uM^-1 s^-1)' = 0.54.

normalized_value_unit_evidence: Km: printed TABLE I cell 84 uM; 1 uM is 0.001 mM, so 84 / 1000 = 0.084 mM. kcat: printed TABLE I cell 45 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE I cell 0.54 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.54 x 1000 = 540.0 s^-1 mM^-1. Quotient disclosure for this printed row: 45 / 0.084 = 535.7142857142857 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE I uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 45.0 s^(-1) and the exported Km is 0.084 mM.

raw_value_unit_evidence: TABLE I (Kinetic parameters of MECI), substrate row '2-trans,5-cis-Octadienoyl-CoA': Km = 84 +/- 18 uM; kcat = 45 +/- 4.8 s^-1; printed kcat/Km = 0.54 uM^-1 s^-1.

row_label: TABLE I, substrate row '2-trans,5-cis-Octadienoyl-CoA'


column_label: Table III (PDF page 5 of 6, journal page 9131), substrate row `2-trans,5-cis-Tetradecadienoyl-CoA (footnote b)`: Km (uM) = 9.6 +/- 0.71; kcat (s^-1) = 12 +/- 0.46; kcat/Km (uM^-1 s^-1) = 1.3.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1 -> 12 s^(-1) (unit is already s^-1); the exported value is 12.0 s^(-1). Km: printed cell 9.6 uM -> 0.0096 mM (divide by 1000); the exported value is 0.01 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.3 uM^-1 s^-1 for this substrate line -> 1300.0 s^(-1)*mM^(-1) (multiply by 1000 for uM^-1 to mM^-1); the exported value is 1200.0 s^(-1)*mM^(-1).

row_label: Table III, decoded plain-numeral transcription, substrate row `2-trans,5-cis-Tetradecadienoyl-CoA (footnote b)`


column_label: TABLE III: Kinetic parameters of the enoyl-CoA isomerase of MFE1 (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-cis-Hexenoyl-CoA'; column 'Km (uM)' = 31 +/- 4; column 'kcat (s^-1)' = 1.6 +/- 0.13; column 'kcat/Km (uM^-1 s^-1)' = 0.052.

normalized_value_unit_evidence: Km: printed TABLE III cell 31 uM; 1 uM is 0.001 mM, so 31 / 1000 = 0.031 mM. kcat: printed TABLE III cell 1.6 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE III cell 0.052 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.052 x 1000 = 52.0 s^-1 mM^-1. Quotient disclosure for this printed row: 1.6 / 0.031 = 51.612903225806456 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the significant figures TABLE III uses, and it sits inside the last-place rounding interval of the quotient. The exported kcat is 1.6 s^(-1) and the exported Km is 0.031 mM.

raw_value_unit_evidence: TABLE III (Kinetic parameters of the enoyl-CoA isomerase of MFE1), substrate row '3-cis-Hexenoyl-CoA': Km = 31 +/- 4 uM; kcat = 1.6 +/- 0.13 s^-1; printed kcat/Km = 0.052 uM^-1 s^-1.

row_label: TABLE III, substrate row '3-cis-Hexenoyl-CoA'


column_label: TABLE II: Kinetic parameters of ECI (The Journal of Biological Chemistry 2002, volume 277, number 11, pages 9127-9132), substrate row '3-cis-Hexenoyl-CoA'; column 'Km (uM)' = 1200 +/- 157; column 'kcat (s^-1)' = 58 +/- 5.6; column 'kcat/Km (uM^-1 s^-1)' = 0.049.

normalized_value_unit_evidence: Km: printed TABLE II cell 1200 uM; 1 uM is 0.001 mM, so 1200 / 1000 = 1.2 mM. kcat: printed TABLE II cell 58 s^-1; the column head prints s^-1, which is the export unit, so no unit conversion applies. kcat/Km: printed TABLE II cell 0.049 uM^-1 s^-1; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.049 x 1000 = 49.0 s^-1 mM^-1. The exported kcat is 58.0 s^(-1) and equals the printed cell. The exported Km is 1.2 mM and equals the printed cell. The exported kcat_over_km is 48.333333333333336 s^(-1)*mM^(-1), the quotient of the exported kcat and Km, against the printed efficiency cell 49.0 s^(-1)*mM^(-1) that this record carries.

raw_value_unit_evidence: TABLE II (Kinetic parameters of ECI), substrate row '3-cis-Hexenoyl-CoA': Km = 1200 +/- 157 uM; kcat = 58 +/- 5.6 s^-1; printed kcat/Km = 0.049 uM^-1 s^-1.

row_label: TABLE II, substrate row '3-cis-Hexenoyl-CoA'


column_label: Table III (PDF page 5 of 6, journal page 9131), substrate row `3-cis-Octenoyl-CoA (footnote a)`: Km (uM) = 32 +/- 6.3; kcat (s^-1) = 2.4 +/- 0.21; kcat/Km (uM^-1 s^-1) = 0.075.

normalized_value_unit_evidence: kcat: printed cell 2.4 s^-1 -> 2.4 s^(-1) (unit is already s^-1); the exported value is 2.4 s^(-1). Km: printed cell 32 uM -> 0.032 mM (divide by 1000); the exported value is 0.032 mM. kcat/Km: the paper PRINTS the kcat/Km cell 0.075 uM^-1 s^-1 for this substrate line -> 75.000 s^(-1)*mM^(-1) (multiply by 1000 for uM^-1 to mM^-1); the exported value is 75.0 s^(-1)*mM^(-1).

row_label: Table III, decoded plain-numeral transcription, substrate row `3-cis-Octenoyl-CoA (footnote a)`


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: L-dopachrome

substrate: L-dopachrome


substrate_name: Itaconate

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

substrate: Itaconate


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


substrate_name: Zymosterol

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

source_databases_merged: sabio_rk brenda skid

substrate: Zymosterol


column_label: Figure 5 caption reports for cholesta-7,24-dienol: Km = 66.1 +/- 3.1 uM, Vmax = 0.034 +/- 0.018 nmol min^-1 mg^-1, r2 = 0.95.

raw_value_unit_evidence: Km raw_value=66.1 +/- 3.1 raw_unit=uM

row_label: hSI using cholesta-7,24-diene-3beta-ol (B)

table_label: Figure 5: Michaelis-Menten hyperbolic curves of hSI using zymosterol (A) and cholesta-7,24-diene-3beta-ol (B)


substrate_name: crotonyl-CoA (for enoyl-CoA hydratase activity)


substrate_name: acetoacetyl-CoA (for 3-hydroxyacyl-CoA dehydrogenase activity)


substrate_name: NADH (for 3-hydroxyacyl-CoA dehydrogenase activity)

assay_conditions_summary: cofactor NADH


substrate_name: cis-aconitate

substrate: cis-aconitate


assay_conditions_summary: pH 7; cofactor CoA

proof_lines:
pH 7
pH 9.0
Raw SKiD Env: Temp=-----, pH=7


organism: Arabidopsis thaliana

substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


substrate_name: acryloyl-CoA

column_label: Primary paper Table 2 row Acryloyl-CoA, column Km (uM), value 34.04.

raw_value_unit_evidence: Table 2 row Acryloyl-CoA reports Km 34.04 uM.

row_label: Acryloyl-CoA

table_label: Table 2: Substrate specificity of partially purified human ECHS1

substrate: acryloyl-CoA


substrate_name: tiglyl-CoA (2-methylcrotonoyl-CoA)

column_label: Primary paper Table 2 row Tiglyl-CoA, column Km (uM), value 57.87.

raw_value_unit_evidence: Table 2 row Tiglyl-CoA reports Km 57.87 uM.

row_label: Tiglyl-CoA

substrate: tiglyl-CoA (2-methylcrotonoyl-CoA)


substrate_name: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol (in the AEBS complex assay)

column_label: PMC2922168 Results section D8D7I and DHCR7 Coexpression Allows the Reconstitution of ChEH reports Km 4.47 +/- 0.05 uM for D8D7I and DHCR7 coexpression experiments; Fig. 4B is the Michaelis-Menten plot versus alpha-CE.

raw_value_unit_evidence: Km raw_value=4.47 raw_unit=uM; Vmax raw_value=0.46 raw_unit=nmol CT/mg protein/min

row_label: D8D7I + DHCR7 coexpression ChEH kinetic parameter

table_label: PMC2922168 Results prose and Fig. 4B


organism: Yersinia pestis

substrate_name: ATP

assay_conditions_summary: pH 7; 310.15 K; buffer Tris; cofactor ATP

proof_lines: wild type enzyme, at pH 7.0, in Tris buffer at 37°C

proof_lines: wild type enzyme, at pH 7.5, in Tris buffer at 37°C

proof_lines: wild type enzyme, at pH 8.0, in Tris buffer at 37°C

substrate: ATP


assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines: mutant enzyme C83A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme C83A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme R63A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme R63A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme D55K, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme D55K, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme E12Q, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme E12Q, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme F5A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme F5A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme L72A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme L72A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme M140A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme M140A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme K76A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme K76A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme R113A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme E136A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme E136A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme K14A, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme K14A, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


proof_lines: mutant enzyme E10Q, in the presence of 10 mM Mn2+, at pH 8.5 and 37°C

proof_lines: mutant enzyme E10Q, in the presence of 20 mM Mg2+, at pH 8.5 and 37°C


substrate_name: GTP

substrate: GTP