column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate EA, Product 1b(OH)EA; column Km (uM) = 68.80; column kcat (s^-1) = 0.293; column kcat/Km (s^-1/uM) = 0.0043. captured primary segment: Table II | enzyme I486A | substrate EA | product 1b(OH)EA | Km 68.80 +/- 4.04 uM | kcat 0.293 +/- 0.010 s^-1 | kcat/Km 0.0043 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 68.80 uM; 1 uM is 1/1000 mM, so 68.80 / 1000 = 0.0688 mM; the exported value is 0.0688 mM. kcat: printed Table II kcat cell 0.293 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.293 s^(-1); the exported value is 0.293 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0043 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0043 x 1000 = 4.3 s^(-1)*mM^(-1); the exported value is 4.258720930232558 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.293 / 0.0688 = 4.258720930232558 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate EA, Product 1b(OH)EA: Km = 68.80 uM; kcat = 0.293 s^-1; printed kcat/Km = 0.0043 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate EA, Product 1b(OH)EA


enzyme_display_name: 5-epiaristolochene 1,3-dihydroxylase

organism: Nicotiana tabacum

source_db: brenda

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:Q94FM7 and applied mutation signature S368T to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368T, Substrate 1b(OH)EA, Product CD; column Km (uM) = 9.97; column kcat (s^-1) = 0.482; column kcat/Km (s^-1/uM) = 0.0483. captured primary segment: Table II | enzyme S368T | substrate 1b(OH)EA | product CD | Km 9.97 +/- 1.14 uM | kcat 0.482 +/- 0.019 s^-1 | kcat/Km 0.0483 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 9.97 uM; 1 uM is 1/1000 mM, so 9.97 / 1000 = 0.009970000000000001 mM; the exported value is 0.00997 mM. kcat: printed Table II kcat cell 0.482 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.482 s^(-1); the exported value is 0.482 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0483 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0483 x 1000 = 48.300000000000004 s^(-1)*mM^(-1); the exported value is 48.34503510531595 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.482 / 0.009970000000000001 = 48.34503510531594 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368T, Substrate 1b(OH)EA, Product CD: Km = 9.97 uM; kcat = 0.482 s^-1; printed kcat/Km = 0.0483 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368T, Substrate 1b(OH)EA, Product CD

data_origin: experimental

enzyme: 5-epiaristolochene 1,3-dihydroxylase

status: corrected

source: brenda


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 II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row Wild-type, Substrate EA, Product CD; column Km (uM) = 19.18; column kcat (s^-1) = 0.493; column kcat/Km (s^-1/uM) = 0.0257. captured primary segment: Table II | enzyme Wild-type | substrate EA | product CD | Km 19.18 +/- 2.90 uM | kcat 0.493 +/- 0.039 s^-1 | kcat/Km 0.0257 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 19.18 uM; 1 uM is 1/1000 mM, so 19.18 / 1000 = 0.01918 mM; the exported value is 0.01918 mM. kcat: printed Table II kcat cell 0.493 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.493 s^(-1); the exported value is 0.493 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0257 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0257 x 1000 = 25.7 s^(-1)*mM^(-1); the exported value is 25.703858185610013 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.493 / 0.01918 = 25.703858185610013 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row Wild-type, Substrate EA, Product CD: Km = 19.18 uM; kcat = 0.493 s^-1; printed kcat/Km = 0.0257 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row Wild-type, Substrate EA, Product CD


verification_status: unverified

sequence_variant_note: Mutation signature S386V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme S386V, the reaction product is 1beta-hydroxy-5-epiaristolochene, in 100 mM Tris-HCl (pH 7.5), at 30°C

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368A to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 6.20; column kcat (s^-1) = 0.581; column kcat/Km (s^-1/uM) = 0.0937. captured primary segment: Table II | enzyme S368A | substrate 1b(OH)EA | product CD | Km 6.20 +/- 0.47 uM | kcat 0.581 +/- 0.012 s^-1 | kcat/Km 0.0937 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 6.20 uM; 1 uM is 1/1000 mM, so 6.20 / 1000 = 0.006200000000000001 mM; the exported value is 0.0062 mM. kcat: printed Table II kcat cell 0.581 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.581 s^(-1); the exported value is 0.581 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0937 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0937 x 1000 = 93.7 s^(-1)*mM^(-1); the exported value is 93.70967741935483 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.581 / 0.006200000000000001 = 93.70967741935482 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate 1b(OH)EA, Product CD: Km = 6.20 uM; kcat = 0.581 s^-1; printed kcat/Km = 0.0937 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate 1b(OH)EA, Product CD


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row Wild-type, Substrate 1b(OH)EA, Product CD; column Km (uM) = 1.74; column kcat (s^-1) = 0.582; column kcat/Km (s^-1/uM) = 0.3344. captured primary segment: Table II | enzyme Wild-type | substrate 1b(OH)EA | product CD | Km 1.74 +/- 0.08 uM | kcat 0.582 +/- 0.006 s^-1 | kcat/Km 0.3344 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 1.74 uM; 1 uM is 1/1000 mM, so 1.74 / 1000 = 0.00174 mM; the exported value is 0.00174 mM. kcat: printed Table II kcat cell 0.582 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.582 s^(-1); the exported value is 0.582 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.3344 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.3344 x 1000 = 334.4 s^(-1)*mM^(-1); the exported value is 334.48275862068965 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.582 / 0.00174 = 334.48275862068965 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row Wild-type, Substrate 1b(OH)EA, Product CD: Km = 1.74 uM; kcat = 0.582 s^-1; printed kcat/Km = 0.3344 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row Wild-type, Substrate 1b(OH)EA, Product CD


organism: Zea mays

substrate_name: indole

kcat_display: Not reported

kcat_over_km_display: Not reported

proof_lines: native enzyme, in 50 mM potassium phosphate, pH 7.5, at 25°C

proof_lines: recombinant enzyme, in 50 mM potassium phosphate, pH 7.5, at 25°C

substrate: indole


enzyme_display_name: sterol 14alpha-demethylase

organism: Aspergillus fumigatus

substrate_name: lanosterol

proof_lines: isozyme CYP51B, pH not specified in the publication, temperature not specified in the publication

enzyme: sterol 14alpha-demethylase

substrate: lanosterol


substrate_name: eburicol

sequence_source: multiple

source_databases_merged: brenda uniprot

substrate: eburicol


enzyme_display_name: angelicin synthase

organism: Pastinaca sativa

substrate_name: NADPH; O2; H+; Columbianetin

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

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: pH 7.0, isopropyloxy-hydroxylation of substrate

proof_lines: pH 7.0, anti-3'-hydroxylation of substrate

source_databases_merged: sabio_rk brenda uniprot

enzyme: angelicin synthase

substrate: NADPH; O2; H+; Columbianetin


substrate_name: NADPH; H+; O2; 5-Epiaristolochene

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

assay_conditions_summary: cofactor NADPH

substrate: NADPH; H+; O2; 5-Epiaristolochene


enzyme_display_name: Lanosterol 14-alpha demethylase

organism: Homo sapiens

substrate_name: Unknown

source_db: uniprot

km_display: Not reported

enzyme: Lanosterol 14-alpha demethylase

substrate: Unknown

source: uniprot


enzyme_display_name: Lanosterol 14-alpha demethylase CYP51

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Lanosterol 14-alpha demethylase CYP51


enzyme_display_name: premnaspirodiene oxygenase

organism: Hyoscyamus muticus

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 1; row label HPO | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | EA | 2beta-(OH)EA': Km 3.3 uM; kcat 0.2 s^-1; kcat/Km 0.06 s^-1 uM^-1.

row_label: HPO | EA | 2beta-(OH)EA

table_label: Table 1

enzyme: premnaspirodiene oxygenase


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V480I/A484I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V480I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V480I/A484I | EA | 2beta-(OH)EA': Km 2.5 uM; kcat 0.7 s^-1; kcat/Km 0.28 s^-1 uM^-1.

row_label: HPO, V480I/A484I | EA | 2beta-(OH)EA

table_label: Table 3

status: verified


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:A6YIH8 and applied mutation signature V482I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V482I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | EA | 2beta-(OH)EA': Km 17.9 uM; kcat 1.4 s^-1; kcat/Km 0.08 s^-1 uM^-1.

row_label: HPO, V482I | EA | 2beta-(OH)EA


substrate_name: valencene

column_label: Table 1; row label HPO | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | Valencene | beta-Nootkatol': Km 7.4 uM; kcat 1.9 s^-1; kcat/Km 0.26 s^-1 uM^-1.

row_label: HPO | Valencene | beta-Nootkatol

substrate: valencene


substrate_name: (-)-vetispiradiene

column_label: Table 1; row label HPO | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | PSD | Solavetivol': Km 14 uM; kcat 2.1 s^-1; kcat/Km 0.15 s^-1 uM^-1.

row_label: HPO | PSD | Solavetivol

substrate: (-)-vetispiradiene


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:A6YIH8 and applied mutation signature V482I/A484I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V482I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | EA | 2beta-(OH)EA': Km 4.3 uM; kcat 2.8 s^-1; kcat/Km 0.65 s^-1 uM^-1.

row_label: HPO, V482I/A484I | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | PSD | Solavetivol': Km 6.2 uM; kcat 3.8 s^-1; kcat/Km 0.61 s^-1 uM^-1.

row_label: HPO, V482I | PSD | Solavetivol


column_label: Table 3; row label HPO, V482I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | Valencene | beta-Nootkatol': Km 6.9 uM; kcat 5.1 s^-1; kcat/Km 0.74 s^-1 uM^-1.

row_label: HPO, V482I | Valencene | beta-Nootkatol


kcat_over_km_origin: calculated

proof_lines: mutant enzyme V480I/A484I, product is beta-nootkatol, in 100 mM Tris-HCl, pH 7.5, at 30°C


proof_lines: mutant enzyme V480I/A484I, in 100 mM Tris-HCl, pH 7.5, at 30°C


column_label: Table 3; row label HPO, V482I/A484I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | Valencene | beta-Nootkatol': Km 12.1 uM; kcat 15.9 s^-1; kcat/Km 1.31 s^-1 uM^-1.


column_label: Table 3; row label HPO, V482I/A484I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | PSD | Solavetivol': Km 13 uM; kcat 20.7 s^-1; kcat/Km 1.59 s^-1 uM^-1.

row_label: HPO, V482I/A484I | PSD | Solavetivol


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

column_label: Table 1 row Lanosterol; column group C. albicans; metric column K_M^a; footnote a gives uM.

normalized_value_unit_evidence: 15.0 uM = 0.015 mM, which does not match package Km 0.0063 mM.

raw_value_unit_evidence: Table 1 row Lanosterol, C. albicans CYP51 orthologue, K_M^a column: 15.0; footnote a = uM.

row_label: Lanosterol


column_label: Table 1 row Dihydrolanosterol; column group C. albicans; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Dihydrolanosterol, C. albicans CYP51 orthologue, K_M^a column: 25.0; footnote a = uM.

row_label: Dihydrolanosterol


column_label: Table 1 row 24-methyleneDHL; column group C. albicans; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row 24-methyleneDHL, C. albicans CYP51 orthologue, K_M^a column: 11.0; footnote a = uM.


substrate_name: obtusifoliol

column_label: Table 1 row Obtusifoliol; column group C. albicans; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Obtusifoliol, C. albicans CYP51 orthologue, K_M^a column: 28.5; footnote a = uM.

row_label: Obtusifoliol

substrate: obtusifoliol


substrate_name: NADPH; O2; Vetispiradiene

substrate: NADPH; O2; Vetispiradiene


substrate_name: NADPH; Vetispiradiene; O2

assay_conditions_summary: cofactor NADP+

substrate: NADPH; Vetispiradiene; O2


substrate_name: Obtusifoliol; NADPH; H+; O2

substrate: Obtusifoliol; NADPH; H+; O2


substrate_name: NADPH; H+; O2; Eburicol

substrate: NADPH; H+; O2; Eburicol


organism: Candida albicans

substrate_name: H+; Lanosterol; NADPH; O2

substrate: H+; Lanosterol; NADPH; O2


enzyme_display_name: UniProt A2TEF2

organism: Leishmania infantum

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A2TEF2

source: skid


organism: Rattus norvegicus

substrate_name: Lanosterol; H+; NADPH; O2

substrate: Lanosterol; H+; NADPH; O2


column_label: Table 1 row Lanosterol; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Lanosterol, Human CYP51 orthologue, K_M^a column: 29; footnote a = uM.


column_label: Table 1 row Dihydrolanosterol; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Dihydrolanosterol, Human CYP51 orthologue, K_M^a column: 27; footnote a = uM.


column_label: Table 1 row 24-methyleneDHL; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row 24-methyleneDHL, Human CYP51 orthologue, K_M^a column: 32; footnote a = uM.


column_label: Table 1 row Obtusifoliol; column group Human; metric column K_M^a; footnote a gives uM.

raw_value_unit_evidence: Table 1 row Obtusifoliol, Human CYP51 orthologue, K_M^a column: 32; footnote a = uM.


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row EA -> CD; raw Km cell 19.18 +/- 2.90 uM; normalized Km 0.01918 mM. EA is 5-epiaristolochene in the article text.

raw_value_unit_evidence: Km raw_value=19.18 +/- 2.90 raw_unit=uM

row_label: EA -> CD


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row 3alpha(OH)EA -> CD; raw Km cell 6.38 +/- 0.42 uM; normalized Km 0.00638 mM. 3alpha-hydroxy-EA is the 1-deoxycapsidiol monohydroxylated intermediate of capsidiol.

raw_value_unit_evidence: Km raw_value=6.38 +/- 0.42 raw_unit=uM

row_label: 3alpha(OH)EA -> CD


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row 1beta(OH)EA -> CD; raw Km cell 1.74 +/- 0.08 uM; normalized Km 0.00174 mM. 1beta-hydroxy-EA is the 3-deoxycapsidiol monohydroxylated intermediate of capsidiol.

raw_value_unit_evidence: Km raw_value=1.74 +/- 0.08 raw_unit=uM

row_label: 1beta(OH)EA -> CD


enzyme_display_name: UniProt P00183

organism: Pseudomonas putida

substrate_name: NADH

enzyme: UniProt P00183

substrate: NADH


substrate_name: imidazole

substrate: imidazole


enzyme_display_name: ecgonone synthase

organism: Atropa belladonna

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

enzyme: ecgonone synthase


source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature I486A to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 21.24; column kcat (s^-1) = 0.132; column kcat/Km (s^-1/uM) = 0.0062. captured primary segment: Table II | enzyme I486A | substrate 1b(OH)EA | product CD | Km 21.24 +/- 2.84 uM | kcat 0.132 +/- 0.008 s^-1 | kcat/Km 0.0062 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 21.24 uM; 1 uM is 1/1000 mM, so 21.24 / 1000 = 0.02124 mM; the exported value is 0.02124 mM. kcat: printed Table II kcat cell 0.132 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.132 s^(-1); the exported value is 0.132 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0062 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0062 x 1000 = 6.2 s^(-1)*mM^(-1); the exported value is 6.214689265536724 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.132 / 0.02124 = 6.214689265536724 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate 1b(OH)EA, Product CD: Km = 21.24 uM; kcat = 0.132 s^-1; printed kcat/Km = 0.0062 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate 1b(OH)EA, Product CD

source: oed


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate 1b(OH)EA, Product CD; column Km (uM) = 6.20; column kcat (s^-1) = 0.581; column kcat/Km (s^-1/uM) = 0.0937. captured primary segment: Table II | enzyme S368A | substrate 1b(OH)EA | product CD | Km 6.20 +/- 0.47 uM | kcat 0.581 +/- 0.012 s^-1 | kcat/Km 0.0937 s^-1/uM

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate 1b(OH)EA, Product CD: Km = 6.20 uM; kcat = 0.581 s^-1; printed kcat/Km = 0.0937 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate 1b(OH)EA, Product CD


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368T, Substrate 1b(OH)EA, Product CD; column Km (uM) = 9.97; column kcat (s^-1) = 0.482; column kcat/Km (s^-1/uM) = 0.0483. captured primary segment: Table II | enzyme S368T | substrate 1b(OH)EA | product CD | Km 9.97 +/- 1.14 uM | kcat 0.482 +/- 0.019 s^-1 | kcat/Km 0.0483 s^-1/uM

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368T, Substrate 1b(OH)EA, Product CD: Km = 9.97 uM; kcat = 0.482 s^-1; printed kcat/Km = 0.0483 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368T, Substrate 1b(OH)EA, Product CD


column_label: Table I. EAH kinetic constants for EA and monohydroxylated intermediates row 1beta(OH)EA -> CD; raw cells kcat 0.582 +/- 0.006, Km 1.74 +/- 0.08 uM, kcat/Km 0.3344 s^-1/uM; normalized cells kcat 0.582 s^-1, Km 0.00174 mM, kcat/Km 334.4 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.582 normalized_unit=s^-1; Km normalized_value=0.00174 normalized_unit=mM; kcat/Km normalized_value=334.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.582 +/- 0.006 raw_unit=s^-1; Km raw_value=1.74 +/- 0.08 raw_unit=uM; kcat/Km raw_value=0.3344 raw_unit=s^-1*uM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368C to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368C, Substrate EA, Product 1b(OH)EA; column Km (uM) = 38.63; column kcat (s^-1) = 0.278; column kcat/Km (s^-1/uM) = 0.0072. captured primary segment: Table II | enzyme S368C | substrate EA | product 1b(OH)EA | Km 38.63 +/- 2.64 uM | kcat 0.278 +/- 0.008 s^-1 | kcat/Km 0.0072 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 38.63 uM; 1 uM is 1/1000 mM, so 38.63 / 1000 = 0.038630000000000005 mM; the exported value is 0.03863 mM. kcat: printed Table II kcat cell 0.278 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.278 s^(-1); the exported value is 0.278 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0072 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0072 x 1000 = 7.2 s^(-1)*mM^(-1); the exported value is 7.196479420139789 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.278 / 0.038630000000000005 = 7.196479420139788 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368C, Substrate EA, Product 1b(OH)EA: Km = 38.63 uM; kcat = 0.278 s^-1; printed kcat/Km = 0.0072 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368C, Substrate EA, Product 1b(OH)EA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q94FM7 and applied mutation signature S368V to reconstruct the assayed variant sequence.

column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368V, Substrate EA, Product 1b(OH)EA; column Km (uM) = 16.72; column kcat (s^-1) = 0.553; column kcat/Km (s^-1/uM) = 0.0331. captured primary segment: Table II | enzyme S368V | substrate EA | product 1b(OH)EA | Km 16.72 +/- 2.21 uM | kcat 0.553 +/- 0.025 s^-1 | kcat/Km 0.0331 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 16.72 uM; 1 uM is 1/1000 mM, so 16.72 / 1000 = 0.01672 mM; the exported value is 0.01672 mM. kcat: printed Table II kcat cell 0.553 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.553 s^(-1); the exported value is 0.553 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0331 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0331 x 1000 = 33.099999999999994 s^(-1)*mM^(-1); the exported value is 33.07416267942584 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.553 / 0.01672 = 33.07416267942584 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368V, Substrate EA, Product 1b(OH)EA: Km = 16.72 uM; kcat = 0.553 s^-1; printed kcat/Km = 0.0331 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368V, Substrate EA, Product 1b(OH)EA


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row I486A, Substrate EA, Product 1b(OH)EA; column Km (uM) = 68.80; column kcat (s^-1) = 0.293; column kcat/Km (s^-1/uM) = 0.0043. captured primary segment: Table II | enzyme I486A | substrate EA | product 1b(OH)EA | Km 68.80 +/- 4.04 uM | kcat 0.293 +/- 0.010 s^-1 | kcat/Km 0.0043 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 68.80 uM; 1 uM is 1/1000 mM, so 68.80 / 1000 = 0.0688 mM; the exported value is 0.069 mM. kcat: printed Table II kcat cell 0.293 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.293 s^(-1); the exported value is 0.293 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0043 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0043 x 1000 = 4.3 s^(-1)*mM^(-1); the exported value is 4.246376811594202 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.293 / 0.0688 = 4.258720930232558 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row I486A, Substrate EA, Product 1b(OH)EA: Km = 68.80 uM; kcat = 0.293 s^-1; printed kcat/Km = 0.0043 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row I486A, Substrate EA, Product 1b(OH)EA


column_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM). Enzyme row S368A, Substrate EA, Product CD; column Km (uM) = 22.67; column kcat (s^-1) = 0.154; column kcat/Km (s^-1/uM) = 0.0068. captured primary segment: Table II | enzyme S368A | substrate EA | product CD | Km 22.67 +/- 4.00 uM | kcat 0.154 +/- 0.009 s^-1 | kcat/Km 0.0068 s^-1/uM

normalized_value_unit_evidence: Km: printed Table II Km cell 22.67 uM; 1 uM is 1/1000 mM, so 22.67 / 1000 = 0.022670000000000003 mM; the exported value is 0.023 mM. kcat: printed Table II kcat cell 0.154 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.154 s^(-1); the exported value is 0.154 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0068 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0068 x 1000 = 6.8 s^(-1)*mM^(-1); the exported value is 6.695652173913044 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.154 / 0.022670000000000003 = 6.793118659020731 s^-1 mM^-1.

raw_value_unit_evidence: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA, Enzyme row S368A, Substrate EA, Product CD: Km = 22.67 uM; kcat = 0.154 s^-1; printed kcat/Km = 0.0068 s^-1/uM (the catalytic-efficiency cell).

row_label: Table II, Enzyme row S368A, Substrate EA, Product CD


normalized_value_unit_evidence: Km: printed Table II Km cell 38.63 uM; 1 uM is 1/1000 mM, so 38.63 / 1000 = 0.038630000000000005 mM; the exported value is 0.039 mM. kcat: printed Table II kcat cell 0.278 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.278 s^(-1); the exported value is 0.278 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0072 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0072 x 1000 = 7.2 s^(-1)*mM^(-1); the exported value is 7.128205128205129 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.278 / 0.038630000000000005 = 7.196479420139788 s^-1 mM^-1.

table_label: Table II: Comparison of the kinetic constants for EAH and several site-specific mutants for the initial substrate (EA) and the monohydroxylated intermediate 1b(OH)EA (J Biol Chem. 2005, 280(5): 3686-3696), printed column heads Enzyme | Substrate | Product | Km (uM) | kcat (s^-1) | kcat/Km (s^-1/uM)


normalized_value_unit_evidence: Km: printed Table II Km cell 16.72 uM; 1 uM is 1/1000 mM, so 16.72 / 1000 = 0.01672 mM; the exported value is 0.017 mM. kcat: printed Table II kcat cell 0.553 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 0.553 s^(-1); the exported value is 0.553 s^(-1). kcat/Km: printed Table II kcat/Km cell 0.0331 s^-1/uM; 1 s^-1/uM is 1000 s^-1 mM^-1, so 0.0331 x 1000 = 33.099999999999994 s^(-1)*mM^(-1); the exported value is 32.529411764705884 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.553 / 0.01672 = 33.07416267942584 s^-1 mM^-1.


enzyme_display_name: taxoid 7beta-hydroxylase

organism: Taxus cuspidata

substrate_name: (+)-taxusin

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: taxoid 7beta-hydroxylase

substrate: (+)-taxusin


enzyme_display_name: UniProt Q06069

organism: Priestia megaterium

enzyme: UniProt Q06069


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V480I/A484I to reconstruct the assayed variant sequence.

column_label: Table 3; row label HPO, V480I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V480I/A484I | EA | 2beta-(OH)EA': Km 2.5 uM; kcat 0.7 s^-1; kcat/Km 0.28 s^-1 uM^-1.

row_label: HPO, V480I/A484I | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | EA | 2beta-(OH)EA': Km 17.9 uM; kcat 1.4 s^-1; kcat/Km 0.08 s^-1 uM^-1.

row_label: HPO, V482I | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I/A484I | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | EA | 2beta-(OH)EA': Km 4.3 uM; kcat 2.8 s^-1; kcat/Km 0.65 s^-1 uM^-1.

row_label: HPO, V482I/A484I | EA | 2beta-(OH)EA


column_label: Table 1; row label HPO | EA | 2beta-(OH)EA; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | EA | 2beta-(OH)EA': Km 3.3 uM; kcat 0.2 s^-1; kcat/Km 0.06 s^-1 uM^-1.

row_label: HPO | EA | 2beta-(OH)EA


column_label: Table 3; row label HPO, V482I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | Valencene | beta-Nootkatol': Km 6.9 uM; kcat 5.1 s^-1; kcat/Km 0.74 s^-1 uM^-1.

row_label: HPO, V482I | Valencene | beta-Nootkatol


column_label: Table 3; row label HPO, V482I/A484I | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | Valencene | beta-Nootkatol': Km 12.1 uM; kcat 15.9 s^-1; kcat/Km 1.31 s^-1 uM^-1.


column_label: Table 1; row label HPO | Valencene | beta-Nootkatol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | Valencene | beta-Nootkatol': Km 7.4 uM; kcat 1.9 s^-1; kcat/Km 0.26 s^-1 uM^-1.

row_label: HPO | Valencene | beta-Nootkatol


column_label: Table 3; row label HPO, V482I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat_over_km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I | PSD | Solavetivol': Km 6.2 uM; kcat 3.8 s^-1; kcat/Km 0.61 s^-1 uM^-1.

row_label: HPO, V482I | PSD | Solavetivol


enzyme_display_name: taxoid 2alpha-hydroxylase

substrate_name: taxusin

enzyme: taxoid 2alpha-hydroxylase

substrate: taxusin


enzyme_display_name: Sterol 14-alpha demethylase cyp51B

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

enzyme: Sterol 14-alpha demethylase cyp51B


substrate_name: lanosterol

column_label: PDF text lines 285-303 contain Table I. Rendered PDF page 4 visually confirms the Lanosterol row and Km (uM) column value 165.

normalized_value_unit_evidence: Lanosterol Km 165 uM normalizes to 0.165 mM, not the current 0.0105 mM.

raw_value_unit_evidence: Table I Lanosterol row reports Km 165 uM, Ki 100 uM, Vmax 3390 pmol/min/mg, Vmax/Km 20.5, accumulated oxysterol 25%.

row_label: Lanosterol

table_label: Table I. Kinetic constants and effect of mutual competitive inhibitors upon accumulation of oxysterol demethylation intermediates

substrate: lanosterol


column_label: PDF text lines 285-303 contain Table I. Rendered PDF page 4 visually confirms the Dihydrolanosterol row and Km (uM) column value 312.

normalized_value_unit_evidence: Dihydrolanosterol Km 312 uM normalizes to 0.312 mM, not the current 0.02 mM.

raw_value_unit_evidence: Table I Dihydrolanosterol row reports Km 312 uM, Ki 298 uM, Vmax 645 pmol/min/mg, Vmax/Km 2.1, accumulated oxysterol 15%.

row_label: Dihydrolanosterol


substrate_name: eburicol

substrate: eburicol


enzyme_display_name: UniProt P9WPP3

organism: Mycobacterium tuberculosis

substrate_name: 15-methylpalmitic acid

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

enzyme: UniProt P9WPP3

substrate: 15-methylpalmitic acid


substrate_name: phytanic acid

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

substrate: phytanic acid


enzyme_display_name: UniProt P10614

organism: Saccharomyces cerevisiae

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

proof_lines: Yeast P-45014DM shows substrate-specific 14a-demethylation of 24-methylene-24,25-dihydrolanosterol and lanosterol.

source_databases_merged: skid uniprot

enzyme: UniProt P10614


organism: Papaver somniferum

substrate_name: (S)-N-methylcanadine

substrate: (S)-N-methylcanadine


substrate_name: (-)-vetispiradiene

column_label: Table 3; row label HPO, V482I/A484I | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1); required metrics checked: kcat, kcat_over_km, km.

raw_value_unit_evidence: Table 3 row 'HPO, V482I/A484I | PSD | Solavetivol': Km 13 uM; kcat 20.7 s^-1; kcat/Km 1.59 s^-1 uM^-1.

row_label: HPO, V482I/A484I | PSD | Solavetivol

substrate: (-)-vetispiradiene


column_label: Table 1; row label HPO | PSD | Solavetivol; columns Km (uM), kcat (s^-1), kcat/Km (s^-1 uM^-1).

raw_value_unit_evidence: Table 1 row 'HPO | PSD | Solavetivol': Km 14 uM; kcat 2.1 s^-1; kcat/Km 0.15 s^-1 uM^-1.

row_label: HPO | PSD | Solavetivol


enzyme_display_name: Premnaspirodiene oxygenase

substrate_name: premnaspirodiene

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

column_label: Table 1; row label HPO | PSD | Solavetivol; required column Km (uM); substrate PSD; product/readout Solavetivol.

normalized_value_unit_evidence: Km 0.014 mM for the required metric; table also reports kcat 2.1 s^-1 and kcat/Km 150 s^-1 mM^-1.

enzyme: Premnaspirodiene oxygenase

substrate: premnaspirodiene


substrate_name: solavetivol

column_label: Table 1; row label HPO | Solavetivol | Solavetivone; required column Km (uM); substrate Solavetivol; product/readout Solavetivone.

normalized_value_unit_evidence: Km 0.0012 mM for the required metric; table also reports kcat 0.1 s^-1 and kcat/Km 80 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 'HPO | Solavetivol | Solavetivone': Km 1.2 uM; kcat 0.1 s^-1; kcat/Km 0.08 s^-1 uM^-1.

row_label: HPO | Solavetivol | Solavetivone

substrate: solavetivol


substrate_name: valencene

column_label: Table 1; row label HPO | Valencene | alpha-Nootkatol; required column Km (uM); substrate Valencene; product/readout alpha-Nootkatol.

normalized_value_unit_evidence: Km 0.0115 mM for the required metric; table also reports kcat 0.1 s^-1 and kcat/Km 10 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 'HPO | Valencene | alpha-Nootkatol': Km 11.5 uM; kcat 0.1 s^-1; kcat/Km 0.01 s^-1 uM^-1.

row_label: HPO | Valencene | alpha-Nootkatol

substrate: valencene


column_label: Table 1; row label HPO | EA | 2beta-(OH)EA; required column Km (uM); substrate EA; product/readout 2beta-(OH)EA.

normalized_value_unit_evidence: Km 0.0033 mM for the required metric; table also reports kcat 0.2 s^-1 and kcat/Km 60 s^-1 mM^-1.


column_label: Table 1; row label HPO | Cedr-8-ene | Cedr-8-en-15-ol; required column Km (uM); substrate Cedr-8-ene; product/readout Cedr-8-en-15-ol.

normalized_value_unit_evidence: Km 0.0265 mM for the required metric; table also reports kcat 0.1 s^-1 and kcat/Km 0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 'HPO | Cedr-8-ene | Cedr-8-en-15-ol': Km 26.5 uM; kcat 0.1 s^-1; kcat/Km 0 s^-1 uM^-1.

row_label: HPO | Cedr-8-ene | Cedr-8-en-15-ol


enzyme_display_name: UniProt P18326

organism: Streptomyces griseolus

substrate_name: 1alpha,25-dihydroxyvitamin D3

enzyme: UniProt P18326

substrate: 1alpha,25-dihydroxyvitamin D3


enzyme_display_name: UniProt P9WPP1

enzyme: UniProt P9WPP1


enzyme_display_name: (S)-N-methylcanadine 1-hydroxylase

substrate_name: (S)-N-Methylcanadine; H+; O2; NADPH

enzyme: (S)-N-methylcanadine 1-hydroxylase

substrate: (S)-N-Methylcanadine; H+; O2; NADPH


enzyme_display_name: UniProt F1CMX0

organism: Rhodococcus rhodochrous

enzyme: UniProt F1CMX0


enzyme_display_name: UniProt F1CMY8

enzyme: UniProt F1CMY8


enzyme_display_name: UniProt P71875

enzyme: UniProt P71875


smiles: O=O


substrate_name: testosterone

substrate: testosterone


enzyme_display_name: UniProt Q00441

organism: Saccharopolyspora erythraea

enzyme: UniProt Q00441


substrate_name: androstenedione

substrate: androstenedione


substrate_name: dehydroepiandrostenedione

substrate: dehydroepiandrostenedione


enzyme_display_name: sterol 14alpha-demethylase

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

enzyme: sterol 14alpha-demethylase


substrate_name: obtusifoliol

substrate: obtusifoliol


enzyme_display_name: Rhazimal synthase

organism: Alstonia scholaris

substrate_name: geissoschizine

enzyme: Rhazimal synthase

substrate: geissoschizine


enzyme_display_name: 6-deoxyerythronolide B hydroxylase

organism: Actinopolyspora erythraea

substrate_name: 6-Deoxyerythronolide b

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

enzyme: 6-deoxyerythronolide B hydroxylase

substrate: 6-Deoxyerythronolide b


enzyme_display_name: 3-ketosteroid 9alpha-monooxygenase

substrate_name: 3-oxo-23,24-bisnorchol-4-en-22-oic acid

enzyme: 3-ketosteroid 9alpha-monooxygenase

substrate: 3-oxo-23,24-bisnorchol-4-en-22-oic acid


assay_conditions_summary: pH 7; 295.15 K; cofactor CoA


enzyme_display_name: sterol 14alpha-demethylase (ferredoxin)

organism: Nocardia farcinica

substrate_name: lanosterol

assay_conditions_summary: pH 7

proof_lines: wild-type, pH 7.0, temperature not specified in the publication

enzyme: sterol 14alpha-demethylase (ferredoxin)

substrate: lanosterol


proof_lines: FprD fusion construct F1, pH 7.0, temperature not specified in the publication

proof_lines: FprD fusion construct F2, pH 7.0, temperature not specified in the publication


organism: Sinomonas cyclohexanicum

proof_lines: pH and temperature not specified in the publication


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.9


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A245T to reconstruct the assayed variant sequence.

proof_lines: mutant A245T, pH 7.5, 37°C, S50 value, Hill coefficient 1.7


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.2


proof_lines: mutant A245T, pH 7.5, 37°C, S50 value, Hill coefficient 1.09


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.64


proof_lines: wild-type, pH 7.5, 37°C, S50 value, Hill coefficient 1.55


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 4-BNC (at pH 7 and at 22 degrees Celsius)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 2.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7 and at 22 degrees Celsius) (PubMed:21987574). kcat is 0.8 sec(-1) for ADD as substrate (at pH 7 and at 25 degrees Celsius) (PubMed:19234303). kcat is 0.61 sec(-1) for 4-BNC-CoA as su


substrate_name: 4-BNC-CoA (at pH 7 and at 22 degrees Celsius)


substrate_name: 1,4-BNC-CoA (at pH 7 and at 22 degrees Celsius)

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


substrate_name: 1,4-BNC (at pH 7 and at 22 degrees Celsius)


enzyme_display_name: 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component

substrate: 4-BNC (at pH 7 and at 22 degrees Celsius)


enzyme: 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component

substrate: 4-BNC-CoA (at pH 7 and at 22 degrees Celsius)


substrate: 1,4-BNC-CoA (at pH 7 and at 22 degrees Celsius)


substrate: 1,4-BNC (at pH 7 and at 22 degrees Celsius)


substrate_name: AD (at pH 7 and at 25 degrees Celsius)

substrate: AD (at pH 7 and at 25 degrees Celsius)


proof_lines: kcat is 1.7 sec(-1) for 1,4-BNC-CoA as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 0.8 sec(-1) for 5alpha-androstan-3,17-dione, AD and testosterone as substrates (at pH 7.0 and 22 degrees Celsius). kcat is 0.7 sec(-1) for ADD as s


proof_lines: kcat is 2.6 sec(-1) for 4-BNC as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.4 sec(-1) for testosterone as substrate (at pH 7.0 and 22 degrees Celsius). kcat is 1.3 sec(-1) for ADD as substrate (at pH 7.0 and 22 degrees Celsius)


enzyme_display_name: Pentalenene oxygenase

organism: Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)

substrate_name: active enantiomer of pentalenene

proof_lines: kcat is 0.503 min(-1) with active enantiomer of pentalenene as substrate.

enzyme: Pentalenene oxygenase

substrate: active enantiomer of pentalenene


enzyme_display_name: L-tyrosine 3-nitrase

organism: Streptomyces atratus

substrate_name: Nle-RYLH

proof_lines: kcat is 0.25 min(-1) with Nle-RYLH as substrate.

enzyme: L-tyrosine 3-nitrase

substrate: Nle-RYLH


enzyme_display_name: pentalenene oxygenase

organism: Streptomyces avermitilis

substrate_name: (+/-)-pentalenene

assay_conditions_summary: pH 7.4; 295.15 K; buffer phosphate

proof_lines: recombinant enzyme, in 50 mM phosphate buffer, 10% (v/v) glycerol, pH 7.4, at 22°C

enzyme: pentalenene oxygenase

substrate: (+/-)-pentalenene


enzyme_display_name: UniProt P04176

organism: Rattus norvegicus

substrate_name: L-phenylalanine

enzyme: UniProt P04176

substrate: L-phenylalanine


enzyme_display_name: UniProt P30967

organism: Chromobacterium violaceum

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P30967


substrate_name: L-tryptophan

substrate: L-tryptophan


enzyme_display_name: UniProt P00439

organism: Homo sapiens

substrate_name: S-carboxymethyl-L-cysteine

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

enzyme: UniProt P00439

substrate: S-carboxymethyl-L-cysteine


substrate_name: (S)-methyl-L-cysteine

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

substrate: (S)-methyl-L-cysteine


substrate_name: S-methyl-L-cysteine

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

substrate: S-methyl-L-cysteine


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

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

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


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

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

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


enzyme_display_name: UniProt P17752

enzyme: UniProt P17752


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: UniProt P70080

organism: Gallus gallus

enzyme: UniProt P70080


organism: Aeromicrobium erythreum

substrate_name: 6-Deoxyerythronolide b

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

substrate: 6-Deoxyerythronolide b


enzyme_display_name: Cytochrome P450 monooxygenase PikC

organism: Streptomyces venezuelae

substrate_name: narbomycin

enzyme: Cytochrome P450 monooxygenase PikC

substrate: narbomycin


organism: Mycobacterium tuberculosis


organism: Rhodococcus rhodochrous

column_label: Table 2 identifies 5alpha-androstane-3,17-dione substrate row; adjacent Results prose reports Km = 23 +/- 2 uM

raw_value_unit_evidence: Results prose adjacent to Table 2; 5alpha-androstane-3,17-dione Km = 23 +/- 2 uM

table_label: Table 2. Steroid substrate range of the KSH enzyme of R. rhodochrous DSM 43269


organism: Saccharopolyspora erythraea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I379V to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH not specified in the publication, mutant enzyme I379V


proof_lines: 30°C, pH not specified in the publication, wild-type enzyme


column_label: Table 2 identifies 19-nor-AD / nordion substrate row; adjacent Results prose reports Km = 10 +/- 1 uM

raw_value_unit_evidence: Results prose adjacent to Table 2; 19-nor-AD / nordion Km = 10 +/- 1 uM


substrate_name: nordion

substrate: nordion


substrate_name: 3-oxo-23,24-bisnorchol-4-en-22-oic acid

proof_lines: in 0.1 M potassium phosphate, pH 7.0, at 22°C

substrate: 3-oxo-23,24-bisnorchol-4-en-22-oic acid


proof_lines: apparent Km value, in the presence of 3-oxo-23,24-bisnorchola-1,4-dien-22-oic acid-CoA, in 0.1 M potassium phosphate, pH 7.0, at 22°C

proof_lines: in the presence of 1,4-androstadiene-3,17-dione, kcat above 7 1/sec, in 0.1 M potassium phosphate, pH 7.0, at 25°C

proof_lines: in the presence of 1,4-androstadiene-3,17-dione, Km above 1.2 mM, in 0.1 M potassium phosphate, pH 7.0, at 25°C


assay_conditions_summary: pH 7; 295.15 K; buffer 50mMTris-HCl

proof_lines:
pH 7.0, 22°C
isoform KshA5, at pH 7.0 and 22°C
isoform KshA1, at pH 7.0 and 22°C


substrate_name: testosterone

substrate: testosterone


enzyme_display_name: catechol 1,2-dioxygenase

organism: Ralstonia sp.

enzyme: catechol 1,2-dioxygenase


substrate_name: catechol

substrate: catechol


enzyme_display_name: nitric-oxide synthase (NADPH)

substrate_name: NADPH

enzyme: nitric-oxide synthase (NADPH)

substrate: NADPH


enzyme_display_name: catechol 2,3-dioxygenase

organism: Stutzerimonas stutzeri

enzyme: catechol 2,3-dioxygenase


organism: Sus scrofa

substrate_name: dichlorophenolindophenol

substrate: dichlorophenolindophenol


substrate_name: nitroblue tetrazolium

substrate: nitroblue tetrazolium


substrate_name: L-arginine

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

substrate: L-arginine


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

organism: Zea mays

enzyme: 9-cis-epoxycarotenoid dioxygenase


enzyme_display_name: homogentisate 1,2-dioxygenase

organism: Aspergillus niger

substrate_name: homogentisate

enzyme: homogentisate 1,2-dioxygenase

substrate: homogentisate


enzyme_display_name: gibberellin 3beta-dioxygenase

organism: Arabidopsis sp.

substrate_name: gibberellin a9

enzyme: gibberellin 3beta-dioxygenase

substrate: gibberellin a9


substrate_name: gibberellin a20

substrate: gibberellin a20


enzyme_display_name: indole-3-pyruvate monooxygenase

organism: Arabidopsis thaliana

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: in the presence of phenylpyruvate, in 50 mM sodium phosphate, pH 8.0, 500 mM NaCl, and 30% (v/v) glycerol, at 25°C

enzyme: indole-3-pyruvate monooxygenase


substrate_name: phenylpyruvate

proof_lines: in the presence of NADPH, in 50 mM sodium phosphate, pH 8.0, 500 mM NaCl, and 30% (v/v) glycerol, at 25°C

substrate: phenylpyruvate


enzyme_display_name: nitric-oxide synthase (flavodoxin)

organism: Bacillus subtilis

enzyme: nitric-oxide synthase (flavodoxin)


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


enzyme_display_name: peptide-aspartate beta-dioxygenase

organism: Bos taurus

proof_lines:
56 kDa protein
52 kDa protein

enzyme: peptide-aspartate beta-dioxygenase


enzyme_display_name: taurine dioxygenase

organism: Escherichia coli

proof_lines: wild type enzyme, in the presence of taurine

enzyme: taurine dioxygenase


substrate_name: taurine

proof_lines:
wild type enzyme
wild-type, 30°C

substrate: taurine


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Desulfovibrio desulfuricans

substrate_name: ferrocytochrome c3

proof_lines:
H2-evolution assay
tetraheme cytochrome c3
nonaheme cytochrome c

enzyme: cytochrome-c3 hydrogenase

substrate: ferrocytochrome c3


substrate_name: reduced methyl viologen

substrate: reduced methyl viologen


enzyme_display_name: alkanesulfonate monooxygenase

substrate_name: octanesulfonate

enzyme: alkanesulfonate monooxygenase

substrate: octanesulfonate


substrate_name: NADH

assay_conditions_summary: pH 7.4; 295.15 K; cofactor NADH

proof_lines: pH 7.4, 22°C, recombinant wild-type enzyme

substrate: NADH


assay_conditions_summary: pH 7.4; 295.15 K; cofactor NADPH


organism: Felis catus

assay_conditions_summary: cofactor FAD

proof_lines:
with FAD and tetrahydropterin
without tetrahydropterin and FAD


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: cysteine dioxygenase

organism: Histoplasma capsulatum

substrate_name: L-cysteine

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

enzyme: cysteine dioxygenase

substrate: L-cysteine


substrate_name: beta-mercaptoethanol

smiles: C(CS)O

substrate: beta-mercaptoethanol


organism: Homo sapiens


enzyme_display_name: arachidonate 15-lipoxygenase

substrate_name: lipoic acid

enzyme: arachidonate 15-lipoxygenase

substrate: lipoic acid


substrate_name: arachidonic acid

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

proof_lines:
splice variant 15-LOb1
splice variant 15-LOb2

substrate: arachidonic acid


enzyme_display_name: UniProt P14925

organism: Rattus norvegicus

substrate_name: N-(Phenylacetyl)glycine

enzyme: UniProt P14925

substrate: N-(Phenylacetyl)glycine


substrate_name: hippuryl-Gly-Gly

substrate: hippuryl-Gly-Gly


substrate_name: hippuric acid

substrate: hippuric acid


substrate_name: 4-hydroxyhippuric acid

substrate: 4-hydroxyhippuric acid


substrate_name: isocaproylglycine

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

substrate: isocaproylglycine


substrate_name: 3-chlorohippuric acid

substrate: 3-chlorohippuric acid


substrate_name: phenylmercaptoacetylglycine

substrate: phenylmercaptoacetylglycine


substrate_name: 2-aminohippuric acid

substrate: 2-aminohippuric acid


substrate_name: 3-methylhippuric acid

substrate: 3-methylhippuric acid


substrate_name: 4-methylhippuric acid

substrate: 4-methylhippuric acid


substrate_name: cinnamoylglycine

substrate: cinnamoylglycine


substrate_name: nicotinuric acid

substrate: nicotinuric acid


substrate_name: 2-methylhippuric acid

substrate: 2-methylhippuric acid


substrate_name: 4-chlorohippuric acid

substrate: 4-chlorohippuric acid


substrate_name: 4-methoxyhippuric acid

substrate: 4-methoxyhippuric acid


substrate_name: CBZ-glycine

substrate: CBZ-glycine


substrate_name: 4-nitrohippuric acid

substrate: 4-nitrohippuric acid


substrate_name: phenylthioacetylglycine

substrate: phenylthioacetylglycine


substrate_name: phenylhydantoic acid

substrate: phenylhydantoic acid


substrate_name: 2-hydroxyhippuric acid

substrate: 2-hydroxyhippuric acid


substrate_name: N-dansyl-Tyr-Val-D-Ala

substrate: N-dansyl-Tyr-Val-D-Ala


substrate_name: hydrocinnamoylglycine

substrate: hydrocinnamoylglycine


substrate_name: 4-aminohippuric acid

substrate: 4-aminohippuric acid


substrate_name: 2-iodohippuric acid

substrate: 2-iodohippuric acid


substrate_name: CBZ-D-alanine

substrate: CBZ-D-alanine


substrate_name: 2,6-difluorohippuric acid

substrate: 2,6-difluorohippuric acid


substrate_name: benzoyl-D-alanine

substrate: benzoyl-D-alanine


substrate_name: N-acetylglycine

smiles: CC(=O)NCC(=O)O

proof_lines:
Raw SKiD Env: Temp=37°C, pH=6
Raw SKiD Env: Temp=-----, pH=-----

substrate: N-acetylglycine


enzyme_display_name: tyrosinase

organism: Streptomyces antibioticus

enzyme: tyrosinase


organism: Neurospora crassa

substrate_name: D-Tyr

substrate: D-Tyr


substrate_name: tyramine

substrate: tyramine


substrate_name: 4-hydroxyphenyl acetic acid

substrate: 4-hydroxyphenyl acetic acid


substrate_name: L-Dopa

substrate: L-Dopa


organism: Triticum aestivum


enzyme_display_name: UniProt B2ZB02

organism: Priestia megaterium

enzyme: UniProt B2ZB02


substrate_name: L-tyrosine

substrate: L-tyrosine


enzyme_display_name: UniProt C0LU17

organism: Juglans regia

enzyme: UniProt C0LU17


enzyme_display_name: UniProt C7FF04

organism: Agaricus bisporus

substrate_name: deoxyarbutin

enzyme: UniProt C7FF04

substrate: deoxyarbutin


substrate_name: beta-arbutin

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7

substrate: beta-arbutin


enzyme_display_name: trimethylamine monooxygenase

substrate_name: Methimazole

enzyme: trimethylamine monooxygenase

substrate: Methimazole


substrate_name: homogentisate

substrate: homogentisate


organism: Carthamus tinctorius


enzyme_display_name: arachidonate 12-lipoxygenase

substrate_name: O2; Arachidonate

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: arachidonate 12-lipoxygenase

substrate: O2; Arachidonate


enzyme_display_name: indoleamine 2,3-dioxygenase

proof_lines:
pH 6.5, 25°C, recombinant enzyme IDO1
recombinant enzyme
37°C, pH 6.5

enzyme: indoleamine 2,3-dioxygenase


proof_lines: pH and temperature not specified in the publication


substrate_name: 5,8,11,14,17-eicosapentaenoic acid

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

substrate: 5,8,11,14,17-eicosapentaenoic acid


substrate_name: 8,11,14-eicosatrienoic acid

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

substrate: 8,11,14-eicosatrienoic acid


substrate_name: L-tryptophan

assay_conditions_summary: pH 8

proof_lines: H76A mutant enzyme, pH 8.0, normal atmospheric conditions

substrate: L-tryptophan


proof_lines: Y42F mutant enzyme, pH 8.0, normal atmospheric conditions


substrate_name: arachidonic acid

assay_conditions_summary: pH 7.5; 288.15 K; buffer 25 mM Hepes

proof_lines:
at 15°C, pH 7.5
at 40°C, pH 7.5

substrate: arachidonic acid


assay_conditions_summary: pH 7.5; 298.15 K; buffer 25 mM Hepes

proof_lines: with arachidonic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid

proof_lines: with linoleic acid as substrate, in 25 mM Hepes buffer, pH 7.5, 25°C, in the presence of 12(S)-hydroperoxyeicosatetraenoic acid


substrate_name: Benzydamine

assay_conditions_summary: pH 7.4; 310.15 K; buffer 0.1 M tricine

proof_lines: in in 0.1 M tricine buffer, pH 7.4, at 37°C

substrate: Benzydamine


substrate_name: sulindac sulfide

assay_conditions_summary: pH 9; 310.15 K; buffer 0.1 M tricine

proof_lines: in in 0.1 M tricine buffer, pH 9.0, at 37°C

substrate: sulindac sulfide


substrate_name: D-tryptophan

substrate: D-tryptophan


proof_lines: recombinant wild-type enzyme, pH 7.4, 25°C

proof_lines: wild type, 50 mM potassium phosphate buffer (pH 6.5), 20 mM ascorbic acid, 0.3 mg/ml catalase, 0.01 mM methylene blue, 0.4 mM tryptophan, 37°C, 10-60 min


enzyme_display_name: 4alpha-methylsterol monooxygenase

enzyme: 4alpha-methylsterol monooxygenase


enzyme_display_name: UniProt E9P162

organism: Streptomyces toxytricini

substrate_name: anthranilamide

enzyme: UniProt E9P162

substrate: anthranilamide


substrate_name: kynurenine

substrate: kynurenine


enzyme_display_name: tryptophan 6-halogenase

organism: Streptomyces albogriseolus

enzyme: tryptophan 6-halogenase


substrate_name: bromide

substrate: bromide


substrate_name: chloride

substrate: chloride


enzyme_display_name: sphingolipid C4-monooxygenase

organism: Zea mays

substrate_name: NADPH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

enzyme: sphingolipid C4-monooxygenase

substrate: NADPH


substrate_name: NADH

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

substrate: NADH


substrate_name: D-erythro-sphinganine

smiles: CCCCCCCCCCCCCCCC(C(CO)N)O

substrate: D-erythro-sphinganine


enzyme_display_name: pseudobaptigenin synthase

organism: Cicer arietinum

substrate_name: Pratensein

enzyme: pseudobaptigenin synthase

substrate: Pratensein


substrate_name: Calycosin

substrate: Calycosin


assay_conditions_summary: pH 7.5; 285.15 K; cofactor NADPH

proof_lines: pH 7.5, 12°C, 5-hydroxypseudobaptigenin synthesis

proof_lines: pH 7.5, 12°C, pseudobaptigenin synthesis


enzyme_display_name: tryptophan 5-halogenase

organism: Xenorhabdus szentirmaii

proof_lines: with chloride as cosubstrate, at pH 7.4 and 37°C

enzyme: tryptophan 5-halogenase


enzyme_display_name: (S)-cheilanthifoline synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

enzyme: (S)-cheilanthifoline synthase

substrate: (S)-scoulerine


enzyme_display_name: sterol 22-desaturase

organism: Nakaseomyces glabratus

assay_conditions_summary: pH 6.8; cofactor NADPH

column_label: Abstract reports enzyme kinetic studies revealed a Km for ergosta-5,7-dienol of 12.5 microM.

raw_value_unit_evidence: Km raw_value=12.5 microM raw_unit=microM

row_label: Candida glabrata sterol delta22-desaturase / ergosta-5,7-dienol

table_label: PubMed XML abstract PMID 10390230

enzyme: sterol 22-desaturase


organism: uncultured bacterium


enzyme_display_name: UniProt P18548

organism: Streptomyces clavuligerus

substrate_name: Penicillin N

enzyme: UniProt P18548

substrate: Penicillin N


substrate_name: penicillin G

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.5

substrate: penicillin G


substrate_name: ampicillin

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.5

substrate: ampicillin


enzyme_display_name: 1,2-dehydroreticuline synthase

organism: Papaver rhoeas

substrate_name: (S)-reticuline

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: pH 7.8, temperature not specified in the publication

enzyme: 1,2-dehydroreticuline synthase

substrate: (S)-reticuline


column_label: Table 2, Kinetics of selected substrates with SttH wild type; row=kynurenine (4); metric columns=Km [uM], kcat [min^-1], kcat/Km [min^-1 mM^-1].

normalized_value_unit_evidence: Normalized values from the primary table: Km 0.241 mM; kcat 0.51/60 = 0.0085 s^-1; kcat/Km 2.1/60 = 0.035 s^-1 mM^-1.

row_label: kynurenine (4)

table_label: Table 2


column_label: Table 2, Kinetics of selected substrates with SttH wild type; row=anthranilamide (5); metric columns=Km [uM], kcat [min^-1], kcat/Km [min^-1 mM^-1].

row_label: anthranilamide (5)


enzyme_display_name: all-trans-retinol 3,4-desaturase

organism: Danio rerio

substrate_name: all-trans-retinal

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

enzyme: all-trans-retinol 3,4-desaturase

substrate: all-trans-retinal


substrate_name: all-trans-retinoic acid

substrate: all-trans-retinoic acid


substrate_name: all-trans-retinol

substrate: all-trans-retinol


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Actinomyces sp.

enzyme: deacetoxycephalosporin-C synthase


enzyme_display_name: (S)-canadine synthase

organism: Thalictrum tuberosum

substrate_name: (S)-tetrahydrocolumbamine

proof_lines: canadine synthase in complex with a cytochrome P-450 reductase

enzyme: (S)-canadine synthase

substrate: (S)-tetrahydrocolumbamine


substrate_name: [reduced NADPH-hemoprotein reductase]

assay_conditions_summary: cofactor NADPH

substrate: [reduced NADPH-hemoprotein reductase]


enzyme_display_name: salutaridine synthase

organism: Sus scrofa

substrate_name: (R)-reticuline

enzyme: salutaridine synthase

substrate: (R)-reticuline


organism: Hapsidospora chrysogena

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M306I to reconstruct the assayed variant sequence.

proof_lines: 30°C, double mutant with truncation at residue 310 and M306I


sequence_variant_note: Mutation signature M306I/N305L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: 30°C, triple mutant with truncation at residue 310, M306I and N305L


sequence_variant_note: Mutation signature N305L/M306I could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 30°C, recombinant mutant DELTA310/N305L/M306I


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 not specified in the publication, temperature not specified in the publication

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R308L to reconstruct the assayed variant sequence.

proof_lines: mutant R308L, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R308I to reconstruct the assayed variant sequence.

proof_lines: mutant R308I, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: Noroxomaritidine synthase

organism: Narcissus aff. pseudonarcissus MK-2014

assay_conditions_summary: pH 6.5; buffer 200 mM KPO4 pH 6.5

column_label: Table 5 row 4'-O-Methylnorbelladine, column Km (uM) = 1.13 +/- 0.54.

normalized_value_unit_evidence: Required Km: 1.13 uM = 0.00113 mM. Kcat and kcat/Km are present in the table but not required for this UniProt row.

raw_value_unit_evidence: Table 5 4'-O-Methylnorbelladine row: Km 1.13 +/- 0.54 uM; kcat 15.0 +/- 2.03 1/min; kcat/Km 13 1/uM*min; modifications monitored: C-C phenol coupling.

table_label: Table 5. Substrate specificity tests for CYP96T1.

enzyme: Noroxomaritidine synthase


substrate_name: (S)-coclaurine

column_label: Table 5 row (S)-Coclaurine, column Km (uM) = 637 +/- 156.

normalized_value_unit_evidence: Required Km: 637 uM = 0.637 mM. Kcat and kcat/Km are present in the table but not required for this UniProt row.

raw_value_unit_evidence: Table 5 (S)-Coclaurine row: Km 637 +/- 156 uM; kcat 1.34 +/- 0.15 1/min; kcat/Km 2.11 x 10^-3 1/uM*min; modifications monitored: intramolecular phenol coupling and intermolecular coupling.

row_label: (S)-Coclaurine

substrate: (S)-coclaurine


enzyme_display_name: sn-1 linoleoyl-lipid 6-desaturase

organism: Limnospira platensis

substrate_name: linoleic acid

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

enzyme: sn-1 linoleoyl-lipid 6-desaturase

substrate: linoleic acid


organism: Homo sapiens

proof_lines: pH 7.4, temperature not specified in the publication


enzyme_display_name: biflaviolin synthase

organism: Streptomyces coelicolor

substrate_name: flaviolin

proof_lines: wild type isoform CYP158A2, at pH 8.2 and 37°C

enzyme: biflaviolin synthase

substrate: flaviolin


proof_lines: wild type isoform CYP158A1, at pH 8.2 and 37°C


enzyme_display_name: UniProt Q9FCA6

proof_lines: kcat is 1.4 min(-1) with flaviolin as substrate (at pH 7.5 and 37 degrees Celsius). kcat is 0.02 min(-1) with 2-hydroxy-1,4-naphthoquinone as substrate (at pH 7.5 and 25 degrees Celsius).

enzyme: UniProt Q9FCA6


enzyme_display_name: UniProt Q9KZF5

proof_lines: kcat is 0.9 min(-1) with flaviolin as substrate (at pH 8.2 and 37 degrees Celsius).

enzyme: UniProt Q9KZF5


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R307L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N305L with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


enzyme_display_name: tryptophan 6-halogenase

organism: Streptomyces toxytricini

substrate_name: kynurenine

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

enzyme: tryptophan 6-halogenase

substrate: kynurenine


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: anthranilamide

substrate: anthranilamide


enzyme_display_name: Tryptophan 6-halogenase SttH

proof_lines: kcat is 1.53 min(-1) with L-tryptophan as substrate (PubMed:21424165). kcat is 0.65 min(-1) with tryptophan as substrate (PubMed:26840773). kcat is 0.51 min(-1) with kynurenine as substrate (PubMed:26840773). kcat is 1.21 min(-1) with anthr

enzyme: Tryptophan 6-halogenase SttH


enzyme_display_name: 2-hydroxy fatty acid dioxygenase

organism: Saccharomyces cerevisiae

substrate_name: (2R)-2-hydroxypalmitic acid

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

enzyme: 2-hydroxy fatty acid dioxygenase

substrate: (2R)-2-hydroxypalmitic acid


enzyme_display_name: tetracycline 7-halogenase

organism: Kitasatospora aureofaciens

proof_lines: kcat is 0.51 min(-1) for tetracycline (TC) as substrate.

enzyme: tetracycline 7-halogenase


organism: Papaver somniferum

proof_lines: pH 7.8, temperature not specified in the publication

proof_lines: Cyp82Y2 module, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: 7-chloro-L-tryptophan 6-halogenase

organism: Kutzneria sp. 744

assay_conditions_summary: pH 7; cofactor NADH

column_label: Prose states the KtzR kcat ratio for 7-Cl-L-Trp/L-Trp is 1.4 min^-1/0.08 min^-1 and the Km value for 7-Cl-L-Trp is 114 uM versus 808 uM for L-Trp.

normalized_value_unit_evidence: kcat normalized=0.0013 s^-1; Km normalized=0.808 mM; kcat/Km normalized=0.0016089108910891088 s^-1 mM^-1

raw_value_unit_evidence: kcat raw=0.08 min^-1; Km raw=808 uM; kcat/Km raw=computed from same prose kcat and Km

row_label: KtzR with L-Trp as halogenation substrate

table_label: PMC full text Results prose, KtzR kinetic characterization

enzyme: 7-chloro-L-tryptophan 6-halogenase


normalized_value_unit_evidence: kcat normalized=0.023 s^-1; Km normalized=0.114 mM; kcat/Km normalized=0.20175438596491227 s^-1 mM^-1

raw_value_unit_evidence: kcat raw=1.4 min^-1; Km raw=114 uM; kcat/Km raw=computed from same prose kcat and Km

row_label: KtzR with 7-Cl-L-Trp as halogenation substrate


enzyme_display_name: tryptophan 5-halogenase

organism: Streptomyces rugosporus

proof_lines:
pH 7.2, 30°C
Raw SKiD Env: Temp=30°C, pH=7.2
kcat is 3.56 min(-1).

source_databases_merged: brenda skid uniprot

enzyme: tryptophan 5-halogenase


enzyme_display_name: camalexin synthase

organism: Arabidopsis thaliana

proof_lines: pH and temperature not specified in the publication

enzyme: camalexin synthase


proof_lines: kcat is 1.64 min(-1) for (R)-reticuline.


enzyme_display_name: (S)-cheilanthifoline synthase

organism: Argemone mexicana

substrate_name: (S)-scoulerine

enzyme: (S)-cheilanthifoline synthase

substrate: (S)-scoulerine


column_label: Abstract reports recombinant CYP719A21 displayed strict substrate specificity and high affinity (Km=4.63+/-0.71 microM) for (S)-tetrahydrocolumbamine.

raw_value_unit_evidence: Km raw_value=4.63+/-0.71 microM raw_unit=microM

row_label: recombinant CYP719A21 / (S)-tetrahydrocolumbamine

table_label: PubMed XML abstract PMID 24316226


enzyme_display_name: Pluviatolide synthase

organism: Podophyllum peltatum

substrate_name: (-)-matairesinol

proof_lines: kcat is 7.8 min(-1) with (-)-matairesinol as substrate.

enzyme: Pluviatolide synthase

substrate: (-)-matairesinol


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Streptomyces clavuligerus

substrate_name: O2; Penicillin N; 2-Oxoglutarate

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

enzyme: deacetoxycephalosporin-C synthase

substrate: O2; Penicillin N; 2-Oxoglutarate


assay_conditions_summary: pH 6


enzyme_display_name: Trifunctional (S)-stylopine synthase/(S)-nandinine synthase/(S)-canadine synthase

substrate_name: Unknown

proof_lines: kcat is 13.8 min(-1) for (S)-cheilanthifoline.

substrate: Unknown


enzyme_display_name: (S)-canadine synthase CYP719A21

enzyme: (S)-canadine synthase CYP719A21


organism: Cephalosporium acremonium

substrate_name: O2; 2-Oxoglutarate; Penicillin G

substrate: O2; 2-Oxoglutarate; Penicillin G


assay_conditions_summary: pH 7.2; 303.15 K; buffer potassium phosphate

proof_lines: wild type enzyme, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y454F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y454F, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E46Q with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E46Q, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F49A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F49A, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C


enzyme_display_name: (S)-stylopine synthase

substrate_name: (S)-cheilanthifoline

enzyme: (S)-stylopine synthase

substrate: (S)-cheilanthifoline


enzyme_display_name: Cheilanthifoline synthase

enzyme: Cheilanthifoline synthase


organism: Sinopodophyllum hexandrum

proof_lines: kcat is 14.9 min(-1) with (-)-matairesinol as substrate.


enzyme_display_name: noroxomaritidine synthase

column_label: Table 5; row 4′ -O-Methyl-N-methylnorbelladine; column Km (uM) cell 3.28 +/- 2.27; column kcat (1/min) cell 2.44 +/- 0.54; column kcat/Km (1/uM*min) cell 0.742; column Modifications monitored cell C-C phenol coupling.

raw_value_unit_evidence: Table 5 row 4′ -O-Methyl-N-methylnorbelladine: Km (µM) 3.28 +/- 2.27; kcat (1/min) 2.44 +/- 0.54; kcat/Km (1/µM*min) 0.742; Modifications monitored C-C phenol coupling.

row_label: 4′ -O-Methyl-N-methylnorbelladine

table_label: Table 5 | Substrate specificity tests for CYP96T1.

enzyme: noroxomaritidine synthase


column_label: Table 5; row 4′ -O-Methylnorbelladine; column Km (uM) cell 1.13 +/- 0.54; column kcat (1/min) cell 15.0 +/- 2.03; column kcat/Km (1/uM*min) cell 13; column Modifications monitored cell C-C phenol coupling.

normalized_value_unit_evidence: Km 1.13 uM = 1.13/1000 = 0.00113 mM. kcat 15.0 1/min = 15.0/60 = 0.25 s^-1. kcat/Km recorded here is this same Table 5 row's kcat divided by its Km, 0.25 / 0.00113 = 221.23893805309734 s^-1*mM^-1; the table's own efficiency column prints 13 1/uM*min, which equals 216.66666666666666 s^-1*mM^-1 at the rounded precision the table prints.

raw_value_unit_evidence: Table 5 row 4′ -O-Methylnorbelladine: Km (µM) 1.13 +/- 0.54; kcat (1/min) 15.0 +/- 2.03; kcat/Km (1/µM*min) 13; Modifications monitored C-C phenol coupling.

row_label: 4′ -O-Methylnorbelladine


substrate_name: (R)-coclaurine

column_label: Table 5; row (R)-Coclaurine; column Km (uM) cell 659 +/- 104; column kcat (1/min) cell 2.07 +/- 0.14; column kcat/Km (1/uM*min) cell 3.15 × 10−3; column Modifications monitored cell Intramolecular phenol coupling and Intermolecular coupling.

normalized_value_unit_evidence: Km 659 uM = 659/1000 = 0.659 mM. kcat 2.07 1/min = 2.07/60 = 0.0345 s^-1. kcat/Km recorded here is this same Table 5 row's kcat divided by its Km, 0.0345 / 0.659 = 0.05235204855842185 s^-1*mM^-1; the table's own efficiency column prints 3.15 × 10−3 1/uM*min, which equals 0.0525 s^-1*mM^-1 at the rounded precision the table prints.

raw_value_unit_evidence: Table 5 row (R)-Coclaurine: Km (µM) 659 +/- 104; kcat (1/min) 2.07 +/- 0.14; kcat/Km (1/µM*min) 3.15 × 10−3; Modifications monitored Intramolecular phenol coupling and Intermolecular coupling.

row_label: (R)-Coclaurine

substrate: (R)-coclaurine


substrate_name: (S)-Coclaurine

column_label: Table 5; row (S)-Coclaurine; column Km (uM) cell 637 +/- 156; column kcat (1/min) cell 1.34 +/- 0.15; column kcat/Km (1/uM*min) cell 2.11 × 10−3; column Modifications monitored cell Intramolecular phenol coupling and Intermolecular coupling.

raw_value_unit_evidence: Table 5 row (S)-Coclaurine: Km (µM) 637 +/- 156; kcat (1/min) 1.34 +/- 0.15; kcat/Km (1/µM*min) 2.11 × 10−3; Modifications monitored Intramolecular phenol coupling and Intermolecular coupling.

substrate: (S)-Coclaurine


substrate_name: Ampicillin

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258A to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258A mutant

substrate: Ampicillin


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258F to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258F mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258H to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258H mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258K to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258K mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258L to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258L mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R258Q to reconstruct the assayed variant sequence.

proof_lines:
deacetoxycephalosporin C synthase
2-oxoacid cosubstrate selectivity
R258Q mutant


substrate_name: Penicillin G

substrate: Penicillin G


proof_lines:
deacetoxycephalosporin-C synthase
R258 mutants
2-oxoacid cosubstrate selectivity


assay_conditions_summary: pH 7; 295.15 K; cofactor NADH


organism: Pseudomonas syringae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H116Q to reconstruct the assayed variant sequence.

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H168Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H169Q with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H268Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H284Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H305Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H309Q with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H335Q to reconstruct the assayed variant sequence.


organism: Pseudomonas savastanoi pv. phaseolicola

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


substrate_name: L-arginine

substrate: L-arginine


substrate_name: 2-Hydroxymyristate; O2

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

substrate: 2-Hydroxymyristate; O2


organism: Oryctolagus cuniculus

substrate_name: O2; H+; 7alpha-Hydroxycholest-4-en-3-one; NADPH


enzyme_display_name: methylsterol monooxygenase

organism: Rattus norvegicus

substrate_name: H+; NADH; O2; 5alpha-Cholest-7-ene-3-one-4alpha-carbaldehyde

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

enzyme: methylsterol monooxygenase


enzyme_display_name: all-trans-retinol 3,4-desaturase

organism: Homo sapiens

substrate_name: all-trans-retinoic acid from cellular retinoic acid-binding protein-2

enzyme: all-trans-retinol 3,4-desaturase


substrate_name: all-trans-retinaldehyde from cellular retinol-binding protein-1


enzyme_display_name: salutaridine synthase

substrate_name: [reduced NADPH-hemoprotein reductase]

enzyme: salutaridine synthase

substrate: [reduced NADPH-hemoprotein reductase]


enzyme_display_name: (S)-canadine synthase

organism: Coptis japonica

enzyme: (S)-canadine synthase


enzyme_display_name: Methylsterol monooxygenase 1

enzyme: Methylsterol monooxygenase 1


enzyme_display_name: Cytochrome P450 710A1

substrate_name: beta-sisterol

enzyme: Cytochrome P450 710A1

substrate: beta-sisterol


enzyme_display_name: sterol 22-desaturase

organism: Saccharomyces cerevisiae

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

enzyme: sterol 22-desaturase


enzyme_display_name: Cytochrome P450 710A11

organism: Solanum lycopersicum

enzyme: Cytochrome P450 710A11


enzyme_display_name: Noroxomaritidine synthase

organism: Narcissus aff. pseudonarcissus MK-2014

proof_lines: kcat is 15.0 min(-1) with 4'-O-methylnorbelladine as substrate. kcat is 2.44 min(-1) with 4'-O-methyl-N-methylnorbelladine as substrate. kcat is 1.34 min(-1) with (S)-coclaurine as substrate. kcat is 2.07 min(-1) with (R)-coclaurine as subs

enzyme: Noroxomaritidine synthase


enzyme_display_name: tryptophan 5-halogenase

substrate_name: L-tryptophan

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E46D with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E46D, in potassium phosphate buffer (10 mM, pH 7.2), at 30°C

enzyme: tryptophan 5-halogenase

substrate: L-tryptophan


organism: Hapsidospora chrysogena


substrate_name: Penicillin N

substrate: Penicillin N


enzyme_display_name: 2-hydroxy-palmitic acid dioxygenase MPO1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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


enzyme_display_name: UniProt P05979

organism: Ovis aries

smiles: O=O

enzyme: UniProt P05979


enzyme_display_name: UniProt P23219

smiles: CCC=CCC=CCC=CCC=CCC=CCC=CCCC(=O)O

enzyme: UniProt P23219


substrate_name: cis-5,8,11,14,17-eicosapentaenoic acid

substrate: cis-5,8,11,14,17-eicosapentaenoic acid


substrate_name: alpha-linolenic acid

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

substrate: alpha-linolenic acid


substrate_name: cis-5,8,11,14-eicosatetraenoic acid

substrate: cis-5,8,11,14-eicosatetraenoic acid


substrate_name: linoleic acid

substrate: linoleic acid


substrate_name: cis-11,14-eicosadienoic acid

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

substrate: cis-11,14-eicosadienoic acid


substrate_name: cis-7,10,13,16-docosatetraenoic acid

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

substrate: cis-7,10,13,16-docosatetraenoic acid


substrate_name: gamma-linolenic acid

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

substrate: gamma-linolenic acid


enzyme_display_name: UniProt P35354

enzyme: UniProt P35354


substrate_name: cis-8,11,14-eicosatrienoic acid

substrate: cis-8,11,14-eicosatrienoic acid


enzyme_display_name: UniProt Q05769

organism: Mus musculus

substrate_name: arachidonate

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

enzyme: UniProt Q05769

substrate: arachidonate


column_label: PubMed abstract metric sentence gives Km for CYP61 sterol delta22-desaturation as 20.4 microM, normalized to 0.0204 mM

normalized_value_unit_evidence: PubMed abstract Km normalized_value=0.0204 normalized_unit=mM

raw_value_unit_evidence: PubMed abstract: The enzyme kinetics associated with its endogenous role in sterol Delta22-desaturation revealed a Km of 20.4 microM and a Vmax of 2.9nmol/min/nmol CYP61

row_label: CYP61 sterol delta22-desaturation Km sentence

table_label: PubMed abstract


enzyme_display_name: Trifunctional (S)-stylopine synthase 2/(S)-nandinine synthase/(S)-canadine synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

column_label: PMID 17250743 substrate-affinity section, CYP719A3 / (S)-scoulerine row/segment, Km = 0.54 +/- 0.03 uM.

raw_value_unit_evidence: CYP719A3 Km for (S)-scoulerine was 0.54 +/- 0.03 uM.

row_label: CYP719A3 / (S)-scoulerine

table_label: Substrate-affinity section for CYP719A3 toward (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: (S)-stylopine synthase 1

substrate_name: (R,S)-scoulerine

enzyme: (S)-stylopine synthase 1

substrate: (R,S)-scoulerine


organism: Arthrobacter sp.


substrate_name: beta-sitosterol

substrate: beta-sitosterol


enzyme_display_name: deacetoxycephalosporin-C synthase

organism: Amycolatopsis lactamdurans

substrate_name: oxoglutarate

assay_conditions_summary: pH 7

column_label: Captured primary-paper prose: The apparent Km for 2-oxoglutarate was 3 uM.

raw_value_unit_evidence: Km raw_value=3 raw_unit=uM for 2-oxoglutarate.

row_label: 2-oxoglutarate varied from 1 to 50 uM

table_label: Primary-paper Results prose: Kinetics of the DAOC synthase, journal pages 3169-3171

enzyme: deacetoxycephalosporin-C synthase

substrate: oxoglutarate


column_label: Captured primary-paper prose: For penicillin N, the apparent Km was 52 uM.

raw_value_unit_evidence: Km raw_value=52 raw_unit=uM for penicillin N.

row_label: Penicillin N varied from 0.01 to 0.15 mM


enzyme_display_name: sn-1 linoleoyl-lipid 6-desaturase

organism: Limnospira platensis

substrate_name: linoleate

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

enzyme: sn-1 linoleoyl-lipid 6-desaturase

substrate: linoleate


enzyme_display_name: beta-carotene 15,15'-monooxygenase

substrate_name: beta-carotene

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

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

enzyme: beta-carotene 15,15'-monooxygenase

substrate: beta-carotene


enzyme_display_name: UniProt G2LET6

organism: Chloracidobacterium thermophilum

substrate_name: hercynine

enzyme: UniProt G2LET6

substrate: hercynine


substrate_name: gamma-L-glutamyl-L-cysteine

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

substrate: gamma-L-glutamyl-L-cysteine


enzyme_display_name: kynurenine 7,8-hydroxylase

organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

enzyme: kynurenine 7,8-hydroxylase

substrate: Unknown

source: unknown


assay_conditions_summary: cofactor NADH


enzyme_display_name: all-trans-retinol 3,4-desaturase

substrate_name: all-trans-retinol

enzyme: all-trans-retinol 3,4-desaturase

substrate: all-trans-retinol


enzyme_display_name: Corytuberine synthase

substrate_name: (R,S)-reticuline

enzyme: Corytuberine synthase

substrate: (R,S)-reticuline


enzyme_display_name: gamma-glutamyl hercynylcysteine S-oxide synthase

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

proof_lines: mutant D52L, pH not specified in the publication, temperature not specified in the publication


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

enzyme: gamma-glutamyl hercynylcysteine S-oxide synthase


proof_lines: mutant A420Y, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant D52L/A420Y, pH not specified in the publication, temperature not specified in the publication


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


organism: Erwinia tasmaniensis

substrate_name: histamine

substrate: histamine


substrate_name: L-histidinamide

substrate: L-histidinamide


substrate_name: D-histidine

substrate: D-histidine


substrate_name: L-cysteine

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

substrate: L-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K108F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K108L to reconstruct the assayed variant sequence.


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


enzyme_display_name: Bifunctional protein STORR

organism: Papaver somniferum

enzyme: Bifunctional protein STORR


enzyme_display_name: lytic cellulose monooxygenase (C1-hydroxylating)

organism: Thermothelomyces thermophilus

substrate_name: cellulose

substrate: cellulose


organism: Talaromyces amestolkiae

smiles: OO

enzyme: lytic cellulose monooxygenase (C1-hydroxylating)


proof_lines: variant lacking the C-terminal linker-like region, pH 6, 23°C

proof_lines: variant with an additional C-terminal carbohydrate binding domain, pH 6, 23°C


enzyme_display_name: Hercynine oxygenase

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

enzyme: Hercynine oxygenase


enzyme_display_name: UniProt G7CFI3

organism: Mycolicibacterium thermoresistibile

proof_lines: kcat is 0.87 sec(-1) for the oxidative sulfurization of hercynine with gamma-L-glutamyl-L-cysteine as sulfur donor. kcat is 0.25 sec(-1) for the oxidative sulfurization of hercynine with N-glutaryl-cysteine as sulfur donor.

enzyme: UniProt G7CFI3


enzyme_display_name: UniProt Q9UBK8

organism: Homo sapiens

substrate_name: 3-acetylpyridine adenine dinucleotide phosphate

enzyme: UniProt Q9UBK8


substrate_name: menadione

substrate: menadione


substrate_name: doxorubicin

substrate: doxorubicin


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 8

proof_lines: pH 8.0, 26°C, recombinant enzyme mutant Y377F

proof_lines: pH 6.0, 26°C, recombinant enzyme mutant Y377F


organism: Trichoderma reesei


organism: Thermothielavioides terrestris


substrate_name: gamma-L-glutamyl-cysteine

substrate: gamma-L-glutamyl-cysteine


organism: Mycolicibacterium thermoresistibile (strain ATCC 19527 / DSM 44167 / CIP 105390 / JCM 6362 / NCTC 10409 / 316)


enzyme_display_name: hercynylcysteine S-oxide synthase

organism: Neurospora crassa

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

enzyme: hercynylcysteine S-oxide synthase


column_label: Table 1 row D-Histidine (9) reports kcat = 7.8 x 10^-1 s^-1 and KM = 6.7 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: kcat normalized_value=0.78 normalized_unit=s^-1; Km normalized_value=0.67 normalized_unit=mM; kcat_over_km normalized_value=1.164179104477612 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=7.8 x 10^-1 raw_unit=s^-1; Km raw_value=6.7 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.67 mM

row_label: Sulphur acceptor / D-Histidine (9)

table_label: Table 1. Michaelis-Menten parameters of OvoA catalyzed sulphurization of imidazole derivatives


column_label: Table 1 row Histamine (7) reports kcat = 3.6 x 10^-1 s^-1 and KM = 2.3 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: kcat normalized_value=0.36 normalized_unit=s^-1; Km normalized_value=0.23 normalized_unit=mM; kcat_over_km normalized_value=1.5652173913043477 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=3.6 x 10^-1 raw_unit=s^-1; Km raw_value=2.3 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.23 mM

row_label: Sulphur acceptor / Histamine (7)


column_label: Table 1 row L-Histidinamide (6) reports kcat = 5.7 x 10^-1 s^-1 and KM = 3.1 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: kcat normalized_value=0.57 normalized_unit=s^-1; Km normalized_value=0.31 normalized_unit=mM; kcat_over_km normalized_value=1.8387096774193548 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: kcat raw_value=5.7 x 10^-1 raw_unit=s^-1; Km raw_value=3.1 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.31 mM

row_label: Sulphur acceptor / L-Histidinamide (6)


substrate_name: L-histidine

column_label: Table 1 row L-Histidine (5) reports KM = 3.4 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: Km normalized_value=0.34 normalized_unit=mM; kcat_over_km normalized_value=9.999999999999998 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=3.4 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.34 mM

row_label: Sulphur acceptor / L-Histidine (5)

substrate: L-histidine


substrate_name: L-Cysteine

column_label: Table 1 row L-Cysteine reports KM = 3.5 x 10^-4 M.; same Table 1 row kcat and KM columns support the kcat/KM quotient after KM unit conversion

normalized_value_unit_evidence: Km normalized_value=0.35 normalized_unit=mM; kcat_over_km normalized_value=9.428571428571429 normalized_unit=s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=3.5 x 10^-4 raw_unit=M; kcat/KM same-row quotient from kcat=-1 s^-1 and KM=0.35 mM

row_label: Sulphur donor / L-Cysteine

substrate: L-Cysteine


enzyme_display_name: tryptophan 5-halogenase

organism: Streptomyces rugosporus

substrate_name: L-tryptophan

enzyme: tryptophan 5-halogenase

substrate: L-tryptophan


enzyme_display_name: superoxide dismutase

organism: Psidium guajava

substrate_name: riboflavin

enzyme: superoxide dismutase

substrate: riboflavin


substrate_name: Nitro blue tetrazolium

substrate: Nitro blue tetrazolium


enzyme_display_name: Transferred entry: 1.21.3.10

enzyme: Transferred entry: 1.21.3.10


enzyme_display_name: tryptophan 6-halogenase

organism: Streptomyces toxytricini

enzyme: tryptophan 6-halogenase


enzyme_display_name: mercury(II) reductase

organism: Azotobacter chroococcum

substrate_name: Hg

smiles: [Hg]

enzyme: mercury(II) reductase

substrate: Hg


enzyme_display_name: diferric-transferrin reductase

organism: Mycobacterium avium subsp. paratuberculosis

substrate_name: ferric ammonium citrate

enzyme: diferric-transferrin reductase

substrate: ferric ammonium citrate


organism: Yersinia enterolytica


substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus

substrate_name: NADH

substrate: NADH


organism: Penicillium sp.


enzyme_display_name: Mercuric reductase

organism: Lysinibacillus sphaericus

enzyme: Mercuric reductase


enzyme_display_name: Mycocyclosin synthase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: cYY (at pH7.2 and 30 degrees Celsius)

enzyme: Mycocyclosin synthase

substrate: cYY (at pH7.2 and 30 degrees Celsius)


enzyme_display_name: Trifunctional (S)-stylopine synthase 2/(S)-nandinine synthase/(S)-canadine synthase

organism: Eschscholzia californica

substrate_name: (S)-scoulerine

substrate: (S)-scoulerine


enzyme_display_name: Sarpagan bridge enzyme 1

organism: Rauvolfia serpentina

substrate_name: geissoschizine

column_label: Article results prose states Rs_12057 and Gs_207-0.13 exhibited Michaelis-Menten kinetics with apparent KM values of 22.5 uM and 35.3 uM, respectively, for geissoschizine.

raw_value_unit_evidence: apparent KM value of 22.5 uM for Rs_12057 with geissoschizine

row_label: Rs_12057 / RsSBE with geissoschizine

table_label: Results prose, Supplementary Figure 8

enzyme: Sarpagan bridge enzyme 1

substrate: geissoschizine


organism: Benthodytes marianensis

substrate_name: superoxide

substrate: superoxide


enzyme_display_name: Superoxide dismutase [Mn/Fe]

organism: Propionibacterium freudenreichii subsp. shermanii

substrate_name: superoxide (at pH 9.5, with the Fe-SOD form)

column_label: Abstract states the Michaelis constant for the Fe-superoxide dismutase was Km = 0.54 mmol/l at pH 9.5.

raw_value_unit_evidence: Km raw_value=0.54 raw_unit=mmol/l

row_label: Propionibacterium shermanii Fe-superoxide dismutase with superoxide

table_label: PubMed/PMC abstract PMID 7575431

enzyme: Superoxide dismutase [Mn/Fe]


organism: Metallosphaera sedula

assay_conditions_summary: pH 6.7; 310.15 K; cofactor NADPH

column_label: PMC Results prose states Hg2+ Km values of 400 and 150 uM at 37 and 70 C, respectively; Table 1 M. sedula row lists Hg Km 400a/150b and specific activity 1.9a/3.1b.

raw_value_unit_evidence: Km raw_value=150 uM raw_unit=uM for Hg2+ at 70 C; table also lists 400 uM at 37 C.

row_label: M. sedula MerA / Hg2+ / 70 C

table_label: PMC Table 1 MerA comparison and Results prose


enzyme_display_name: Sarpagan bridge enzyme

organism: Gelsemium sempervirens

raw_value_unit_evidence: apparent KM value of 35.3 uM for Gs_207-0.13 with geissoschizine

row_label: Gs_207-0.13 / GsSBE with geissoschizine

enzyme: Sarpagan bridge enzyme


enzyme_display_name: gamma-glutamyl hercynylcysteine S-oxide synthase

organism: Mycolicibacterium thermoresistibile

substrate_name: hercynine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y377F with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

substrate: hercynine


enzyme: gamma-glutamyl hercynylcysteine S-oxide synthase


enzyme_display_name: ferroxidase

organism: Caretta caretta

substrate_name: p-phenylenediamine

enzyme: ferroxidase

substrate: p-phenylenediamine


enzyme_display_name: iron-cytochrome-c reductase

organism: Acidithiobacillus ferrooxidans

substrate_name: ferrocytochrome c

enzyme: iron-cytochrome-c reductase

substrate: ferrocytochrome c


organism: Acidomyces acidophilus

substrate_name: Fe(II)

proof_lines: recombinant wild-type enzyme, pH 5.0, 25°C

substrate: Fe(II)


enzyme_display_name: manganese oxidase

organism: Bacillus sp. PL-12

proof_lines: at pH 7.8, temperature not specified in the publication

enzyme: manganese oxidase


organism: Shewanella oneidensis

proof_lines:
isozyme MtrC, at pH 8.0 and 30°C
isozyme OmcA, at pH 8.0 and 30°C


organism: Desulfovibrio sp. A2


organism: Bacillus sp.


enzyme_display_name: Ceruloplasmin

organism: Homo sapiens

substrate_name: glutathione

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

proof_lines: kcat is 22.5 min(-1) and 30.3 min(-1) with Cu(+) and Fe(2+) as substrates, respectively.

enzyme: Ceruloplasmin

substrate: glutathione


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide