organism: Vigna radiata

substrate_name: Prephenate; NADP+

assay_conditions_summary: cofactor NADP+

substrate: Prephenate; NADP+


enzyme_display_name: prephenate dehydrogenase (NADP+)

substrate_name: NADP+

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

proof_lines:
pretyrosine as substrate
prephenate as substrate

enzyme: prephenate dehydrogenase (NADP+)

substrate: NADP+

status: unverified

source: brenda


substrate_name: prephenate

substrate: prephenate


organism: Nanoarchaeum equitans

assay_conditions_summary: pH 8; 353.15 K; cofactor NADP+


proof_lines: with NAD+ as cosubstrate, at pH 8.0 and 80°C

proof_lines: with NADP+ as cosubstrate, at pH 8.0 and 80°C


substrate_name: NAD+

assay_conditions_summary: pH 8; 353.15 K; cofactor NAD+

substrate: NAD+


organism: Acinetobacter calcoaceticus


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: competitive inhibition with respect to substrate and noncompetitively with respect to cofactor

substrate: Unknown


enzyme_display_name: dihydroorotate dehydrogenase (NADP+)

organism: Bacteria

substrate_name: Orotate

assay_conditions_summary: cofactor NADPH

enzyme: dihydroorotate dehydrogenase (NADP+)

substrate: Orotate


substrate_name: NADPH

substrate: NADPH


organism: Persea americana

substrate_name: crotonyl-[acyl-carrier protein]

substrate: crotonyl-[acyl-carrier protein]


substrate_name: Crotonyl-N-acetyl-cysteamine

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

substrate: Crotonyl-N-acetyl-cysteamine


enzyme_display_name: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)

organism: Porphyromonas gingivalis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


enzyme: enoyl-[acyl-carrier-protein] reductase (NADPH, Si-specific)


enzyme_display_name: prephenate dehydrogenase

organism: Azomonas insignis

enzyme: prephenate dehydrogenase


assay_conditions_summary: cofactor NAD+


organism: Ignicoccus hospitalis


organism: Phaseolus vulgaris


organism: Staphylococcus aureus


enzyme_display_name: beta-nitroacrylate reductase

organism: Penicillium atrovenetum

enzyme: beta-nitroacrylate reductase


enzyme_display_name: 2-coumarate reductase

organism: Arthrobacter sp.

substrate_name: o-coumarate

enzyme: 2-coumarate reductase

substrate: o-coumarate


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 7.6; 310.15 K; cofactor NAD+

proof_lines: with NAD+ as cosubstrate, pH 7.6 and 37°C

proof_lines: with NAD+ as cosubstrate, at pH 7.6 and 37°C


organism: Plasmodium falciparum

substrate_name: Crotonoyl-CoA; H+; NADH

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

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

assay_conditions_summary: cofactor NADH

substrate: Crotonoyl-CoA; H+; NADH


substrate_name: Butanoyl-CoA; NAD+

substrate: Butanoyl-CoA; NAD+


enzyme_display_name: UniProt A0A1C9HA64

organism: uncultured bacterium

substrate_name: NADH

source_db: skid

protein_accession_database: UniProt

source_license: CC BY-NC-ND 4.0

assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADH

enzyme: UniProt A0A1C9HA64

substrate: NADH

source: skid


substrate_name: crotonoyl-CoA

assay_conditions_summary: pH 5.5; 303.15 K; cofactor CoA

substrate: crotonoyl-CoA


enzyme_display_name: dihydroorotate dehydrogenase (NAD+)

organism: Lactococcus lactis subsp. lactis

substrate_name: L-Dihydroorotate; NAD+

enzyme: dihydroorotate dehydrogenase (NAD+)

substrate: L-Dihydroorotate; NAD+


substrate_name: NAD+; L-Dihydroorotate

substrate: NAD+; L-Dihydroorotate


organism: Enterococcus faecalis


organism: Bacillus subtilis


enzyme_display_name: dihydroorotate dehydrogenase (NAD(+))

source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K48Q to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: dihydroorotate dehydrogenase (NAD(+))

source: oed


substrate_name: L-Dihydroorotate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K48A to reconstruct the assayed variant sequence.

substrate: L-Dihydroorotate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K48E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K48R to reconstruct the assayed variant sequence.


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


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Corynebacterium glutamicum


organism: Bacillus cereus


organism: Clostridium oroticum


organism: Streptomyces collinus

assay_conditions_summary: cofactor CoA

proof_lines:
vmax 0.0075 mmol/mg/min
vmax 0.0053 mmol/mg/min


organism: Pleurotus ostreatus


organism: Homo sapiens

substrate_name: (9E)-9-nitrooctadec-9-enoic acid

smiles: CCCCCCCCC=C(CCCCCCCC(=O)O)[N+](=O)[O-]

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication

substrate: (9E)-9-nitrooctadec-9-enoic acid


organism: Ignicoccus hospitalis


organism: Aquifex aeolicus

verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O67636 and applied mutation signature H217N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 328.15 K; cofactor NAD+

column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'H217N', variable-substrate block 'NAD+'; column 'Km (uM)' = 12 +/- 0.2; column 'kcat (s^-1)' = 0.3 +/- 0.01; column 'kcat/Km (M^-1 s^-1)' = 2.5 x 10^4.

normalized_value_unit_evidence: Km: printed Table 4 cell 12 uM; 12 / 1000 = 0.012 mM; the exported value is 0.012 mM. kcat: printed Table 4 cell 0.3 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 0.3 s^(-1). kcat/Km: printed Table 4 cell 2.5 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 x 10^4 / 1000 = 25.0 s^-1 mM^-1. The quotient of the same measurement's two printed component cells is 0.3 / 0.012 = 25.0 s^-1 mM^-1, which is the exported catalytic efficiency.

raw_value_unit_evidence: Table 4, protein row 'H217N', variable substrate NAD+: Km = 12 +/- 0.2 uM; kcat = 0.3 +/- 0.01 s^-1; printed kcat/Km = 2.5 x 10^4 M^-1 s^-1.

row_label: Table 4 row H217N, variable substrate NAD+

table_label: Table 4: Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases at pH 7.4 and 55 C (J. Biol. Chem. 2009, 284(19):13223-13232)

status: verified


verification_status: corrected

assay_conditions_summary: pH 7.5; 328.15 K; cofactor NADH

column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'H217N', variable-substrate block 'prephenate'; column 'Km (uM)' = 3213 +/- 445; column 'kcat (s^-1)' = 0.5 +/- 0.02; column 'kcat/Km (M^-1 s^-1)' = 1.5 x 10^2.

normalized_value_unit_evidence: Km: printed Table 4 cell 3213 uM; 3213 / 1000 = 3.213 mM. kcat: printed Table 4 cell 0.5 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed Table 4 cell 1.5 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.5 x 10^2 / 1000 = 0.15 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, protein row 'H217N', variable substrate prephenate: Km = 3213 +/- 445 uM; kcat = 0.5 +/- 0.02 s^-1; printed kcat/Km = 1.5 x 10^2 M^-1 s^-1.

row_label: Table 4 row H217N, variable substrate prephenate

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O67636 and applied mutation signature H217A to reconstruct the assayed variant sequence.

column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'H217A', variable-substrate block 'NAD+'; column 'Km (uM)' = 10 +/- 0.5; column 'kcat (s^-1)' = 0.6 +/- 0.004; column 'kcat/Km (M^-1 s^-1)' = 6.0 x 10^4.

normalized_value_unit_evidence: Km: printed Table 4 cell 10 uM; 10 / 1000 = 0.01 mM; the exported value is 0.01 mM. kcat: printed Table 4 cell 0.6 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 0.6 s^(-1). kcat/Km: printed Table 4 cell 6.0 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.0 x 10^4 / 1000 = 60.0 s^-1 mM^-1. The quotient of the same measurement's two printed component cells is 0.6 / 0.01 = 60.0 s^-1 mM^-1, which is the exported catalytic efficiency.

raw_value_unit_evidence: Table 4, protein row 'H217A', variable substrate NAD+: Km = 10 +/- 0.5 uM; kcat = 0.6 +/- 0.004 s^-1; printed kcat/Km = 6.0 x 10^4 M^-1 s^-1.

row_label: Table 4 row H217A, variable substrate NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O67636 and applied mutation signature S126A to reconstruct the assayed variant sequence.

column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'S126A', variable-substrate block 'prephenate'; column 'Km (uM)' = 1335 +/- 39; column 'kcat (s^-1)' = 0.8 +/- 0.01; column 'kcat/Km (M^-1 s^-1)' = 1.4 x 10^3.

normalized_value_unit_evidence: Km: printed Table 4 cell 1335 uM; 1335 / 1000 = 1.335 mM. kcat: printed Table 4 cell 0.8 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed Table 4 cell 1.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 x 10^3 / 1000 = 1.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, protein row 'S126A', variable substrate prephenate: Km = 1335 +/- 39 uM; kcat = 0.8 +/- 0.01 s^-1; printed kcat/Km = 1.4 x 10^3 M^-1 s^-1.

row_label: Table 4 row S126A, variable substrate prephenate


column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'H217A', variable-substrate block 'prephenate'; column 'Km (uM)' = 4132 +/- 277; column 'kcat (s^-1)' = 0.8 +/- 0.03; column 'kcat/Km (M^-1 s^-1)' = 1.9 x 10^2.

normalized_value_unit_evidence: Km: printed Table 4 cell 4132 uM; 4132 / 1000 = 4.132 mM; the exported value is 4.132 mM. kcat: printed Table 4 cell 0.8 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 0.8 s^(-1). kcat/Km: printed Table 4 cell 1.9 x 10^2 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^2 / 1000 = 0.19 s^-1 mM^-1. The quotient of the same measurement's two printed component cells is 0.8 / 4.132 = 0.19361084220716362 s^-1 mM^-1, which is the exported catalytic efficiency.

raw_value_unit_evidence: Table 4, protein row 'H217A', variable substrate prephenate: Km = 4132 +/- 277 uM; kcat = 0.8 +/- 0.03 s^-1; printed kcat/Km = 1.9 x 10^2 M^-1 s^-1.

row_label: Table 4 row H217A, variable substrate prephenate


column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'S126A', variable-substrate block 'NAD+'; column 'Km (uM)' = 99 +/- 6; column 'kcat (s^-1)' = 0.8 +/- 0.02; column 'kcat/Km (M^-1 s^-1)' = 8.0 x 10^3.

normalized_value_unit_evidence: Km: printed Table 4 cell 99 uM; 99 / 1000 = 0.099 mM. kcat: printed Table 4 cell 0.8 s^-1; the printed unit is already s^-1 and no unit conversion applies. kcat/Km: printed Table 4 cell 8.0 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.0 x 10^3 / 1000 = 8.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, protein row 'S126A', variable substrate NAD+: Km = 99 +/- 6 uM; kcat = 0.8 +/- 0.02 s^-1; printed kcat/Km = 8.0 x 10^3 M^-1 s^-1.

row_label: Table 4 row S126A, variable substrate NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O67636 and applied mutation signature R250Q to reconstruct the assayed variant sequence.

column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'R250Q', variable-substrate block 'prephenate'; column 'Km (uM)' = 1185 +/- 118; column 'kcat (s^-1)' = 9.9 +/- 0.42; column 'kcat/Km (M^-1 s^-1)' = 8.4 x 10^3.

normalized_value_unit_evidence: Km: printed Table 4 cell 1185 uM; 1185 / 1000 = 1.185 mM; the exported value is 1.185 mM. kcat: printed Table 4 cell 9.9 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 9.9 s^(-1). kcat/Km: printed Table 4 cell 8.4 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.4 x 10^3 / 1000 = 8.4 s^-1 mM^-1. The quotient of the same measurement's two printed component cells is 9.9 / 1.185 = 8.354430379746836 s^-1 mM^-1, which is the exported catalytic efficiency.

raw_value_unit_evidence: Table 4, protein row 'R250Q', variable substrate prephenate: Km = 1185 +/- 118 uM; kcat = 9.9 +/- 0.42 s^-1; printed kcat/Km = 8.4 x 10^3 M^-1 s^-1.

row_label: Table 4 row R250Q, variable substrate prephenate


column_label: Table 4 (Summary of kinetics parameters for wild-type delta-19PD and variant dehydrogenases), protein row 'R250Q', variable-substrate block 'NAD+'; column 'Km (uM)' = 89 +/- 12; column 'kcat (s^-1)' = 11.6 +/- 0.6; column 'kcat/Km (M^-1 s^-1)' = 1.3 x 10^5.

normalized_value_unit_evidence: Km: printed Table 4 cell 89 uM; 89 / 1000 = 0.089 mM; the exported value is 0.089 mM. kcat: printed Table 4 cell 11.6 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 11.6 s^(-1). kcat/Km: printed Table 4 cell 1.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^5 / 1000 = 130.0 s^-1 mM^-1. The quotient of the same measurement's two printed component cells is 11.6 / 0.089 = 130.3370786516854 s^-1 mM^-1, which is the exported catalytic efficiency.

raw_value_unit_evidence: Table 4, protein row 'R250Q', variable substrate NAD+: Km = 89 +/- 12 uM; kcat = 11.6 +/- 0.6 s^-1; printed kcat/Km = 1.3 x 10^5 M^-1 s^-1.

row_label: Table 4 row R250Q, variable substrate NAD+


organism: Yersinia pestis

assay_conditions_summary: pH 8; cofactor CoA

column_label: Table 1; row trans-2-octenoyl-CoA; KM, kcat, and kcat/KM columns.

raw_value_unit_evidence: Table 1 row trans-2-octenoyl-CoA: KM 7 +/- 1 uM; kcat 16 +/- 1 min^-1; kcat/KM 2 +/- 0 uM^-1 min^-1.

table_label: Table 1. Kinetic parameters for the reduction of CoA and ACP-based substrates by ypFabV


assay_conditions_summary: pH 8; 303.15 K; cofactor NADH


enzyme_display_name: Cyclohexadienyl dehydrogenase

organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

substrate_name: L-arogenate (at pH 6.6 and 37 degrees Celsius)

source_db: uniprot

proof_lines: The KM value obtained for NAD(+) is the same regardless of whether the enzyme is assayed as arogenate dehydrogenase or as prephenate dehydrogenase. Has a greater Vmax with L-arogenate as substrate (about 3-fold higher than with prephenate).

enzyme: Cyclohexadienyl dehydrogenase

source: uniprot


substrate_name: prephenate (at pH 6.6 and 37 degrees Celsius)


substrate_name: NAD(+) (at pH 6.6 and 37 degrees Celsius)


organism: Glycine max

substrate_name: prephenate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T206S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q184A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T131S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T131A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S101A to reconstruct the assayed variant sequence.


organism: Mycolicibacterium smegmatis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature M161V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; cofactor CoA


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature A124V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; cofactor NADH


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: NADH (at pH 6.8 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: kcat is 320.4 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 7.5 and 25 degrees Celsius) (PubMed:21143326). kcat is 278 min(-1) for the reduction of 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius) (PubMed:10521269).

substrate: NADH (at pH 6.8 and 25 degrees Celsius)


substrate_name: 2-trans-dodecenoyl-CoA (at pH 6.8 and 25 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor CoA


enzyme_display_name: UniProt Q2P9J6

organism: Xanthomonas oryzae

substrate_name: crotonyl-CoA

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

sequence_source: multiple

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: kcat is 1335 sec(-1) for reductase activity.

source_databases_merged: skid uniprot

enzyme: UniProt Q2P9J6

substrate: crotonyl-CoA


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Burkholderia mallei (strain ATCC 23344)

substrate_name: DD-CoA (with His tag)

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

proof_lines: kcat is 1728 min(-1) for reductase activity with DD-CoA as substrate (without His tag). kcat is 1242 min(-1) for reductase activity with DD-CoA as substrate (with His tag).

substrate: DD-CoA (with His tag)


enzyme_display_name: Prephenate dehydrogenase

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

proof_lines: kcat is 170.36 sec(-1) toward prephenate, and 356.07 sec(-1) toward NAD(+) (at pH 7.9 and 37 degrees Celsius).

enzyme: Prephenate dehydrogenase


substrate_name: NAD(+) (at pH 7.9 and 37 degrees Celsius)

assay_conditions_summary: pH 7.9; cofactor NAD+


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R294Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: prephenate


substrate_name: NAD+

substrate: NAD+


organism: Spinacia oleracea

substrate_name: NADH

assay_conditions_summary: cofactor NADH


organism: Staphylococcus aureus

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A95V with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; buffer 100 mM Na2HPO4; cofactor NADPH

proof_lines: mutant enzyme A95V, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)

substrate: NADPH


organism: Bacillus subtilis

assay_conditions_summary: cofactor NADPH

proof_lines:
no cooperativity in binding NADPH
Raw SKiD Env: Temp=-----, pH=-----

source_databases_merged: brenda skid


organism: Methanohalophilus mahii

assay_conditions_summary: cofactor NADP+

proof_lines:
cofactor NADP+
cofactor NAD+


organism: Streptococcus pneumoniae

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

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

proof_lines: 30°C, pH 6.5, in the presence of 100 mM NH4+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K37Q/H197N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H197N/K37Q to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+


organism: Medicago truncatula

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

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


organism: Eimeria tenella

assay_conditions_summary: pH 7.5; buffer wording; cofactor CoA


assay_conditions_summary: pH 7.5; buffer 0.1 mM Tris-HCl; cofactor NADH

proof_lines: recombinant enzyme, in the absence of enoyl-CoA as scosubstrate, in 0.1 mM Tris-HCl buffer (pH 7.2)


organism: Plasmodium falciparum

substrate_name: crotonoyl-CoA

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N218D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row N218D; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row Wild-type; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.

raw_value_unit_evidence: Wild-type | kcat 1.62 (+/-0.06) s^-1 | Km Crotonoyl-CoA 160+/-5 uM | Km NADH 33+/-3 uM

row_label: Wild-type


substrate_name: Prephenate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H131A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 303.15 K; buffer a three-component

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H131A, dehydrogenase activity, prephenate column group; column KM (uM) = 56 ± 12; column kcat (s^-1) = 3.1 ± 0.2; column kcat/KM (M^-1 s^-1) = 0.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.1 s^-1; already in s^-1, no conversion; the exported value is 3.1 s^(-1). Km: printed Table 3 cell 56 uM; 56 / 1000 = 0.056 mM; the exported value is 0.056 mM. kcat/Km: printed Table 3 cell 0.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60000.0 / 1000 = 60.0 s^-1 mM^-1; the exported value is 55.357142857142854 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H131A, dehydrogenase activity, prephenate column group: KM = 56 ± 12 uM; kcat = 3.1 ± 0.2 s^-1; printed kcat/KM = 0.6 x 10^5 M^-1 s^-1.

table_label: Table 3: Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C (Biochemistry 1998, 37(45):15703-15712)

substrate: Prephenate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H153N to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H153N, dehydrogenase activity, prephenate column group; column KM (uM) = 46 ± 5; column kcat (s^-1) = 19 ± 1; column kcat/KM (M^-1 s^-1) = 4.2 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 19 s^-1; already in s^-1, no conversion; the exported value is 19.0 s^(-1). Km: printed Table 3 cell 46 uM; 46 / 1000 = 0.046 mM; the exported value is 0.046 mM. kcat/Km: printed Table 3 cell 4.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 420000.0 / 1000 = 420.0 s^-1 mM^-1; the exported value is 413.04347826086956 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H153N, dehydrogenase activity, prephenate column group: KM = 46 ± 5 uM; kcat = 19 ± 1 s^-1; printed kcat/KM = 4.2 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H239N with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H239N, dehydrogenase activity, prephenate column group; column KM (uM) = 34 ± 4; column kcat (s^-1) = 5.6 ± 0.4; column kcat/KM (M^-1 s^-1) = 1.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.6 s^-1; already in s^-1, no conversion; the exported value is 5.6 s^(-1). Km: printed Table 3 cell 34 uM; 34 / 1000 = 0.034 mM; the exported value is 0.034 mM. kcat/Km: printed Table 3 cell 1.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 160000.0 / 1000 = 160.0 s^-1 mM^-1; the exported value is 164.70588235294116 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H239N, dehydrogenase activity, prephenate column group: KM = 34 ± 4 uM; kcat = 5.6 ± 0.4 s^-1; printed kcat/KM = 1.6 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H245N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 303.15 K; cofactor NAD+

column_label: Table 3 row H245N, dehydrogenase activity substrate Prephenate; raw cells KM 100 uM, kcat 12 s^-1, kcat/KM 1.2 x 10^5 M^-1 s^-1; normalized cells KM 0.100 mM, kcat 12 s^-1, kcat/Km 120 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.100 normalized_unit=mM; kcat normalized_value=12 normalized_unit=s^-1; kcat/Km normalized_value=120 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=100 raw_unit=uM; kcat raw_value=12 raw_unit=s^-1; kcat/Km raw_value=1.2 x 10^5 raw_unit=M^-1*s^-1

row_label: H245N / dehydrogenase activity substrate Prephenate

table_label: Table 3. Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H257A to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H257A, dehydrogenase activity, prephenate column group; column KM (uM) = 99 ± 8; column kcat (s^-1) = 20 ± 0.7; column kcat/KM (M^-1 s^-1) = 2.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 20 s^-1; already in s^-1, no conversion; the exported value is 20.0 s^(-1). Km: printed Table 3 cell 99 uM; 99 / 1000 = 0.099 mM; the exported value is 0.099 mM. kcat/Km: printed Table 3 cell 2.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 200000.0 / 1000 = 200.0 s^-1 mM^-1; the exported value is 202.02020202020202 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H257A, dehydrogenase activity, prephenate column group: KM = 99 ± 8 uM; kcat = 20 ± 0.7 s^-1; printed kcat/KM = 2.0 x 10^5 M^-1 s^-1.


sequence_variant_note: Mutation signature H265A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H347N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
H347N
prephenate dehydrogenase
Escherichia coli


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature K37Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row K37Q, dehydrogenase activity, prephenate column group; column KM (uM) = 54 ± 9; column kcat (s^-1) = 23 ± 1; column kcat/KM (M^-1 s^-1) = 4.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 23 s^-1; already in s^-1, no conversion; the exported value is 23.0 s^(-1). Km: printed Table 3 cell 54 uM; 54 / 1000 = 0.054 mM; the exported value is 0.054 mM. kcat/Km: printed Table 3 cell 4.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 430000.0 / 1000 = 430.0 s^-1 mM^-1; the exported value is 425.9259259259259 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row K37Q, dehydrogenase activity, prephenate column group: KM = 54 ± 9 uM; kcat = 23 ± 1 s^-1; printed kcat/KM = 4.3 x 10^5 M^-1 s^-1.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row WT, dehydrogenase activity, prephenate column group; column KM (uM) = 44 ± 8; column kcat (s^-1) = 27 ± 1; column kcat/KM (M^-1 s^-1) = 6.2 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 27 s^-1; already in s^-1, no conversion; the exported value is 27.0 s^(-1). Km: printed Table 3 cell 44 uM; 44 / 1000 = 0.044 mM; the exported value is 0.044 mM. kcat/Km: printed Table 3 cell 6.2 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 620000.0 / 1000 = 620.0 s^-1 mM^-1; the exported value is 613.6363636363636 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row WT, dehydrogenase activity, prephenate column group: KM = 44 ± 8 uM; kcat = 27 ± 1 s^-1; printed kcat/KM = 6.2 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BH77 and applied mutation signature A217G with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row A217G; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BH77 and applied mutation signature A217V with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row A217V; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F368I to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row F368I; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M281T to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row M281T; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row N218D; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row Wild-type; substrate axis NADH; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row A217G; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row A217V; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row F368I; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.


column_label: Table 2. Kinetic constants for NADH and crotonoyl-CoA with respect to wild-type and mutant PfENR. row M281T; substrate axis crotonoyl-CoA; exact required metric cells preserved in paper_metric_evidence.


assay_conditions_summary: pH 7.2; 303.15 K; buffer a three-component; cofactor NAD+

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H131A, dehydrogenase activity, NAD+ column group; column KM (uM) = 280 ± 37; column kcat (s^-1) = 2.6 ± 0.1; column kcat/KM (M^-1 s^-1) = 9.3 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.6 s^-1; already in s^-1, no conversion; the exported value is 2.6 s^(-1). Km: printed Table 3 cell 280 uM; 280 / 1000 = 0.28 mM; the exported value is 0.28 mM. kcat/Km: printed Table 3 cell 9.3 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9300.0 / 1000 = 9.3 s^-1 mM^-1; the exported value is 9.285714285714285 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H131A, dehydrogenase activity, NAD+ column group: KM = 280 ± 37 uM; kcat = 2.6 ± 0.1 s^-1; printed kcat/KM = 9.3 x 10^3 M^-1 s^-1.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H153N, dehydrogenase activity, NAD+ column group; column KM (uM) = 171 ± 28; column kcat (s^-1) = 19 ± 1.0; column kcat/KM (M^-1 s^-1) = 1.1 x 10^5.

raw_value_unit_evidence: Table 3, protein row H153N, dehydrogenase activity, NAD+ column group: KM = 171 ± 28 uM; kcat = 19 ± 1.0 s^-1; printed kcat/KM = 1.1 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H197N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H239N, dehydrogenase activity, NAD+ column group; column KM (uM) = 186 ± 18; column kcat (s^-1) = 5.6 ± 0.4; column kcat/KM (M^-1 s^-1) = 0.3 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.6 s^-1; already in s^-1, no conversion; the exported value is 5.6 s^(-1). Km: printed Table 3 cell 186 uM; 186 / 1000 = 0.186 mM; the exported value is 0.186 mM. kcat/Km: printed Table 3 cell 0.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 30000.0 / 1000 = 30.0 s^-1 mM^-1; the exported value is 30.10752688172043 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H239N, dehydrogenase activity, NAD+ column group: KM = 186 ± 18 uM; kcat = 5.6 ± 0.4 s^-1; printed kcat/KM = 0.3 x 10^5 M^-1 s^-1.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H245N, dehydrogenase activity, NAD+ column group; column KM (uM) = 185 ± 22; column kcat (s^-1) = 15 ± 0.4; column kcat/KM (M^-1 s^-1) = 0.8 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 15 s^-1; already in s^-1, no conversion; the exported value is 15.0 s^(-1). Km: printed Table 3 cell 185 uM; 185 / 1000 = 0.185 mM; the exported value is 0.185 mM. kcat/Km: printed Table 3 cell 0.8 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 80000.0 / 1000 = 80.0 s^-1 mM^-1; the exported value is 81.08108108108108 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H245N, dehydrogenase activity, NAD+ column group: KM = 185 ± 22 uM; kcat = 15 ± 0.4 s^-1; printed kcat/KM = 0.8 x 10^5 M^-1 s^-1.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H257A, dehydrogenase activity, NAD+ column group; column KM (uM) = 142 ± 15; column kcat (s^-1) = 15 ± 0.5; column kcat/KM (M^-1 s^-1) = 1.0 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 15 s^-1; already in s^-1, no conversion; the exported value is 15.0 s^(-1). Km: printed Table 3 cell 142 uM; 142 / 1000 = 0.142 mM; the exported value is 0.142 mM. kcat/Km: printed Table 3 cell 1.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 100000.0 / 1000 = 100.0 s^-1 mM^-1; the exported value is 105.63380281690142 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H257A, dehydrogenase activity, NAD+ column group: KM = 142 ± 15 uM; kcat = 15 ± 0.5 s^-1; printed kcat/KM = 1.0 x 10^5 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P07023 and applied mutation signature H347N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row H347N, dehydrogenase activity, NAD+ column group; column KM (uM) = 73 ± 10; column kcat (s^-1) = 4.5 ± 0.2; column kcat/KM (M^-1 s^-1) = 0.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.5 s^-1; already in s^-1, no conversion; the exported value is 4.5 s^(-1). Km: printed Table 3 cell 73 uM; 73 / 1000 = 0.073 mM; the exported value is 0.073 mM. kcat/Km: printed Table 3 cell 0.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 60000.0 / 1000 = 60.0 s^-1 mM^-1; the exported value is 61.64383561643836 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row H347N, dehydrogenase activity, NAD+ column group: KM = 73 ± 10 uM; kcat = 4.5 ± 0.2 s^-1; printed kcat/KM = 0.6 x 10^5 M^-1 s^-1.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row K37Q, dehydrogenase activity, NAD+ column group; column KM (uM) = 141 ± 16; column kcat (s^-1) = 22 ± 0.7; column kcat/KM (M^-1 s^-1) = 1.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22 s^-1; already in s^-1, no conversion; the exported value is 22.0 s^(-1). Km: printed Table 3 cell 141 uM; 141 / 1000 = 0.141 mM; the exported value is 0.141 mM. kcat/Km: printed Table 3 cell 1.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 160000.0 / 1000 = 160.0 s^-1 mM^-1; the exported value is 156.02836879432627 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row K37Q, dehydrogenase activity, NAD+ column group: KM = 141 ± 16 uM; kcat = 22 ± 0.7 s^-1; printed kcat/KM = 1.6 x 10^5 M^-1 s^-1.


column_label: Table 3 (Summary of Kinetic Data for Wild-Type and Mutant Mutase-Dehydrogenase Measured at pH 7.2 and 30 C), protein row WT, dehydrogenase activity, NAD+ column group; column KM (uM) = 103 ± 11; column kcat (s^-1) = 27 ± 0.7; column kcat/KM (M^-1 s^-1) = 2.6 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 27 s^-1; already in s^-1, no conversion; the exported value is 27.0 s^(-1). Km: printed Table 3 cell 103 uM; 103 / 1000 = 0.103 mM; the exported value is 0.102 mM. kcat/Km: printed Table 3 cell 2.6 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 260000.0 / 1000 = 260.0 s^-1 mM^-1; the exported value is 264.7058823529412 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, protein row WT, dehydrogenase activity, NAD+ column group: KM = 103 ± 11 uM; kcat = 27 ± 0.7 s^-1; printed kcat/KM = 2.6 x 10^5 M^-1 s^-1.


organism: Burkholderia mallei

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K244A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K244R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K245M to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y235A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y235S with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


organism: Yersinia pestis

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

column_label: Table 1; row trans-2-decenoyl-CoA; KM, kcat, and kcat/KM columns.

raw_value_unit_evidence: Table 1 row trans-2-decenoyl-CoA: KM 23 +/- 3 uM; kcat 332 +/- 20 min^-1; kcat/KM 14 +/- 2 uM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T267A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T267G with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T267S with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T267V with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T267W with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T267Y with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


column_label: Table 1 row trans-2-dodecenoyl-CoA and Table 2 row Wt ypFabV; KM, kcat, and kcat/KM columns.

raw_value_unit_evidence: Table 1 and Table 2 WT ddCoA rows: KM 14 +/- 1 uM; kcat 5468 +/- 426 min^-1; kcat/KM 390 +/- 41 uM^-1 min^-1.

row_label: trans-2-dodecenoyl-CoA / Wt ypFabV

table_label: Table 1/Table 2 kinetic parameters for ypFabV


column_label: Table 1; row trans-2-octenoyl-CoA; KM, kcat, and kcat/KM columns.

raw_value_unit_evidence: Table 1 row trans-2-octenoyl-CoA: KM 7 +/- 1 uM; kcat 16 +/- 1 min^-1; kcat/KM 2 +/- 0 uM^-1 min^-1.


organism: Homo sapiens

substrate_name: Dodecenoyl-CoA

assay_conditions_summary: pH 7; 298.15 K; cofactor CoA

column_label: T4 TABLE FOUR. Kinetic parameters for the enoyl reductase activity of wild-type HFAS as a function of chain length; row label Dodecenoyl-CoA (C12); column label kcat, K_ACYL, and kcat/K_ACYL columns; raw cells 13 ± 5 min^-1, K_ACYL 7 ± 1 µM, kcat/K_ACYL 2 ± 1 µM^-1 min^-1; strict blocker: The explicit paper kcat/K_ACYL column converts to 33.3333333333 s^-1 mM^-1, while the export row carries 31.0 s^-1 mM^-1 from central-cell division; not strict exact..

raw_value_unit_evidence: TABLE FOUR. Kinetic parameters for the enoyl reductase activity of wild-type HFAS as a function of chain length (T4), row Dodecenoyl-CoA (C12); columns kcat, K_ACYL, and kcat/K_ACYL columns: 13 ± 5 min^-1; K_ACYL 7 ± 1 µM; kcat/K_ACYL 2 ± 1 µM^-1 min^-1.

row_label: Dodecenoyl-CoA (C12)

substrate: Dodecenoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49327 and applied mutation signature K1699A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: TABLE THREE enoyl reductase block, enzyme row K1699A; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 9 min^-1; KNADPH cell = 400 uM; kcat/KNADPH cell = 0.02; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | K1699A HFAS, the site-directed K1699A mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE enoyl reductase block, enzyme row K1699A: Km NADPH 400 uM | kcat 9 min^-1 | kcat/Km NADPH printed cell 0.02 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE enoyl reductase block, enzyme row K1699A: KNADPH = 400 uM; kcat = 9 min^-1; printed kcat/KNADPH = 0.02 uM^-1 min^-1.

table_label: TABLE THREE (kinetic evaluation of the wild-type and Lys-1699 mutant HFAS enzymes), enoyl reductase block; printed column heads enzyme | kcat (min^-1) | KNADPH (uM) | KCRT (uM) | kcat/KNADPH (uM^-1 min^-1) | kcat/KCRT (uM^-1 min^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49327 and applied mutation signature K1699Q with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

column_label: TABLE THREE enoyl reductase block, enzyme row K1699Q; columns kcat (min^-1), KNADPH (uM) and kcat/KNADPH (uM^-1 min^-1); kcat cell = 13 min^-1; KNADPH cell = 350 uM; kcat/KNADPH cell = 0.04; author manuscript page 15 (PDF page 15). captured primary segment: NADPH | K1699Q HFAS, the site-directed K1699Q mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE enoyl reductase block, enzyme row K1699Q: Km NADPH 350 uM | kcat 13 min^-1 | kcat/Km NADPH printed cell 0.04 under the column head kcat/KNADPH (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE enoyl reductase block, enzyme row K1699Q: KNADPH = 350 uM; kcat = 13 min^-1; printed kcat/KNADPH = 0.04 uM^-1 min^-1.


proof_lines: NADPH crotonoyl-CoA FASN


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K1699A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


column_label: TABLE THREE enoyl reductase block, enzyme row K1699Q; columns kcat (min^-1), KCRT (uM) and kcat/KCRT (uM^-1 min^-1); kcat cell = 13 min^-1; KCRT cell = 3.0 uM; kcat/KCRT cell = 4; author manuscript page 15 (PDF page 15). captured primary segment: crotonyl-CoA | K1699Q HFAS, the site-directed K1699Q mutant of recombinant human fatty-acid synthase (HFAS) expressed in Sf9 insect cells | TABLE THREE enoyl reductase block, enzyme row K1699Q: Km CRT 3.0 uM | kcat 13 min^-1 | kcat/Km CRT printed cell 4 under the column head kcat/KCRT (uM^-1 min^-1)

raw_value_unit_evidence: TABLE THREE enoyl reductase block, enzyme row K1699Q: KCRT = 3.0 uM; kcat = 13 min^-1; printed kcat/KCRT = 4 uM^-1 min^-1.


column_label: Official PMC Table 3 section T3; row label WT | enoyl reductase | crotonyl-CoA/Crotonoyl-CoA; metric columns kcat, K_CRT, kcat/K_CRT

raw_value_unit_evidence: Table 3 row WT | enoyl reductase | crotonyl-CoA/Crotonoyl-CoA; columns kcat, K_CRT, kcat/K_CRT: kcat 20 +/- 2 min^-1; K value 6 +/- 2 uM; explicit kcat/K value 3 +/- 1 uM^-1 min^-1.

table_label: TABLE THREE. Kinetic evaluation of wild-type, K1699A, and K1699Q HFAS


organism: Burkholderia pseudomallei

assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA


column_label: PMC HTML Table 1 steady-state kinetic parameters for bpmFabI-1 has row trans-2-decenoyl-CoA with kcat 335 +/- 10 min^-1, Km 5.6 +/- 0.7 microM, and kcat/Km 60 +/- 8 microM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=5.583333333333333 normalized_unit=s^-1; Km normalized_value=0.0056 normalized_unit=mM; kcat/Km normalized_value=1000 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 row trans-2-decenoyl-CoA reports kcat=335 min^-1, Km=5.6 microM, and kcat/Km=60 microM^-1 min^-1.

table_label: PMC3037155 Table 1


organism: Mycolicibacterium smegmatis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A124V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M161V to reconstruct the assayed variant sequence.


enzyme_display_name: Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit

organism: Enterococcus faecalis (strain ATCC 700802 / V583)

substrate_name: orotate

assay_conditions_summary: cofactor NADH

substrate: orotate


substrate_name: dihydroorotate

enzyme: Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit

substrate: dihydroorotate


substrate_name: NAD(+)

substrate: NAD(+)


substrate: NADH


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T266A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines:
Thr-266
InhA
phosphoablative (T266A)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T266D to reconstruct the assayed variant sequence.

proof_lines:
Thr-266
InhA
phosphomimetic (T266D/E)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T266E to reconstruct the assayed variant sequence.

proof_lines:
Thr-266
InhA
An InhA-T266E mutant


organism: uncultured bacterium pBF1

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

assay_conditions_summary: pH 7; buffer 100 mM sodium phosphate; cofactor CoA

column_label: The Results prose states crotonyl-CoA had Km = 9.627 uM as substrate; Fig. 3B is the crotonyl-CoA concentration fit.

raw_value_unit_evidence: Km raw_value=9.627 raw_unit=uM for crotonyl-CoA.

row_label: crotonyl-CoA substrate Km segment

table_label: Results prose and Fig. 3B, NADPH-dependent ENR activity of FabL2


assay_conditions_summary: pH 7; buffer 100 mM sodium phosphate; cofactor NADPH

column_label: The Results prose states the purified protein catalyzed NADPH turnover with Michaelis constant Km = 27.64 uM; Fig. 3A is the NADPH concentration fit.

raw_value_unit_evidence: Km raw_value=27.64 raw_unit=uM for NADPH.

row_label: NADPH cofactor Km segment

table_label: Results prose and Fig. 3A, NADPH-dependent ENR activity of FabL2


enzyme_display_name: UniProt P0AEK4

organism: Escherichia coli

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

assay_conditions_summary: cofactor CoA

proof_lines: using both crotonyl-ACP and crotonyl-CoA as substrates

proof_lines: reported kcat (0.23 s^-1) and Km (2.7 mM)

enzyme: UniProt P0AEK4


substrate_name: But-2-enoyl-[acyl-carrier protein]

smiles: CC=CC(=O)S

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

substrate: But-2-enoyl-[acyl-carrier protein]


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G93S to reconstruct the assayed variant sequence.

substrate: crotonoyl-CoA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I21V to reconstruct the assayed variant sequence.

column_label: Table 1 row I21V reports kcat 925 min^-1, Km DDCOA 70 microM, and kcat/Km 13.2 microM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=15.4166666667 normalized_unit=s^-1; Km normalized_value=0.07 normalized_unit=mM; kcat/Km normalized_value=220 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=925 raw_unit=min^-1; Km raw_value=70 raw_unit=microM DDCoA; kcat/Km raw_value=13.2 raw_unit=microM^-1 min^-1

table_label: Table 1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I47T with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WGR1 and applied mutation signature S94A to reconstruct the assayed variant sequence.

column_label: Table 1 row S94A explicitly reports kcat 993 min^-1, Km DDCoA 104 microM, and kcat/Km 8.9 microM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=16.55 normalized_unit=s^-1; Km normalized_value=0.104 normalized_unit=mM; kcat/Km normalized_value=148.33333333333334 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 row S94A: kcat raw_value=993 raw_unit=min^-1; Km DDCoA raw_value=104 raw_unit=microM; kcat/Km raw_value=8.9 raw_unit=microM^-1 min^-1.

table_label: Table 1: Kinetic Parameters for Wild-Type and Mutant InhA Enzymes


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y158F to reconstruct the assayed variant sequence.

column_label: Table 1 row Y158F reports kcat 21 min^-1, Km DDCOA 70 microM, and kcat/Km 0.3 microM^-1 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.35 normalized_unit=s^-1; Km normalized_value=0.07 normalized_unit=mM; kcat/Km normalized_value=5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=21 raw_unit=min^-1; Km raw_value=70 raw_unit=microM DDCoA; kcat/Km raw_value=0.3 raw_unit=microM^-1 min^-1


organism: uncultured bacterium

substrate_name: prephenate


organism: Bacillus subtilis (strain 168)

proof_lines:
Bacillus subtilis DHOD
dihydroorotate
Km


enzyme_display_name: Enoyl-[acyl-carrier-protein] reductase [NADH], chloroplastic

organism: Arabidopsis thaliana

column_label: Results prose and Fig. 7 caption report ENR Km of 288 +/- 97 uM for crotonyl-CoA.

raw_value_unit_evidence: Km raw_value=288 +/- 97 uM raw_unit=uM

row_label: Arabidopsis ENR / crotonyl-CoA

table_label: PMC2442531 Results prose and Figure 7 caption


organism: Lactococcus lactis subsp. cremoris (strain MG1363)

proof_lines: DHODB dihydroorotate orotate


assay_conditions_summary: cofactor NAD+

proof_lines: DHODB NAD+


enzyme_display_name: UniProt P54616

organism: Bacillus subtilis

column_label: Primary-paper page 3 states the apparent Km value of bsFabI for NADH was 7 uM.

raw_value_unit_evidence: bsFabI apparent Km for NADH 7 uM

row_label: bsFabI NADH Km sentence

table_label: Characterization of the Reductases prose and Figure 2 cofactor utilization

enzyme: UniProt P54616


organism: Xanthomonas oryzae

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


enzyme_display_name: Enoyl-[acyl-carrier-protein] reductase [NADH] 1

organism: Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)

column_label: Table 1 row FabV Native column Km Crotonyl-CoA reports 1178 +/- 471 uM

raw_value_unit_evidence: Km raw_value=1178 +/- 471 raw_unit=uM

row_label: Native FabV

table_label: JBC PDF Table 1


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

column_label: Table 4 row Crotonyl-CoA reports Km 4.7 uM under the FabI column, not 704.3 uM.

normalized_value_unit_evidence: Km normalized 0.0047 mM.

raw_value_unit_evidence: Km raw 4.7 uM for FabI/crotonyl-CoA.

row_label: Crotonyl-CoA row

table_label: Table 4 kinetic parameters of P. aeruginosa FabV and FabI


enzyme_display_name: prephenate dehydrogenase (NADP(+))

organism: Ignicoccus hospitalis

assay_conditions_summary: pH 8; 353.15 K; cofactor NADP+

proof_lines:
Ignicoccus hospitalis
prephenate
prephenate dehydrogenase

enzyme: prephenate dehydrogenase (NADP(+))


organism: Pleurotus ostreatus

assay_conditions_summary: pH 7.6; 310.15 K; cofactor NAD+


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

assay_conditions_summary: pH 8; 298.15 K; cofactor CoA


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


organism: Burkholderia mallei

assay_conditions_summary: pH 7.9; 298.15 K; cofactor CoA


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


assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH


substrate_name: crotonyl-[acyl-carrier protein]

proof_lines: substrate 2-dodecenoyl-CoA, pH 7.9, 25°C

substrate: crotonyl-[acyl-carrier protein]


organism: Lactococcus lactis

substrate_name: Orotate

substrate: Orotate


substrate_name: (S)-dihydroorotate

substrate: (S)-dihydroorotate


assay_conditions_summary: pH 6.8; 303.15 K; cofactor NADH


substrate_name: octenoyl-CoA

assay_conditions_summary: pH 6.8; 303.15 K; cofactor CoA

substrate: octenoyl-CoA


proof_lines:
mutant Y158F, pH 6.8, 30°C
pH 6.8, 25°C, mutant enzyme Y158F


proof_lines:
wild-type, pH 6.8, 30°C
pH 6.8, 25°C, wild-type enzyme
wild-type, pH 7.5, 37°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA


proof_lines:
mutant S94A, pH 7.5, 37°C
pH 6.8, 25°C, mutant enzyme S94A


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


proof_lines:
pH 7.5, 25°C, wild-type enzyme
pH 6.8, 25°C, wild-type enzyme
wild-type, pH 7.5, 37°C


organism: Staphylococcus aureus

substrate_name: Crotonyl-N-acetyl-cysteamine

assay_conditions_summary: pH 7.8; 298.15 K; buffer 100 mM Na2HPO4

proof_lines: wild type enzyme, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)

substrate: Crotonyl-N-acetyl-cysteamine


assay_conditions_summary: pH 7.8; 298.15 K; buffer 100 mM Na2HPO4; cofactor NADPH


substrate_name: dodecenoyl-[Staphylococcus aureus acyl carrier protein]

proof_lines: mutant enzyme F204S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)


proof_lines: Km above 1 mM, mutant enzyme I193S, at 25°C, in 100 mM Na2HPO4 buffer (pH 7.8)


organism: Cereibacter sphaeroides


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 6.8; 298.15 K; cofactor CoA

proof_lines:
pH 6.8, 25°C, mutant enzyme Y158F
mutant enzyme Y158F, pH 6.8, 25°C


assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH


proof_lines:
pH 6.8, 25°C, mutant enzyme I21V
I21V mutant enoyl-ACP reductase


proof_lines:
pH 6.8, 25°C, mutant enzyme S94A
mutant S94A, pH 7.5, 37°C


organism: Vibrio cholerae serotype O1

assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate; cofactor NADH

proof_lines: native enzyme, in 0.1 M sodium phosphate buffer (pH 7)


assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate


substrate_name: crotonyl-CoA

assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate; cofactor CoA

substrate: crotonyl-CoA


assay_conditions_summary: pH 7; buffer 0.1 M sodium phosphate; cofactor NADPH


organism: Bacillus anthracis

proof_lines: presence of 0.006mM L-tyrosine, pH 7.5, 25°C

proof_lines: presence of 0.002 mM L-tyrosine, pH 7.5, 25°C

substrate: prephenate


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: Unknown

substrate: Unknown


organism: Cupriavidus necator


assay_conditions_summary: cofactor NAD+


organism: Burkholderia pseudomallei


substrate_name: crotonyl-[acyl-carrier-protein]

substrate: crotonyl-[acyl-carrier-protein]


substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.2; 298.15 K; cofactor CoA

proof_lines: in 10 mM sodium phosphate, pH 7.2, at 25°C


organism: Brassica napus

assay_conditions_summary: cofactor NADH


assay_conditions_summary: cofactor CoA


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 6.5; 360.15 K; cofactor NAD+


organism: Bacillus subtilis


organism: Rattus norvegicus


organism: Pseudomonas sp.

substrate_name: DELTA1-piperidine 6-carboxylate

substrate: DELTA1-piperidine 6-carboxylate


organism: Pseudomonas aeruginosa

substrate_name: CoA

substrate: CoA


enzyme_display_name: retinal dehydrogenase

proof_lines: recombinant wild-type enzyme, pH 7.2, 25°C

enzyme: retinal dehydrogenase


enzyme_display_name: glutamate-5-semialdehyde dehydrogenase

organism: Escherichia coli

substrate_name: glutamic gamma-semialdehyde

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

enzyme: glutamate-5-semialdehyde dehydrogenase

substrate: glutamic gamma-semialdehyde


enzyme_display_name: cinnamoyl-CoA reductase

organism: Triticum aestivum

substrate_name: caffeoyl-CoA

enzyme: cinnamoyl-CoA reductase

substrate: caffeoyl-CoA


enzyme_display_name: formaldehyde dehydrogenase

organism: Pseudomonas putida

substrate_name: aryl alcohol

proof_lines:
native and recombinant protein
substrate formaldehyde
substrate n-butanol

enzyme: formaldehyde dehydrogenase

substrate: aryl alcohol


organism: Bos taurus

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


enzyme_display_name: salicylaldehyde dehydrogenase

enzyme: salicylaldehyde dehydrogenase


enzyme_display_name: alcohol-forming fatty acyl-CoA reductase (NADPH)

organism: Cavia porcellus

substrate_name: NADPH

assay_conditions_summary: pH 6.8; 310.15 K; cofactor NADPH

substrate: NADPH


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

proof_lines: apparent value, in 100 mM Tris-HCl, pH 8.5, at 25°C


organism: Saccharomyces cerevisiae


organism: Saccharomyces sp.


enzyme_display_name: UniProt P31213

organism: Homo sapiens

substrate_name: androstenedione

enzyme: UniProt P31213

substrate: androstenedione


substrate_name: progesterone

substrate: progesterone


enzyme_display_name: UniProt P06762

substrate_name: Biliverdin

enzyme: UniProt P06762

substrate: Biliverdin


enzyme_display_name: UniProt P30043

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.2
Raw SKiD Env: Temp=30°C, pH=7.2

enzyme: UniProt P30043


enzyme_display_name: UniProt P72782

organism: Synechocystis sp. PCC 6803

enzyme: UniProt P72782


substrate: NADH


organism: Sinorhizobium meliloti

proof_lines: mixed-type inhibition model, at pH 7.5, temperature not specified in the publication

proof_lines: uncompetitive inhibition model, at pH 7.5, temperature not specified in the publication


enzyme_display_name: cholestenone 5alpha-reductase

organism: Digitalis lanata

substrate_name: H+; Progesterone; NADPH

assay_conditions_summary: cofactor NADPH

enzyme: cholestenone 5alpha-reductase

substrate: H+; Progesterone; NADPH


organism: Macaca fascicularis

substrate_name: testosterone

proof_lines:
isoenzyme 2
isoenzyme 1

substrate: testosterone


substrate_name: corticosterone

substrate: corticosterone


proof_lines:
isoenzyme 1
isoenzyme 2


proof_lines:
isoenzyme 2
isoenzyme 1
pH 6.0, 37°C


organism: Rhinella arenarum


organism: Penicillium crustosum


proof_lines:
pH 6.0, 37°C
isoenzyme 1
isoenzyme 2


proof_lines:
pH 7.4, 37°C
iosenzyme 2
isoform I


enzyme_display_name: 3-methyleneoxindole reductase

organism: Lathyrus oleraceus

enzyme: 3-methyleneoxindole reductase


organism: Pseudomonas fluorescens


enzyme_display_name: biliverdin reductase

assay_conditions_summary: pH 5.8; cofactor NADP+

proof_lines: mutant enzyme R185A, at pH 5.8, temperature not specified in the publication

enzyme: biliverdin reductase


proof_lines: mutant enzyme R185K, at pH 5.8, temperature not specified in the publication


proof_lines: mutant enzyme K237A, at pH 5.8, temperature not specified in the publication


proof_lines: mutant enzyme Y102F, at pH 5.8, temperature not specified in the publication


proof_lines: wild type enzyme, at pH 5.8, temperature not specified in the publication


proof_lines: mutant enzyme R246A, at pH 5.8, temperature not specified in the publication


proof_lines: mutant enzyme S184A, at pH 5.8, temperature not specified in the publication


proof_lines: mutant enzyme T169A, at pH 5.8, temperature not specified in the publication


proof_lines: mutant enzyme R188A, at pH 5.8, temperature not specified in the publication


organism: Salmo salar

substrate_name: NADPH; H+; Biliverdin

substrate: NADPH; H+; Biliverdin


substrate_name: biliverdin IXalpha

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines:
pH 7.0, 37°C, cosubstrate NADPH
pH 7.0, 37°C, cosubstrate NADH

substrate: biliverdin IXalpha


proof_lines: pH 7.0, 30°C, low Km-isoform from prostate

proof_lines: pH 7.0, 30°C, high Km-isoform from prostate


organism: Synechocystis sp.

proof_lines: enzyme has a 6-histidine-tagged amino-terminal fusion


organism: Spodoptera frugiperda

substrate_name: Unknown

substrate: Unknown


organism: Digitalis purpurea


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G196S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R145W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G183S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G34R to reconstruct the assayed variant sequence.


enzyme_display_name: Aldo-keto reductase family 1 member C2

substrate_name: (s)-tetralol (oxidation)

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

enzyme: Aldo-keto reductase family 1 member C2

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


organism: Macaca fuscata

substrate_name: Camphorquinone

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

proof_lines: mutant enzyme W254Y, in 25 mM Tris-HCl pH 7.5, at 25°C

substrate: Camphorquinone


proof_lines: mutant enzyme F154A, in 25 mM Tris-HCl pH 7.5, at 25°C


proof_lines: mutant enzyme W254A, in 25 mM Tris-HCl pH 7.5, at 25°C


proof_lines: mutant enzyme W125Y, in 25 mM Tris-HCl pH 7.5, at 25°C


substrate_name: D-xylose

substrate: D-xylose


proof_lines: mutant enzyme F279A, in 25 mM Tris-HCl pH 7.5, at 25°C


assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2: Km 22.0 uM; kcat 0.24 min^-1; kcat/Km 11 min^-1 mM^-1.


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S111L with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; cofactor NADPH

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S111A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R124A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines:
wild type enzyme, at pH 7.2 and 25°C
wild type enzyme, at pH 7.2 and 30°C


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


sequence_variant_note: Mutation signature R174A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W116F with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature W116A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R78A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R35S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


substrate_name: NADH

assay_conditions_summary: pH 7.2; cofactor NADH


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


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


substrate_name: Biliverdin

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y98F with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y98F, at pH 8.9, temperature not specified in the publication

substrate: Biliverdin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature R172A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R172A, at pH 8.9, temperature not specified in the publication


proof_lines: wild type enzyme, at pH 8.9, temperature not specified in the publication


organism: Pseudomonas putida

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

proof_lines:
cosubstrate NAD+
30°C, pH 8.0


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


substrate_name: 5alpha-androstan-3,17-dione (reduction)

substrate: 5alpha-androstan-3,17-dione (reduction)


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines: in the absence of urea, at pH 7.2 and 25°C

proof_lines: in the presence of 3 M urea, at pH 7.2 and 25°C

source_databases_merged: brenda uniprot


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

substrate: NADH


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


substrate_name: (s)-indan-1-ol (oxidation)

substrate: (s)-indan-1-ol (oxidation)


enzyme_display_name: Biliverdin reductase A

organism: Rattus norvegicus

substrate_name: biliverdin (at pH 6.75)

enzyme: Biliverdin reductase A

substrate: biliverdin (at pH 6.75)


substrate_name: NADH (at pH 6.75)

assay_conditions_summary: pH 6.75; cofactor NADH

column_label: Table 2 row RKB55 lists the cofactor Km cell under NADH at pH 6.75 as 333, with the table unit line representing uM despite OCR rendering as PM.

raw_value_unit_evidence: K for cofactors, NADH at pH 6.75 = 333 uM; PDF text renders the micro sign as p/P

row_label: RKB55 wild-type rat biliverdin reductase; cofactor NADH at pH 6.75

table_label: Table 2. Effects of mutations Ala280 and Ala291 on the kinetics of biliverdin reductase

substrate: NADH (at pH 6.75)


substrate_name: NADPH (at pH 8.7)

assay_conditions_summary: pH 8.7; cofactor NADPH

column_label: Table 2 row RKB55 lists the cofactor Km cell under NADPH at pH 8.7 as 2.9, with the table unit line representing uM despite OCR rendering as PM.

raw_value_unit_evidence: K for cofactors, NADPH at pH 8.7 = 2.9 uM; PDF text renders the micro sign as p/P

row_label: RKB55 wild-type rat biliverdin reductase; cofactor NADPH at pH 8.7

substrate: NADPH (at pH 8.7)


organism: Macaca fuscata fuscata

substrate_name: naphthalene dihydrodiol (at pH 10.0)

assay_conditions_summary: pH 10

proof_lines: mammalian dimeric dihydrodiol dehydrogenases

substrate: naphthalene dihydrodiol (at pH 10.0)


substrate_name: benzene dihydrodiol (at pH 10.0)

substrate: benzene dihydrodiol (at pH 10.0)


substrate_name: 3-deoxyglucosone (at pH 7.5)

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

substrate: 3-deoxyglucosone (at pH 7.5)


substrate_name: camphorquinone (at pH 7.5)

substrate: camphorquinone (at pH 7.5)


substrate_name: methylglyoxal (at pH 7.5)

smiles: CC(=O)C=O

substrate: methylglyoxal (at pH 7.5)


substrate_name: D-xylose (at pH 7.5)

proof_lines: kinetic analysis of the D-xylose reduction

substrate: D-xylose (at pH 7.5)


substrate_name: D-glucose (at pH 7.5)

proof_lines: pentoses hexoses

substrate: D-glucose (at pH 7.5)


substrate_name: D-Glyceraldehyde

assay_conditions_summary: pH 7.4; 298.15 K; buffer containing 0; cofactor NADP+

column_label: Table I (Substrate specificity of monkey kidney DD), substrate row 'D-Glyceraldehyde'; column 'Cofactor' = NADPH; column 'k_cat (s^-1)' = 31.4; column 'K_m (mM)' = 45; column 'K_cat/K_m (s^-1 mM^-1)' = 0.70.

normalized_value_unit_evidence: kcat: printed Table I cell 31.4 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 31.4 s^(-1). Km: printed Table I cell 45 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 45.0 mM. kcat/Km: printed Table I cell 0.70 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 0.7 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 31.4 / 45 = 0.6977777777777777 s^-1 mM^-1, of which 0.70 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row 'D-Glyceraldehyde' (cofactor NADPH): k_cat = 31.4 s^-1; K_m = 45 mM; printed K_cat/K_m = 0.70 s^-1 mM^-1.

row_label: Table I, substrate row 'D-Glyceraldehyde' with cofactor NADPH

table_label: Table I: Substrate specificity of monkey kidney DD (J. Biochem. 106, 1104-1109, 1989)

substrate: D-Glyceraldehyde


substrate_name: Camphorquinone

column_label: Table I (Substrate specificity of monkey kidney DD), substrate row 'Camphorquinone'; column 'Cofactor' = NADPH; column 'k_cat (s^-1)' = 62.5; column 'K_m (mM)' = 0.17; column 'K_cat/K_m (s^-1 mM^-1)' = 368.

normalized_value_unit_evidence: kcat: printed Table I cell 62.5 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 62.5 s^(-1). Km: printed Table I cell 0.17 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 0.17 mM. kcat/Km: printed Table I cell 368 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 368.0 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 62.5 / 0.17 = 367.6470588235294 s^-1 mM^-1, of which 368 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row 'Camphorquinone' (cofactor NADPH): k_cat = 62.5 s^-1; K_m = 0.17 mM; printed K_cat/K_m = 368 s^-1 mM^-1.

row_label: Table I, substrate row 'Camphorquinone' with cofactor NADPH

substrate: Camphorquinone


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

column_label: Table I (Substrate specificity of monkey kidney DD), substrate row 'Dihydroxyacetone'; column 'Cofactor' = NADPH; column 'k_cat (s^-1)' = 5.5; column 'K_m (mM)' = 5.4; column 'K_cat/K_m (s^-1 mM^-1)' = 1.0.

normalized_value_unit_evidence: kcat: printed Table I cell 5.5 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 5.5 s^(-1). Km: printed Table I cell 5.4 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 5.4 mM. kcat/Km: printed Table I cell 1.0 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 1.0 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 5.5 / 5.4 = 1.0185185185185184 s^-1 mM^-1, of which 1.0 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row 'Dihydroxyacetone' (cofactor NADPH): k_cat = 5.5 s^-1; K_m = 5.4 mM; printed K_cat/K_m = 1.0 s^-1 mM^-1.

row_label: Table I, substrate row 'Dihydroxyacetone' with cofactor NADPH

substrate: Dihydroxyacetone


substrate_name: Glyceraldehyde 3-phosphate

smiles: O=CC(O)COP(=O)(O)O

substrate: Glyceraldehyde 3-phosphate


substrate_name: L-Glyceraldehyde

column_label: Table I (Substrate specificity of monkey kidney DD), substrate row 'L-Glyceraldehyde'; column 'Cofactor' = NADPH; column 'k_cat (s^-1)' = 9.1; column 'K_m (mM)' = 121; column 'K_cat/K_m (s^-1 mM^-1)' = 0.08.

normalized_value_unit_evidence: kcat: printed Table I cell 9.1 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 9.1 s^(-1). Km: printed Table I cell 121 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 121.0 mM. kcat/Km: printed Table I cell 0.08 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 0.08 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 9.1 / 121 = 0.07520661157024792 s^-1 mM^-1, of which 0.08 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row 'L-Glyceraldehyde' (cofactor NADPH): k_cat = 9.1 s^-1; K_m = 121 mM; printed K_cat/K_m = 0.08 s^-1 mM^-1.

row_label: Table I, substrate row 'L-Glyceraldehyde' with cofactor NADPH

substrate: L-Glyceraldehyde


substrate_name: p-Nitrobenzaldehyde

column_label: Table I (Substrate specificity of monkey kidney DD), substrate row '4-Nitrobenzaldehyde'; column 'Cofactor' = NADPH; column 'k_cat (s^-1)' = 11.3; column 'K_m (mM)' = 3.3; column 'K_cat/K_m (s^-1 mM^-1)' = 3.4.

normalized_value_unit_evidence: kcat: printed Table I cell 11.3 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 11.3 s^(-1). Km: printed Table I cell 3.3 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 3.3 mM. kcat/Km: printed Table I cell 3.4 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 3.4 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 11.3 / 3.3 = 3.4242424242424248 s^-1 mM^-1, of which 3.4 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row '4-Nitrobenzaldehyde' (cofactor NADPH): k_cat = 11.3 s^-1; K_m = 3.3 mM; printed K_cat/K_m = 3.4 s^-1 mM^-1.

row_label: Table I, substrate row '4-Nitrobenzaldehyde' with cofactor NADPH

substrate: p-Nitrobenzaldehyde


column_label: Table I (Substrate specificity of monkey kidney DD), substrate row 'trans-Benzene dihydrodiol'; column 'Cofactor' = NADP+; column 'k_cat (s^-1)' = 14.0; column 'K_m (mM)' = 2.6; column 'K_cat/K_m (s^-1 mM^-1)' = 5.4.

normalized_value_unit_evidence: kcat: printed Table I cell 14.0 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 14.0 s^(-1). Km: printed Table I cell 2.6 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 2.6 mM. kcat/Km: printed Table I cell 5.4 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 5.4 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 14.0 / 2.6 = 5.384615384615384 s^-1 mM^-1, of which 5.4 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row 'trans-Benzene dihydrodiol' (cofactor NADP+): k_cat = 14.0 s^-1; K_m = 2.6 mM; printed K_cat/K_m = 5.4 s^-1 mM^-1.

row_label: Table I, substrate row 'trans-Benzene dihydrodiol' with cofactor NADP+


substrate_name: glycerone phosphate

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

column_label: Table I (Substrate specificity of monkey kidney DD), substrate row 'Dihydroxyacetone phosphate'; column 'Cofactor' = NADPH; column 'k_cat (s^-1)' = 4.3; column 'K_m (mM)' = 5.0; column 'K_cat/K_m (s^-1 mM^-1)' = 0.86.

normalized_value_unit_evidence: kcat: printed Table I cell 4.3 s^-1; the printed unit is already the canonical unit, so no unit conversion applies; normalized 4.3 s^(-1). Km: printed Table I cell 5.0 mM; the printed unit is already the canonical unit, so no unit conversion applies; normalized 5.0 mM. kcat/Km: printed Table I cell 0.86 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies; the printed cell normalizes to 0.86 s^(-1)*mM^(-1), and the exact full-precision quotient of the same row's two printed component cells is 4.3 / 5.0 = 0.86 s^-1 mM^-1, of which 0.86 is the printed rounding.

raw_value_unit_evidence: Table I, substrate row 'Dihydroxyacetone phosphate' (cofactor NADPH): k_cat = 4.3 s^-1; K_m = 5.0 mM; printed K_cat/K_m = 0.86 s^-1 mM^-1.

row_label: Table I, substrate row 'Dihydroxyacetone phosphate' with cofactor NADPH

substrate: glycerone phosphate


organism: Homo sapiens

proof_lines:
AKR1C2
dihydrodiol dehydrogenase
tissue distribution of its mRNA


substrate_name: 9alpha,11beta-Prostaglandin F2

substrate: 9alpha,11beta-Prostaglandin F2


substrate_name: Pregnanediol

substrate: Pregnanediol


substrate_name: progesterone (reduction)

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

substrate: progesterone (reduction)


enzyme_display_name: 3-oxo-5-alpha-steroid 4-dehydrogenase 2

substrate_name: testosterone

enzyme: 3-oxo-5-alpha-steroid 4-dehydrogenase 2

substrate: testosterone


substrate_name: progesterone

substrate: progesterone


substrate_name: androstenedione

substrate: androstenedione


substrate_name: corticosterone

substrate: corticosterone


substrate_name: cortisol

substrate: cortisol


proof_lines: recombinant human dihydrodiol dehydrogenase isoforms

proof_lines: substrate-specific excerpt not preserved


proof_lines:
DD2 cDNA
tissue distribution
recombinant isoform kinetics


organism: Solanum lycopersicum

column_label: ScienceDirect Table 2, kinetic constants for progesterone, testosterone, androstenedione of LeDET2 protein expressed in COS-7 cells, lists the Progesterone row with Km 0.75 +/- 0.05 uM.

raw_value_unit_evidence: Km raw_value=0.75 +/- 0.05 raw_unit=uM

row_label: Progesterone

table_label: ScienceDirect Table 2 PMID 15993049 LeDET2 kinetic constants


organism: Canis lupus familiaris

substrate_name: naphthalene dihydrodiol (at pH 7.5)

substrate: naphthalene dihydrodiol (at pH 7.5)


substrate_name: benzene dihydrodiol (at pH 7.5)

substrate: benzene dihydrodiol (at pH 7.5)


substrate_name: D-xylose

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Table 2. Kinetic constants of dimeric DDs and pig liver XDH for monosaccharides; row label: d-xylose; column label: Dog DD column Km; raw value 1.6 mM; normalized value 1.6 mM.

raw_value_unit_evidence: Table 2. Kinetic constants of dimeric DDs and pig liver XDH for monosaccharides; d-xylose row / Dog DD column; Km=1.6 mM.

row_label: d-xylose row / Dog DD column

substrate: D-xylose


substrate_name: 3-deoxyglucosone (at pH 7.5)

substrate: 3-deoxyglucosone (at pH 7.5)


substrate_name: camphorquinone (at pH 7.5)

substrate: camphorquinone (at pH 7.5)


substrate_name: methylglyoxal (at pH 7.5)

substrate: methylglyoxal (at pH 7.5)


enzyme_display_name: 3-oxo-5-alpha-steroid 4-dehydrogenase 1

enzyme: 3-oxo-5-alpha-steroid 4-dehydrogenase 1


assay_conditions_summary: pH 7; buffer potassium phosphate/KCl/EDTA; cofactor NADPH

column_label: PNAS scanned Table 1, row testosterone, human enzyme column Km (uM), reports 3.6; 3.6 uM normalizes to 0.0036 mM.

raw_value_unit_evidence: Km raw_value=3.6 raw_unit=uM

row_label: Table 1 row: testosterone

table_label: PNAS scanned Table 1: Characterization in vitro of rat and human steroid 5 alpha-reductases expressed in transfected COS cells


column_label: PNAS scanned Table 1, row androstenedione, human enzyme column Km (uM), reports 1.7; 1.7 uM normalizes to 0.0017 mM.

raw_value_unit_evidence: Km raw_value=1.7 raw_unit=uM

row_label: Table 1 row: androstenedione


column_label: PNAS scanned Table 1, row progesterone, human enzyme column Km (uM), reports 0.8; 0.8 uM normalizes to 0.0008 mM.

raw_value_unit_evidence: Km raw_value=0.8 raw_unit=uM

row_label: Table 1 row: progesterone


enzyme_display_name: Steroid 5-alpha-reductase DET2

organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.25; cofactor NADPH

column_label: Table 3, DET2 section, row 4-en-3-one, Km (uM) column reports 15.3 +/- 2.1.

raw_value_unit_evidence: Table 3 DET2 row 4-en-3-one: Km = 15.3 +/- 2.1 uM

row_label: DET2 / 4-en-3-one

table_label: Table 3

enzyme: Steroid 5-alpha-reductase DET2


column_label: Table 3, DET2 section, row 22-OH-4-en-3-one, Km (uM) column reports 3.9 +/- 0.4.

raw_value_unit_evidence: Table 3 DET2 row 22-OH-4-en-3-one: Km = 3.9 +/- 0.4 uM


column_label: Table 3, DET2 section, row cholest-4-en-3-one, Km (uM) column reports 8.5 +/- 2.9.

raw_value_unit_evidence: Table 3 DET2 row cholest-4-en-3-one: Km = 8.5 +/- 2.9 uM

row_label: DET2 / cholest-4-en-3-one


column_label: Table 3, DET2 section, row 22,23-diOH-4-en-3-one, Km (uM) column reports 3.0 +/- 0.4.


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S111A to reconstruct the assayed variant sequence.

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S111L to reconstruct the assayed variant sequence.


column_label: Table 1 Wild-type row, columns K_M NADPH, kcat, and kcat/K_M NADPH: 8.3 +/- 2.1 uM; 0.171 +/- 0.03 s^-1; 2.1 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km NADPH 0.0083 mM; kcat 0.171 s^(-1); independently printed kcat/K_M NADPH 21.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Wild-type row: K_M NADPH 8.3 +/- 2.1 uM; kcat 0.171 +/- 0.03 s^-1; independently printed kcat/K_M 2.1 x 10^4 M^-1 s^-1.

row_label: Wild-type

table_label: Table 1. Ser111 mutation characteristics


column_label: Results prose reports the apparent Km value for testosterone was determined to be 2.5 uM with Vmax 0.2 nmol/min/mg.

raw_value_unit_evidence: Km raw_value=2.5 uM raw_unit=uM

row_label: Arabidopsis DET2 protein expressed in human embryonic kidney 293 cells / testosterone

table_label: PMC article Results section: Kinetic Properties of Expressed DET2 Protein / Fig. 3A


column_label: Results prose reports the apparent Km value for progesterone was 0.4 uM with Vmax 0.5 nmol/min/mg.

raw_value_unit_evidence: Km raw_value=0.4 uM raw_unit=uM

row_label: Arabidopsis DET2 protein expressed in human embryonic kidney 293 cells / progesterone

table_label: PMC article Results section: Kinetic Properties of Expressed DET2 Protein / Fig. 3B


organism: Sus scrofa

proof_lines:
dimeric dihydrodiol dehydrogenase
D-xylose dehydrogenase
pig liver


substrate_name: D-xylose (at pH 7.5)

column_label: Table 2. Kinetic constants of dimeric DDs and pig liver XDH for monosaccharides; row label: d-xylose; column label: Pig DD column Km; raw value 0.8 mM; normalized value 0.8 mM.

raw_value_unit_evidence: Table 2. Kinetic constants of dimeric DDs and pig liver XDH for monosaccharides; d-xylose row / Pig DD column; Km=0.8 mM.

row_label: d-xylose row / Pig DD column

substrate: D-xylose (at pH 7.5)


proof_lines:
Raw SKiD Env: Temp=37°C, pH=6
Raw SKiD Env: Temp=37°C, pH=7.4


assay_conditions_summary: pH 6; 310.15 K; cofactor NADPH


organism: Oryctolagus cuniculus


organism: Cavia porcellus

substrate_name: Biliverdin

substrate: Biliverdin


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

proof_lines:
(S)-tetralol
1,2,3,4-Tetrahydronaphth-1-ol
Homo sapiens


substrate_name: Benzene dihydrodiol

proof_lines:
trans-benzene dihydrodiol
benzene dihydrodiol
Homo sapiens

substrate: Benzene dihydrodiol


organism: Pseudomonas sp.

substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines:
required NAD+ as hydrogen acceptor
0.22 mM for NAD+
Pseudomonas benzene dehydrogenase

substrate: NAD+


substrate_name: testosterone

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

substrate: testosterone


assay_conditions_summary: cofactor NADPH


enzyme_display_name: 7-dehydrocholesterol reductase

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

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

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

row_label: D8D7I + DHCR7 coexpression ChEH kinetic parameter

table_label: PMC2922168 Results prose and Fig. 4B

enzyme: 7-dehydrocholesterol reductase


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

proof_lines:
cosubstrate NADH
cosubstrate NADPH, rat liver


substrate_name: trans-benzene dihydrodiol

column_label: Table 2; row trans-Benzene dihydrodiol; jpDD4 (AKR1C4) columns; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

normalized_value_unit_evidence: normalized required paper values: Km=0.025 mM; kcat=1.5/60=0.025 s^-1. Extra paper kcat/Km cell normalizes to 1.0 s^-1 mM^-1 but is not required for this row.

raw_value_unit_evidence: Table 2 row trans-Benzene dihydrodiol, jpDD4 columns: Km=25 uM; kcat=1.5 min^-1; kcat/Km=0.06 min^-1 uM^-1.

row_label: jpDD4 / trans-Benzene dihydrodiol

table_label: Table 2

substrate: trans-benzene dihydrodiol


column_label: Table 2; row 4-Chromanol; jpDD4 (AKR1C4) columns; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

raw_value_unit_evidence: Table 2 row 4-Chromanol, jpDD4 columns: Km=340 uM; kcat=2.5 min^-1; kcat/Km=0.007 min^-1 uM^-1.

row_label: jpDD4 / 4-Chromanol


column_label: Table 2; row S-Indan-1-ol; jpDD4 (AKR1C4) columns; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

raw_value_unit_evidence: Table 2 row S-Indan-1-ol, jpDD4 columns: Km=420 uM; kcat=20 min^-1; kcat/Km=0.05 min^-1 uM^-1.

row_label: jpDD4 / S-Indan-1-ol


organism: Bos taurus


substrate_name: androsterone

substrate: androsterone


substrate_name: Unknown

substrate: Unknown


substrate_name: ergosterol

substrate: ergosterol


substrate_name: cortisone

substrate: cortisone


organism: Zea mays


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


proof_lines: nuclear and microsomal solubilized enzyme


proof_lines:
nuclear enzyme
microsomal membrane-bound enzyme


enzyme_display_name: aldehyde oxidase

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

proof_lines: chimeric rat/monkey enzyme, high affinity value, pH 6.0, 37°C

proof_lines: chimeric rat/monkey enzyme, low affinity value, pH 6.0, 37°C

enzyme: aldehyde oxidase


enzyme_display_name: UniProt P54550

organism: Bacillus subtilis

enzyme: UniProt P54550


substrate_name: methotrexate

substrate: methotrexate


organism: Callithrix jacchus

substrate_name: Phthalazine

proof_lines:
recombinant enzyme, pH 7.4, 37°C
liver cytosolic fraction, pH 7.4, 37°C

substrate: Phthalazine


enzyme_display_name: 2-hexadecenal reductase

smiles: CCCCCCC=CC=O

proof_lines: wild-type, pH 7.5, temperature not specified in the publication

enzyme: 2-hexadecenal reductase


smiles: CC(=O)C=C


smiles: CCCCCC(C=CC=O)O


smiles: CCC(C=CC=O)O


assay_conditions_summary: pH 7.5; cofactor NADPH


proof_lines: mutant Y59F, pH 7.5, temperature not specified in the publication


proof_lines: mutant Y53F, pH 7.5, temperature not specified in the publication


organism: Novosphingobium aromaticivorans

substrate_name: fluoranthene 2,3-dihydrodiol

assay_conditions_summary: pH 7

proof_lines:
at pH 7.0
at pH 9.5

substrate: fluoranthene 2,3-dihydrodiol


substrate_name: chrysene 3,4-dihydrodiol

substrate: chrysene 3,4-dihydrodiol


assay_conditions_summary: pH 7; cofactor NAD+

proof_lines: at pH 7.0, with biphenyl 2,3-dihydrodiol as substrate

proof_lines: at pH 7.0, with phenanthrene 3,4-dihydrodiol


smiles: CCCCCCCCCCCCCC=CC=O


assay_conditions_summary: cofactor NAD+


enzyme_display_name: 2-enoate reductase

organism: Achromobacter sp.

enzyme: 2-enoate reductase


substrate_name: NADPH


assay_conditions_summary: pH 7.5; cofactor NADH


organism: Hordeum vulgare

substrate_name: traumatin

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

substrate: traumatin


smiles: CCCCCC(=O)C=C


smiles: CCCC=CC=O


organism: Mucor circinelloides

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+


substrate_name: NADP+

proof_lines: pH 8.5, 25°C, cosubstrate: (1R,2S)-cis-1,2-dihydronaphthalene-1,2-diol

proof_lines: pH 8.5, 25°C, cosubstrate: (1R,2S)-trans-1,2-dihydronaphthalene-1,2-diol

substrate: NADP+


organism: Nocardia sp.


organism: Klebsiella pneumoniae

substrate_name: NADH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


organism: Gluconobacter oxydans

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH


organism: Heyndrickxia coagulans

substrate_name: trans-cinnamic acid

proof_lines: pH and temperature not specified in the publication

substrate: trans-cinnamic acid


substrate: NADH


organism: Lacticaseibacillus casei

protein_accession_database: NCBI Protein

assay_conditions_summary: pH 7; cofactor NADH


organism: Yersinia bercovieri

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


enzyme_display_name: maleylacetate reductase

organism: Pimelobacter simplex

substrate_name: maleylacetate

enzyme: maleylacetate reductase

substrate: maleylacetate


organism: Sphingobium chlorophenolicum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K140A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 23°C, mutant enzyme K140A, cosubstrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H241A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 23°C, mutant enzyme H241A, cosubstrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H236A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 23°C, mutant enzyme H236A, cosubstrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H237A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 23°C, mutant enzyme H237A, cosubstrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H251A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 23°C, mutant enzyme H251A, cosubstrate: NADH


organism: Escherichia coli (strain K12)

substrate_name: trans-3,5-cyclohexadiene-1,2-diol (at pH 7.4 and 37 degrees Celsius)

proof_lines: kcat is 5550 min(-1) for dehydrogenase activity with 2,3-dihydro-2,3-dihydroxybenzoate as substrate (at pH 7.4 and 37 degrees Celsius). kcat is 1380 min(-1) for dehydrogenase activity with cis-3-hydroxy-4-cyclohexene-1-carboxylate as substr


substrate_name: 2-cyclohexen-1-ol (at pH 7.4 and 37 degrees Celsius)


organism: Artemisia annua

substrate_name: beta-ionone

substrate: beta-ionone


organism: Pseudomonas putida

proof_lines:
at pH 7.0 and 25°C
at pH 9.4 and 25°C
strain G7


substrate_name: NAD+

proof_lines:
at pH 7.0 and 25°C
at pH 9.4 and 25°C
strain biotype A grown on toluene

substrate: NAD+


organism: Clostridium acetobutylicum


substrate_name: cis-Toluene dihydrodiol

substrate: cis-Toluene dihydrodiol


substrate_name: cis-benzene dihydrodiol

substrate: cis-benzene dihydrodiol


assay_conditions_summary: pH 7; 296.15 K; cofactor NADPH

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 2; row NADH / 2-CMA; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 2 row NADH / 2-CMA: Km 0.09 mM; kcat 17.6 s^-1; kcat/Km 195.6 s^-1 mM^-1.

row_label: NADH / 2-CMA

table_label: Table 2. Apparent kinetic parameters for recombinant PcpE


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H236A to reconstruct the assayed variant sequence.

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 1; row H236A; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

table_label: Table 1. Apparent kinetic parameters for recombinant PcpE and its mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H237A to reconstruct the assayed variant sequence.

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 1; row H237A; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row H237A: Km 0.93 mM; kcat 3.8 s^-1; kcat/Km 4.1 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H241A to reconstruct the assayed variant sequence.

column_label: Scientific Reports DOI 10.1038/s41598-017-18475-8 Table 1; row H241A; columns Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).