sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R63Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


enzyme_display_name: NADPH---hemoprotein reductase

organism: Gallus gallus

substrate_name: NADPH; Cytochrome c; H+

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

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

assay_conditions_summary: cofactor NADP+

enzyme: NADPH---hemoprotein reductase

substrate: NADPH; Cytochrome c; H+

status: unverified


organism: Homo sapiens

substrate_name: Ferricytochrome c; NADPH; H+

substrate: Ferricytochrome c; NADPH; H+


enzyme_display_name: NADPH--cytochrome P450 reductase 1

organism: Oryza sativa subsp. japonica

substrate_name: cytochrome c

source_db: uniprot

source_license: CC BY 4.0

enzyme: NADPH--cytochrome P450 reductase 1

substrate: cytochrome c

source: uniprot


enzyme_display_name: NADPH--cytochrome P450 reductase 2

enzyme: NADPH--cytochrome P450 reductase 2


enzyme_display_name: NADPH-hemoprotein reductase

organism: Picrorhiza kurrooa

substrate_name: oxidized cytochrome c

source_db: brenda

enzyme: NADPH-hemoprotein reductase

substrate: oxidized cytochrome c

source: brenda


organism: Rattus norvegicus


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase

organism: Priestia megaterium (strain ATCC 14581 / DSM 32 / CCUG 1817 / JCM 2506 / NBRC 15308 / NCIMB 9376 / NCTC 10342 / NRRL B-14308 / VKM B-512 / Ford 19)

substrate_name: lauric acid at pH 7.4 at room temperature

proof_lines: kcat is 84.1 sec(-1) for lauric acid (PubMed:16403573). kcat is 1480 min(-1) for palmitic acid. kcat is 1880 min(-1) for N-palmitoylglycine. kcat is 1690 min(-1) for N-palmitoyl-L-methionine. kcat is 610 min(-1) for N-palmitoyl-L-glutamine.


organism: Saccharomyces cerevisiae

substrate_name: Cytochrome c; H+; NADPH

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

sequence_source: multiple

assay_conditions_summary: cofactor NADPH

proof_lines: The Vmax of the reaction is 721 pmol/min/pmol enzyme towards cytochrome c, and 662 pmol/min/pmol enzyme toward NADPH.

substrate: Cytochrome c; H+; NADPH


enzyme_display_name: Quinone reductase

organism: Escherichia coli (strain K12)

substrate_name: uranyl (at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7

proof_lines: kcat is 3.7 sec(-1) with chromate as substrate (at pH 5 and 35 degrees Celsius) (PubMed:14766567). kcat is 29 sec(-1) with uranyl as substrate (at pH 7 and 37 degrees Celsius) (PubMed:17088379). kcat is 30 sec(-1) with chromate as substrate

enzyme: Quinone reductase

substrate: uranyl (at pH 7 and 37 degrees Celsius)


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Kluyveromyces marxianus

substrate_name: 1,4-Benzoquinone; H+; NADPH

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: 1,4-Benzoquinone; H+; NADPH


source_db: oed

data_origin: experimental

source: oed


enzyme_display_name: NAD(P)H dehydrogenase [quinone] 1

organism: Mus musculus

substrate_name: Unknown

km_display: Not reported

enzyme: NAD(P)H dehydrogenase [quinone] 1

substrate: Unknown


enzyme_display_name: cytochrome-b5 reductase

organism: Sus scrofa

substrate_name: ferricytochrome b5

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K97R to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: cytochrome-b5 reductase

substrate: ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature R63K with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


organism: Anopheles minimus

substrate_name: ferricytochrome c

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature L86F/L219F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L86F/L219F, pH not specified in the publication, at 25°C

substrate: ferricytochrome c


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase 1

organism: Bacillus subtilis (strain 168)

substrate_name: cytochrome c (in the reductase assay)

proof_lines: kcat is 430 min(-1) for stearic acid hydroxylation. kcat is 5430 min(-1) for phytanic acid hydroxylation. kcat is 6105 min(-1) for 15-methylpalmitic acid hydroxylation. kcat is 11400 min(-1) for the reduction of cytochrome c. kcat is 38150

substrate: cytochrome c (in the reductase assay)


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase 2

proof_lines: kcat is 104 min(-1) for lauric acid hydroxylation. kcat is 5556 min(-1) for myristic acid hydroxylation. kcat is 676 min(-1) for palmitic acid hydroxylation. kcat is 374 min(-1) for stearic acid hydroxylation. kcat is 794 min(-1) for phytan


organism: Capsicum annuum


enzyme_display_name: Monodehydroascorbate reductase

organism: Pisum sativum

enzyme: Monodehydroascorbate reductase


organism: Triphysaria versicolor

proof_lines: kcat is 23.3 sec(-1) with 9,10-phenanthrenequinone as substrate. kcat is 2.44 sec(-1) with 1,2-naphthoquinone as substrate. kcat is 0.31 sec(-1) with 5-hydroxy-1,4-naphthoquinone as substrate. kcat is 0.09 sec(-1) with 2,6-dimethoxy-p-benzo


enzyme_display_name: 2-hydroxy-1,4-benzoquinone reductase

organism: Burkholderia sp

enzyme: 2-hydroxy-1,4-benzoquinone reductase


organism: Pseudomonas putida


organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

proof_lines: kcat is 930 sec(-1) with benzoquinone as substrate (at pH 7.5 and 70 degrees Celsius) (PubMed:15840577). kcat is 440 sec(-1) with menaquinone as substrate (at pH 8.0 and 60 degrees Celsius) (PubMed:15840577). kcat is 25 sec(-1) with duroqui


proof_lines: kcat is 0.075 min(-1) NADH with as substrate. kcat is 0.074 min(-1) with NADPH as substrate.


ki_unit: mM


enzyme_display_name: Monodehydroascorbate reductase, fruit isozyme

organism: Cucumis sativus


enzyme_display_name: Monodehydroascorbate reductase II

organism: Glycine max

sequence: AKTFKYIILG

wild_type_sequence: AKTFKYIILG

enzyme: Monodehydroascorbate reductase II


enzyme_display_name: monodehydroascorbate reductase (NADH)

organism: Arabidopsis thaliana

substrate_name: Monodehydroascorbate; H+; NADH

assay_conditions_summary: cofactor NADH

enzyme: monodehydroascorbate reductase (NADH)

substrate: Monodehydroascorbate; H+; NADH


enzyme_display_name: NADPH:quinone reductase

organism: Cavia porcellus

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: NADPH:quinone reductase


organism: Homo sapiens

kcat_over_km_origin: calculated


enzyme_display_name: p-benzoquinone reductase (NADPH)

organism: Pseudomonas sp.

enzyme: p-benzoquinone reductase (NADPH)


enzyme_display_name: Self-sufficient cytochrome P450 monooxygenase CYP505E3

organism: Phanerodontia chrysosporium

substrate_name: nonanol

verification_status: verified

smiles: CCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 9 nonanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=3.8 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 9 nonanol: Km 3,800 uM (3.8 mM); kcat 250 min^-1; kcat/Km 6.6 × 10−2 min^-1 uM^-1.

row_label: C 9 nonanol

substrate: nonanol

status: verified


substrate_name: decanol

smiles: CCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 10 decanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=1.1 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 10 decanol: Km 1,100 uM (1.1 mM); kcat 220 min^-1; kcat/Km 2.0 × 10−3 min^-1 uM^-1.

row_label: C 10 decanol

enzyme: Self-sufficient cytochrome P450 monooxygenase CYP505E3

substrate: decanol


substrate_name: undecanol

smiles: CCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 11 undecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.42 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 11 undecanol: Km 420 uM (0.42 mM); kcat 310 min^-1; kcat/Km 0.74 min^-1 uM^-1.

row_label: C 11 undecanol

substrate: undecanol


substrate_name: dodecanol

smiles: CCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 12 dodecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.35 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 12 dodecanol: Km 350 uM (0.35 mM); kcat 350 min^-1; kcat/Km 1.0 min^-1 uM^-1.

row_label: C 12 dodecanol

substrate: dodecanol


substrate_name: tridecanol

smiles: CCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 13 tridecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.12 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 13 tridecanol: Km 120 uM (0.12 mM); kcat 370 min^-1; kcat/Km 3.1 min^-1 uM^-1.

row_label: C 13 tridecanol

substrate: tridecanol


substrate_name: tetradecanol

smiles: CCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 14 tetradecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.02 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 14 tetradecanol: Km 20 uM (0.02 mM); kcat 450 min^-1; kcat/Km 23 min^-1 uM^-1.

row_label: C 14 tetradecanol

substrate: tetradecanol


substrate_name: pentadecanol

smiles: CCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 15 pentadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.01 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 15 pentadecanol: Km 10 uM (0.01 mM); kcat 490 min^-1; kcat/Km 49 min^-1 uM^-1.

row_label: C 15 pentadecanol

substrate: pentadecanol


substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 16 hexadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.018 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 16 hexadecanol: Km 18 uM (0.018 mM); kcat 510 min^-1; kcat/Km 28 min^-1 uM^-1.

row_label: C 16 hexadecanol

substrate: hexadecanol


substrate_name: heptadecanol

smiles: CCCCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 17 heptadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.015 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 17 heptadecanol: Km 15 uM (0.015 mM); kcat 340 min^-1; kcat/Km 23 min^-1 uM^-1.

row_label: C 17 heptadecanol

substrate: heptadecanol


substrate_name: octadecanol

smiles: CCCCCCCCCCCCCCCCCCO

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 18 octadecanol; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.019 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 18 octadecanol: Km 19 uM (0.019 mM); kcat 330 min^-1; kcat/Km 17 min^-1 uM^-1.

row_label: C 18 octadecanol

substrate: octadecanol


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K97A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row K97A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); K97A / ferricytochrome b5: Km 16.1 +/- 2.7 uM; kcat 191 +/- 18 s^-1; kcat/Km 11.9 +/- 3.1 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0161 mM; kcat=191.0 s^-1; kcat/Km=11900.0 s^-1*mM^-1.

row_label: K97A / ferricytochrome b5

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K97R to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row K97R / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); K97R / ferricytochrome b5: Km 6.9 +/- 0.5 uM; kcat 415 +/- 12 s^-1; kcat/Km 60.1 +/- 6.1 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0069 mM; kcat=415.0 s^-1; kcat/Km=60100.0 s^-1*mM^-1.

row_label: K97R / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature R63A to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row R63A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); R63A / ferricytochrome b5: Km 42.1 +/- 4.7 uM; kcat 121 +/- 10 s^-1; kcat/Km 2.9 +/- 0.6 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0421 mM; kcat=121.0 s^-1; kcat/Km=2900.0 s^-1*mM^-1.

row_label: R63A / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature R63K to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row R63K / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); R63K / ferricytochrome b5: Km 7.3 +/- 0.4 uM; kcat 347 +/- 9 s^-1; kcat/Km 47.5 +/- 3.8 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0073 mM; kcat=347.0 s^-1; kcat/Km=47500.0 s^-1*mM^-1.

row_label: R63K / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature R63Q to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row R63Q / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); R63Q / ferricytochrome b5: Km 18.5 +/- 1.4 uM; kcat 105 +/- 4 s^-1; kcat/Km 5.7 +/- 0.6 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0185 mM; kcat=105.0 s^-1; kcat/Km=5700.0 s^-1*mM^-1.

row_label: R63Q / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature S99A to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row S99A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); S99A / ferricytochrome b5: Km 14.8 +/- 2.2 uM; kcat 295 +/- 23 s^-1; kcat/Km 19.9 +/- 4.5 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0148 mM; kcat=295.0 s^-1; kcat/Km=19900.0 s^-1*mM^-1.

row_label: S99A / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature S99T to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row S99T / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); S99T / ferricytochrome b5: Km 11.8 +/- 2.3 uM; kcat 520 +/- 49 s^-1; kcat/Km 44.1 +/- 12.8 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0118 mM; kcat=520.0 s^-1; kcat/Km=44100.0 s^-1*mM^-1.

row_label: S99T / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature S99V to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row S99V / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); S99V / ferricytochrome b5: Km 9.9 +/- 2.0 uM; kcat 165 +/- 14 s^-1; kcat/Km 16.7 +/- 4.8 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0099 mM; kcat=165.0 s^-1; kcat/Km=16700.0 s^-1*mM^-1.

row_label: S99V / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature Y65A to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row Y65A / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); Y65A / ferricytochrome b5: Km 5.0 +/- 0.7 uM; kcat 107 +/- 5 s^-1; kcat/Km 21.4 +/- 4.0 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.005 mM; kcat=107.0 s^-1; kcat/Km=21400.0 s^-1*mM^-1.

row_label: Y65A / ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P83686 and applied mutation signature Y65F to reconstruct the assayed variant sequence.

column_label: Table III. Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+; row Y65F / ferricytochrome b5; columns Km Pb5 (uM), kcat Pb5 (s^-1), and kcat Pb5/Km Pb5 (uM^-1*s^-1); Y65F / ferricytochrome b5: Km 6.2 +/- 0.4 uM; kcat 375 +/- 9 s^-1; kcat/Km 60.5 +/- 5.4 uM^-1*s^-1. Direct unit conversion divides Km by 1000 and multiplies kcat/Km by 1000 to give Km=0.0062 mM; kcat=375.0 s^-1; kcat/Km=60500.0 s^-1*mM^-1.

row_label: Y65F / ferricytochrome b5


substrate_name: nonanoic acid

smiles: CCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 9 nonanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=4.5 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 9 nonanoic acid: Km 4,500 uM (4.5 mM); kcat 200 min^-1; kcat/Km 4.4 × 10−2 min^-1 uM^-1.

row_label: C 9 nonanoic acid

substrate: nonanoic acid


substrate_name: decanoic acid

smiles: CCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 10 decanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=1.4 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 10 decanoic acid: Km 1,400 uM (1.4 mM); kcat 230 min^-1; kcat/Km 0.16 min^-1 uM^-1.

row_label: C 10 decanoic acid

substrate: decanoic acid


substrate_name: undecanoic acid

smiles: CCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 11 undecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.61 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 11 undecanoic acid: Km 610 uM (0.61 mM); kcat 230 min^-1; kcat/Km 0.38 min^-1 uM^-1.

row_label: C 11 undecanoic acid

substrate: undecanoic acid


substrate_name: dodecanoic acid

smiles: CCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 12 dodecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.45 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 12 dodecanoic acid: Km 450 uM (0.45 mM); kcat 250 min^-1; kcat/Km 0.56 min^-1 uM^-1.

row_label: C 12 dodecanoic acid

substrate: dodecanoic acid


substrate_name: tridecanoic acid

smiles: CCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 13 tridecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.23 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 13 tridecanoic acid: Km 230 uM (0.23 mM); kcat 310 min^-1; kcat/Km 1.4 min^-1 uM^-1.

row_label: C 13 tridecanoic acid

substrate: tridecanoic acid


substrate_name: tetradecanoic acid

smiles: CCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 14 tetradecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.065 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 14 tetradecanoic acid: Km 65 uM (0.065 mM); kcat 320 min^-1; kcat/Km 4.9 min^-1 uM^-1.

row_label: C 14 tetradecanoic acid

substrate: tetradecanoic acid


substrate_name: pentadecanoic acid

smiles: CCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 15 pentadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.03 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 15 pentadecanoic acid: Km 30 uM (0.03 mM); kcat 390 min^-1; kcat/Km 13 min^-1 uM^-1.

row_label: C 15 pentadecanoic acid

substrate: pentadecanoic acid


substrate_name: hexadecanoic acid

smiles: CCCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 16 hexadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.038 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 16 hexadecanoic acid: Km 38 uM (0.038 mM); kcat 330 min^-1; kcat/Km 8.7 min^-1 uM^-1.

row_label: C 16 hexadecanoic acid

substrate: hexadecanoic acid


substrate_name: heptadecanoic acid

smiles: CCCCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 17 heptadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.036 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 17 heptadecanoic acid: Km 36 uM (0.036 mM); kcat 280 min^-1; kcat/Km 7.8 min^-1 uM^-1.

row_label: C 17 heptadecanoic acid

substrate: heptadecanoic acid


substrate_name: octadecanoic acid

smiles: CCCCCCCCCCCCCCCCCC(=O)O

column_label: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6; row C 18 octadecanoic acid; column Km (uM), normalized to mM.

normalized_value_unit_evidence: km paper=0.028 mM

raw_value_unit_evidence: TABLE 1 | Kinetic parameters of saturated fatty alcohol (C9-18) and fatty acid (C9-18) conversions by CYP505D6, row C 18 octadecanoic acid: Km 28 uM (0.028 mM); kcat 260 min^-1; kcat/Km 9.3 min^-1 uM^-1.

row_label: C 18 octadecanoic acid

substrate: octadecanoic acid


organism: Paracoccus denitrificans

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

column_label: Table 2 / row FerBHis6-E77A / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77A normalized: K_m 0.18 mM; kcat 17.9 s^-1; kcat/K_m 99 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-E77A: K_m 180±30 uM; kcat 17.9±3.0 s^-1; kcat/K_m 99±23 mM^-1 s^-1.

table_label: Table 2

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77K to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-E77K / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77K normalized: K_m 0.03 mM; kcat 0.75 s^-1; kcat/K_m 25 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-E77K: K_m 30±8 uM; kcat 0.75±0.05 s^-1; kcat/K_m 25±7 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77L to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-E77L / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77L normalized: K_m 0.25 mM; kcat 0.072 s^-1; kcat/K_m 0.29 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature E77M to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-E77M / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-E77M normalized: K_m 0.42 mM; kcat 2.5 s^-1; kcat/K_m 6 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G115F to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G115F; columns Km NADH 410 uM (normalized 0.41 mM); kcat 2.2 s^-1; printed kcat/Km 5.4 mM^-1 s^-1; export-normalized kcat/Km 5.36585365853659 from same-row values

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; Km normalized_value=0.41 normalized_unit=mM from 410 uM; kcat/Km normalized_value=5.36585365853659 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=2.2 raw_unit=s^-1; Km raw_value=410 raw_unit=uM for NADH; printed kcat/Km=5.4 mM^-1 s^-1

table_label: Table 2. Kinetic parameters and standard redox potentials of FerBHis6 for the wild-type and mutant variants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G115I to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G115I; columns Km NADH 630 uM (normalized 0.63 mM); kcat 1.7 s^-1; printed kcat/Km 2.7 mM^-1 s^-1; export-normalized kcat/Km 2.6984126984127 from same-row values

normalized_value_unit_evidence: kcat normalized_value=1.7 normalized_unit=s^-1; Km normalized_value=0.63 normalized_unit=mM from 630 uM; kcat/Km normalized_value=2.6984126984127 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=1.7 raw_unit=s^-1; Km raw_value=630 raw_unit=uM for NADH; printed kcat/Km=2.7 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G118F to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G118F; columns Km NADH 85 uM (normalized 0.085 mM); kcat 77 s^-1; printed kcat/Km 906 mM^-1 s^-1; export-normalized kcat/Km 905.882352941176 from same-row values

normalized_value_unit_evidence: kcat normalized_value=77 normalized_unit=s^-1; Km normalized_value=0.085 normalized_unit=mM from 85 uM; kcat/Km normalized_value=905.882352941176 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=77 raw_unit=s^-1; Km raw_value=85 raw_unit=uM for NADH; printed kcat/Km=906 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G118I to reconstruct the assayed variant sequence.

column_label: PDF Table 2 row FerBHis6-G118I; columns Km NADH 38 uM (normalized 0.038 mM); kcat 12 s^-1; printed kcat/Km 316 mM^-1 s^-1; export-normalized kcat/Km 315.789473684211 from same-row values

normalized_value_unit_evidence: kcat normalized_value=12 normalized_unit=s^-1; Km normalized_value=0.038 normalized_unit=mM from 38 uM; kcat/Km normalized_value=315.789473684211 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; Km raw_value=38 raw_unit=uM for NADH; printed kcat/Km=316 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R80E to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R80E / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R80E normalized: K_m 0.03 mM; kcat 0.275 s^-1; kcat/K_m 9.2 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R80K to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R80K / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R80K normalized: K_m 0.35 mM; kcat 9.5 s^-1; kcat/K_m 27 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-R80K: K_m 350±80 uM; kcat 9.5±1.4 s^-1; kcat/K_m 27±7 mM^-1 s^-1.


organism: Sus scrofa

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P83686 and applied mutation signature K97A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: Table III (Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+), printed enzyme-form row 'K97A', NADH metric group; column 'Km^NADH (uM)' = 4.4; column 'kcat^NADH (s-1)' = 1060; column 'kcat^NADH/Km^NADH (uM-1 s-1)' = 240. The value printed after the plus/minus sign beside each of those cells is the printed uncertainty and is not an exported metric (0.3, 19 and 21 respectively). The same printed line also carries the Pb5 metric group ('Km^Pb5 (uM)' = 16.1, 'kcat^Pb5 (s-1)' = 191, 'kcat^Pb5/Km^Pb5 (uM-1 s-1)' = 11.9) and a dissociation-constant column for NAD+.

normalized_value_unit_evidence: Km: printed Table III cell 4.4 in a column headed Km^NADH (uM); 4.4 / 1000 = 0.0044 mM. kcat: printed Table III cell 1060 in a column headed kcat^NADH (s-1); s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1060.0 s^(-1). kcat/Km: printed Table III cell 240 in a column headed kcat^NADH/Km^NADH (uM-1 s-1); 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 240 x 1000 = 240000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, printed enzyme-form row 'K97A', NADH metric group: Km^NADH = 4.4 uM; kcat^NADH = 1060 s-1; printed kcat^NADH/Km^NADH = 240 uM-1 s-1.

table_label: Table III: Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+ (J. Biochem. 2001, 130(4):481-490). Printed column heads: Enzyme; under the group head NADH: Km^NADH (uM), kcat^NADH (s-1), kcat^NADH/Km^NADH (uM-1 s-1); under the group head Pb5: Km^Pb5 (uM), kcat^Pb5 (s-1), kcat^Pb5/Km^Pb5 (uM-1 s-1); then Kd^NAD+ (uM).


sequence_variant_note: Mutation signature K97R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines:
porcine NADH-cytochrome b5 reductase
RXY(T/S)+(T/S) motif
Arg63


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature R63A to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme R63A and substrate NADH.

normalized_value_unit_evidence: kcat 403 s^-1; Km 0.104 mM; printed kcat/Km 3900 s^-1 mM^-1; quotient of printed kcat and Km is 3875 s^-1 mM^-1.

row_label: R63A; NADH

table_label: Table III, Apparent kinetic parameters evaluated by steady-state analysis and dissociation constants for NAD+


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature R63K to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme R63K and substrate NADH.

normalized_value_unit_evidence: kcat 515 s^-1; Km 0.0021 mM; printed kcat/Km 245000 s^-1 mM^-1; current export uses rounded Km 0.002 mM and quotient 257500 s^-1 mM^-1.

row_label: R63K; NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature R63Q to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme R63Q and substrate NADH.

normalized_value_unit_evidence: kcat 412 s^-1; Km 0.021 mM; printed kcat/Km 19600 s^-1 mM^-1; quotient of printed kcat and Km is 19619.04761904762 s^-1 mM^-1.

row_label: R63Q; NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature S99A to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme S99A and substrate NADH.

normalized_value_unit_evidence: kcat 435 s^-1; Km 0.026 mM; printed kcat/Km 16700 s^-1 mM^-1; quotient of printed kcat and Km is 16730.76923076923 s^-1 mM^-1.

row_label: S99A; NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature S99T to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme S99T and substrate NADH.

normalized_value_unit_evidence: kcat 851 s^-1; Km 0.0019 mM; printed kcat/Km 447000 s^-1 mM^-1; current export uses rounded Km 0.002 mM and quotient 425500 s^-1 mM^-1.

row_label: S99T; NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature S99V to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme S99V and substrate NADH.

normalized_value_unit_evidence: kcat 375 s^-1; Km 0.0094 mM; printed kcat/Km 39500 s^-1 mM^-1; current export uses rounded Km 0.009 mM and quotient 41666.66666666667 s^-1 mM^-1.

row_label: S99V; NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature Y65A to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme Y65A and substrate NADH.

normalized_value_unit_evidence: kcat 180 s^-1; Km 0.0042 mM; printed kcat/Km 42900 s^-1 mM^-1; current export uses rounded Km 0.004 mM and quotient 45000 s^-1 mM^-1.

row_label: Y65A; NADH


sequence_variant_note: Resolved canonical sequence from uniprotkb:P83686;rcsb:1NDH and applied mutation signature Y65F to reconstruct the assayed variant sequence.

column_label: Table III columns enzyme, NADH Km (uM), NADH kcat (s^-1), and NADH kcat/Km (uM^-1 s^-1); row matched by enzyme Y65F and substrate NADH.

row_label: Y65F; NADH


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R80L to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R80L / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R80L normalized: K_m 0.58 mM; kcat 0.142 s^-1; kcat/K_m 0.24 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R80M to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R80M / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R80M normalized: K_m 0.78 mM; kcat 0.302 s^-1; kcat/K_m 0.39 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R95A to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R95A / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R95A normalized: K_m 0.02 mM; kcat 146 s^-1; kcat/K_m 7292 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-R95A: K_m 20±2 uM; kcat 146±4 s^-1; kcat/K_m 7292±756 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature R95E to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-R95E / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-R95E normalized: K_m 0.07 mM; kcat 21.1 s^-1; kcat/K_m 302 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-R95E: K_m 70±9 uM; kcat 21.1±0.9 s^-1; kcat/K_m 302±41 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature S113A to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-S113A / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-S113A normalized: K_m 0.06 mM; kcat 76.7 s^-1; kcat/K_m 1278 s^-1 mM^-1.


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

column_label: PDF Table 2 row FerBHis6; columns Km NADH 22 uM (normalized 0.022 mM); kcat 258 s^-1; printed kcat/Km 11727 mM^-1 s^-1; export-normalized kcat/Km 11727.2727272727 from same-row values

normalized_value_unit_evidence: kcat normalized_value=258 normalized_unit=s^-1; Km normalized_value=0.022 normalized_unit=mM from 22 uM; kcat/Km normalized_value=11727.2727272727 normalized_unit=s^-1*mM^-1 from same-row kcat/Km

raw_value_unit_evidence: kcat raw_value=258 raw_unit=s^-1; Km raw_value=22 raw_unit=uM for NADH; printed kcat/Km=11727 mM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot:A1B9E3;rcsb:3U7R and applied mutation signature Y78A to reconstruct the assayed variant sequence.

column_label: Table 2 / row FerBHis6-Y78A / columns K_m (uM), kcat (s^-1), and kcat/K_m (mM^-1 s^-1); note says values were obtained from initial velocity kinetic analysis at constant UQ-0 concentration of 0.1 mM.

normalized_value_unit_evidence: Table 2 row FerBHis6-Y78A normalized: K_m 0.04 mM; kcat 196 s^-1; kcat/K_m 4900 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row FerBHis6-Y78A: K_m 40±10 uM; kcat 196±13 s^-1; kcat/K_m 4900±1267 mM^-1 s^-1.


organism: Rattus norvegicus

substrate_name: Hexacyanoferrate(III)

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H62A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

substrate: Hexacyanoferrate(III)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H62M with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H85A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H85M with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


substrate_name: NADPH

substrate: NADPH


substrate_name: ferricytochrome b5

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H49A with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

substrate: ferricytochrome b5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H49E 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 H49K 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 H49Y with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; 298.15 K; buffer 116 mM MOPS; cofactor NADPH

column_label: Abstract kinetic summary, parenthetical for the NADPH:ferricyanide activity of the wild-type cb5/cb5r fusion protein: cell kcat = 21.7 s^-1, cell Km NADPH = 1 uM, cell Km FeCN6 = 8 uM. The catalog row takes the varied substrate NADPH, so it reads the kcat cell and the Km NADPH cell of that parenthetical.

normalized_value_unit_evidence: kcat: printed abstract cell 21.7 s^-1, already in s^-1, so no unit conversion applies, and the exported value is 21.7 s^(-1). Km: printed abstract cell 1 uM, and 1 / 1000 = 0.001 mM, which is the exported value. kcat/Km: the paper prints no efficiency cell, so the exported ratio is typed as the quotient of the two printed cells of this same abstract tuple, 21.7 / 0.001 = 21700.0 s^-1 mM^-1, which is the exported value 21700.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Abstract parenthetical for the NADPH:ferricyanide activity of the wild-type cb5/cb5r fusion protein: printed kcat = 21.7 s^-1 and printed Km NADPH = 1 uM. The paper prints no catalytic-efficiency cell for this or any other measurement.

row_label: Abstract parenthetical for the NADPH:ferricyanide activity of the wild-type cb5/cb5r fusion protein, varied substrate NADPH

table_label: Abstract kinetic summary of the rat cb5/cb5r fusion protein, Archives of Biochemistry and Biophysics 2002, 400(1):63-75


enzyme_display_name: Cytochrome b5 reductase 4

substrate_name: ferricyanide

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table II; row Wild-Type; KmFeCN = 28.2 +/- 3.5 uM; normalized Km = 0.0282 mM.

row_label: Wild-Type

table_label: Table II. Initial-Rate Kinetic Constants for Rat Liver cb5/cb5r Fusion Protein and the Various Histidine Mutants

enzyme: Cytochrome b5 reductase 4

substrate: ferricyanide


column_label: Abstract prose; row/condition NADPH:ferricyanide; metric KNADPHm; raw KNADPHm = 1 uM; normalized Km = 0.001 mM.

raw_value_unit_evidence: KNADPHm = 1 uM

table_label: Abstract prose kinetic parenthetical


organism: Fusarium oxysporum

assay_conditions_summary: pH 6.5; cofactor NADPH

column_label: Wiley full-text HTML Table 2 row Nonanoic acid column K m (microM) reports 3200, converted to 3.2 mM.

raw_value_unit_evidence: Km raw_value=3200 raw_unit=microM

row_label: Nonanoic acid

table_label: Table 2. Kinetic constants of rP450foxy for various saturated fatty acids

enzyme: Bifunctional cytochrome P450/NADPH--P450 reductase


column_label: Wiley full-text HTML Table 2 row Decanoic acid column K m (microM) reports 260, converted to 0.26 mM.

raw_value_unit_evidence: Km raw_value=260 raw_unit=microM

row_label: Decanoic acid


column_label: Wiley full-text HTML Table 2 row Undecanoic acid column K m (microM) reports 160, converted to 0.16 mM.

raw_value_unit_evidence: Km raw_value=160 raw_unit=microM

row_label: Undecanoic acid


column_label: Wiley full-text HTML Table 2 row Tridecanoic acid column K m (microM) reports 36, converted to 0.036 mM.

raw_value_unit_evidence: Km raw_value=36 raw_unit=microM

row_label: Tridecanoic acid


column_label: Wiley full-text HTML Table 2 row Tetradecanoic acid column K m (microM) reports 19, converted to 0.019 mM.

raw_value_unit_evidence: Km raw_value=19 raw_unit=microM

row_label: Tetradecanoic acid


column_label: Wiley full-text HTML Table 2 row Pentadecanoic acid column K m (microM) reports 8, converted to 0.008 mM.

raw_value_unit_evidence: Km raw_value=8 raw_unit=microM

row_label: Pentadecanoic acid


column_label: Wiley full-text HTML Table 2 row Hexadecanoic acid column K m (microM) reports 10, converted to 0.01 mM.

raw_value_unit_evidence: Km raw_value=10 raw_unit=microM

row_label: Hexadecanoic acid


enzyme_display_name: NADPH--hemoprotein reductase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A635G with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

enzyme: NADPH--hemoprotein reductase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A635G/R636S with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D634A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D634N with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R636A with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R636S with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


proof_lines:
wild type
His49
mutant series


enzyme_display_name: NADPH-dependent quinone reductase ArsH

organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)

proof_lines:
ArsH
Synechocystis sp. PCC 6803
NADPH-dependent quinone reductase

enzyme: NADPH-dependent quinone reductase ArsH


substrate_name: dibromothymoquinone

proof_lines:
ArsH
Synechocystis sp. PCC 6803
quinone reductase

substrate: dibromothymoquinone


substrate_name: duroquinone

substrate: duroquinone


substrate_name: menadione

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

proof_lines:
ArsH
Synechocystis sp. PCC 6803
menadione

substrate: menadione


substrate_name: lawsone

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

substrate: lawsone


substrate_name: coenzyme Q10 (approximate value)

proof_lines:
ArsH
quinone reductase activity
quinones with hydrophobic substituents

substrate: coenzyme Q10 (approximate value)


substrate_name: methyl-red

substrate: methyl-red


organism: Kluyveromyces marxianus

proof_lines:
1,4-benzoquinone
quinone substrates
hydroquinones


substrate_name: hydroquinone

proof_lines:
quinone substrates
hydroquinones

substrate: hydroquinone


enzyme_display_name: NADPH quinone oxidoreductase

enzyme: NADPH quinone oxidoreductase


enzyme_display_name: UniProt P0A8G6

organism: Escherichia coli

source_db: skid

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

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADH

column_label: Official PMC Table 2 row 'NADH / WrbA E. coli', required metric column 'kcat_app (s^-1)': 8.9 +/- 0.064 s^-1; row footnote: K3FeCN6 was the electron acceptor.

normalized_value_unit_evidence: kcat normalized_value=8.9 normalized_unit=s^-1; Km normalized_value=0.014 normalized_unit=mM; printed kcat/Km normalized_value=640 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 WrbA E. coli cells: kcat raw_value=8.9 +/- 0.064 raw_unit=s^-1; Km raw_value=14 +/- 0.43 raw_unit=uM; kcat/Km raw_value=6.4 x 10^5 +/- 0.20 x 10^5 raw_unit=M^-1 s^-1; footnote=K3FeCN6 was the electron acceptor.

row_label: NADH / WrbA E. coli

table_label: Table 2. Apparent kinetic parameters of WrbA E. coli and WrbA A. fulgidus

source_databases_merged: skid uniprot

enzyme: UniProt P0A8G6

source: skid


column_label: Official PMC Table 2 row 'NADH / WrbA E. coli', required metric column 'Km_app (uM)': 14 +/- 0.43 uM; row footnote: K3FeCN6 was the electron acceptor.


column_label: Official PMC Table 2 row '1,4-Benzoquinone / WrbA E. coli', required metric column 'kcat_app (s^-1)': 370 +/- 1.7 s^-1; row footnote: NADH was the electron donor.

normalized_value_unit_evidence: kcat normalized_value=370 normalized_unit=s^-1; Km normalized_value=0.0058 normalized_unit=mM; printed kcat/Km normalized_value=64000 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 WrbA E. coli cells: kcat raw_value=370 +/- 1.7 raw_unit=s^-1; Km raw_value=5.8 +/- 0.12 raw_unit=uM; kcat/Km raw_value=6.4 x 10^7 +/- 0.14 x 10^7 raw_unit=M^-1 s^-1; footnote=NADH was the electron donor.

row_label: 1,4-Benzoquinone / WrbA E. coli


substrate_name: benzoquinone

column_label: Official PMC Table 2 row '1,4-Benzoquinone / WrbA E. coli', required metric column 'Km_app (uM)': 5.8 +/- 0.12 uM; row footnote: NADH was the electron donor.

substrate: benzoquinone


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

column_label: Official PMC Table 2 row 1,4-Benzoquinone / WrbA E. coli: kcat/Km 6.4 x 10^7 +/- 0.14 x 10^7 M^-1 s^-1 | kcat 370 +/- 1.7 s^-1 | Km 5.8 +/- 0.12 uM.

normalized_value_unit_evidence: kcat normalized_value=370 normalized_unit=s^-1; Km normalized_value=0.0058 normalized_unit=mM; kcat/Km ratio normalized_value=63793.10344827587 normalized_unit=s^-1*mM^-1; printed kcat/Km normalized_value=64000.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 WrbA E. coli 1,4-Benzoquinone cells: kcat raw_value=370 +/- 1.7 raw_unit=s^-1; Km raw_value=5.8 +/- 0.12 raw_unit=uM; kcat/Km raw_value=6.4 x 10^7 +/- 0.14 x 10^7 raw_unit=M^-1 s^-1; footnote=NADH was the electron donor.

table_label: Table 2. Apparent kinetic parameters of WrbA E. coli and WrbA A. fulgidus.


normalized_value_unit_evidence: kcat normalized_value=8.9 normalized_unit=s^-1; Km normalized_value=0.014 normalized_unit=mM; kcat/Km ratio normalized_value=635.7142857142858 normalized_unit=s^-1*mM^-1; printed kcat/Km normalized_value=640.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 WrbA E. coli NADH cells: kcat raw_value=8.9 +/- 0.064 raw_unit=s^-1; Km raw_value=14 +/- 0.43 raw_unit=uM; kcat/Km raw_value=6.4 x 10^5 +/- 0.20 x 10^5 raw_unit=M^-1 s^-1; footnote=K3FeCN6 was the electron acceptor.


assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

proof_lines:
WrbA
Escherichia coli
NADH


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.2; cofactor NADH

column_label: Official PMC Table 2 row NADH / WrbA A. fulgidus: kcat/Km 6.3 x 10^6 +/- 0.59 x 10^6 M^-1 s^-1 | kcat 120 +/- 2.9 s^-1 | Km 19 +/- 1.7 uM.

normalized_value_unit_evidence: kcat normalized_value=120 normalized_unit=s^-1; Km normalized_value=0.019 normalized_unit=mM; kcat/Km ratio normalized_value=6315.789473684211 normalized_unit=s^-1*mM^-1; printed kcat/Km normalized_value=6300.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 WrbA A. fulgidus NADH cells: kcat raw_value=120 +/- 2.9 raw_unit=s^-1; Km raw_value=19 +/- 1.7 raw_unit=uM; kcat/Km raw_value=6.3 x 10^6 +/- 0.59 x 10^6 raw_unit=M^-1 s^-1; footnote=K3FeCN6 was the electron acceptor.

row_label: NADH / WrbA A. fulgidus

source_databases_merged: brenda uniprot


assay_conditions_summary: pH 7.2; cofactor NADPH

proof_lines:
WrbA
Archaeoglobus fulgidus
NADH


column_label: Official PMC Table 2 row 1,4-Benzoquinone / WrbA A. fulgidus: kcat/Km 8.6 x 10^7 +/- 0.090 x 10^7 M^-1 s^-1 | kcat 3,200 +/- 130 s^-1 | Km 37 +/- 3.6 uM.

normalized_value_unit_evidence: kcat normalized_value=3200 normalized_unit=s^-1; Km normalized_value=0.037 normalized_unit=mM; kcat/Km ratio normalized_value=86486.4864864865 normalized_unit=s^-1*mM^-1; printed kcat/Km normalized_value=86000.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 2 WrbA A. fulgidus 1,4-Benzoquinone cells: kcat raw_value=3,200 +/- 130 raw_unit=s^-1; Km raw_value=37 +/- 3.6 raw_unit=uM; kcat/Km raw_value=8.6 x 10^7 +/- 0.090 x 10^7 raw_unit=M^-1 s^-1; footnote=NADH was the electron donor.

row_label: 1,4-Benzoquinone / WrbA A. fulgidus


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R139W to reconstruct the assayed variant sequence.

column_label: Table 3 row NQO1 R139W; Menadione columns kcat (s^-1), KM (uM), and kcat/KM (uM^-1 s^-1).

normalized_value_unit_evidence: kcat normalized_value=1730 normalized_unit=s^-1 | km normalized_value=0.0106 normalized_unit=mM | kcat_over_km normalized_value=162000 normalized_unit=s^-1 mM^-1

row_label: NQO1 R139W

table_label: Table 3. Steady state kinetic parameters for NQO1 and NQO1 R139W


column_label: Table 3 row NQO1 R139W; NADH columns kcat,app (s^-1), KM,app (mM), and kcat,app/KM,app (mM^-1 s^-1).

normalized_value_unit_evidence: kcat normalized_value=1580 normalized_unit=s^-1 | km normalized_value=3.31 normalized_unit=mM | kcat_over_km normalized_value=478 normalized_unit=s^-1 mM^-1


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

column_label: Table II; row NADH / DMBQ; use NAD(P)H metric columns for pyridine-nucleotide rows and Oxidant metric columns for quinone/thio-NAD+ oxidant rows; footnotes ND/not determined and detection-limit note preserved.

normalized_value_unit_evidence: normalized required metrics for DMBQ as oxidant: kcat=2.8 s^-1; Km=0.011 mM; central quotient=2.8/0.011=254.54545454545453 mM^-1 s^-1; printed table value rounds to 250 mM^-1 s^-1.

raw_value_unit_evidence: Table II row NADH / DMBQ: kcat=2.8 +/- 0.1 s^-1; oxidant Km=11 +/- 1 uM; oxidant kcat/Km=(2.5 +/- 0.2) x 10^5 M^-1 s^-1

row_label: NADH / DMBQ

table_label: Table II


column_label: Table II; row NADH / 5-HNQ; use NAD(P)H metric columns for pyridine-nucleotide rows and Oxidant metric columns for quinone/thio-NAD+ oxidant rows; footnotes ND/not determined and detection-limit note preserved.

normalized_value_unit_evidence: normalized paper values: kcat=2.5 s^-1; oxidant Km=0.0055 mM; oxidant kcat/Km=450 mM^-1 s^-1. Current export has Km=0.005 mM and kcat/Km=500 mM^-1 s^-1.

row_label: NADH / 5-HNQ


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

normalized_value_unit_evidence: normalized required metrics for NADH as pyridine nucleotide: kcat=2.8 s^-1; Km=0.036 mM; central quotient=2.8/0.036=77.77777777777779 mM^-1 s^-1; printed table value rounds to 77 mM^-1 s^-1.


column_label: Table II; row NADPH / 5-HNQ; use NAD(P)H metric columns for pyridine-nucleotide rows and Oxidant metric columns for quinone/thio-NAD+ oxidant rows; footnotes ND/not determined and detection-limit note preserved.

normalized_value_unit_evidence: normalized paper values for NADPH as pyridine nucleotide: kcat=0.0079 s^-1; Km=0.00044 mM; kcat/Km=18 mM^-1 s^-1. Current export has kcat=0.008, Km=0.0005 mM, and kcat/Km=16.

row_label: NADPH / 5-HNQ


substrate_name: thio-NAD+

substrate: thio-NAD+


column_label: PMID 10848984 Table 1; guinea-pig ZCr columns kcat, Km, kcat/Km; footnote says values recalculated from cited earlier work

raw_value_unit_evidence: Guinea-pig ZCr columns: kcat 4.9 s^-1; Km 27 uM; kcat/Km 0.18

row_label: Guinea-pig ZCr; 5-Hydroxy-1,4-naphtoquinone (juglone)

table_label: PMID 10848984 Table 1


raw_value_unit_evidence: Guinea-pig ZCr columns: kcat 5.9 s^-1; Km 143 uM; kcat/Km 0.04

row_label: Guinea-pig ZCr; 1,4-Benzoquinone


assay_conditions_summary: cofactor NADPH

column_label: PMID 1370456 Table II; NADPH row; Km column

raw_value_unit_evidence: NADPH Km 0.5 in the Table II Km column with unit 10^-5 M

row_label: zeta-crystallin; NADPH substrate row

table_label: PMID 1370456 Table II


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: 5-HNQ (with NADPH at pH 7.5 and at 25 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor NADPH

normalized_value_unit_evidence: normalized required Km-only metric: 0.39 uM = 0.00039 mM.

raw_value_unit_evidence: Table II row NADPH / 5-HNQ: oxidant Km=0.39 +/- 0.04 uM for 5-HNQ


substrate_name: NADPH (with 5-HNQ at pH 7.5 and at 25 degrees Celsius)

normalized_value_unit_evidence: normalized required Km-only metric: 0.44 uM = 0.00044 mM.

raw_value_unit_evidence: Table II row NADPH / 5-HNQ: NAD(P)H Km=0.44 +/- 0.06 uM for NADPH


substrate_name: NADH (with 5-HNQ at pH 7.5 and at 25 degrees Celsius)

normalized_value_unit_evidence: normalized required Km-only metric: 28 uM = 0.028 mM.

raw_value_unit_evidence: Table II row NADH / 5-HNQ: NAD(P)H Km=28 +/- 2 uM for NADH


substrate_name: menadione (at pH 7.5)

proof_lines:
Mycobacterium tuberculosis
LpdA
NAD(P)H-dependent quinone reduction

substrate: menadione (at pH 7.5)


enzyme_display_name: UniProt P15559

enzyme: UniProt P15559


substrate_name: NADH


enzyme_display_name: NAD(P)H dehydrogenase [quinone] 1


proof_lines:
NQO2
oxidation-reduction dyes
quercetin

enzyme: NAD(P)H dehydrogenase (quinone)


substrate_name: Methyl red

substrate: Methyl red


organism: Pseudomonas aeruginosa

column_label: Table 3; 1,4-Naphthoquinones section, naphthoquinone row; app(kcat/Km)=1250000 ± 400000 M^-1 s^-1, appkcat=80 ± 10 s^-1, and appKm=100 ± 25 μM.

row_label: 1,4-Naphthoquinones: naphthoquinone

table_label: Table 3. Apparent Steady-State Kinetic Parameters of PA0660 with Various Quinones


column_label: Table 3; row 1,4-Benzoquinones | 2,6-dimethoxy-; columns app(kcat/Km) (M^-1 s^-1), app kcat (s^-1), and app Km (μM); condition NADPH 50 μM, pH 7.5, 25 °C.

raw_value_unit_evidence: Table 3; 1,4-Benzoquinones; 2,6-dimethoxy- row: app(kcat/Km) 16000 M^-1 s^-1; app kcat 41 s^-1; app Km 2500 μM.

row_label: 1,4-Benzoquinones | 2,6-dimethoxy-

table_label: Table 3. Apparent Steady-State Kinetic Parameters of PA0660 with Various Quinones as Electron Acceptors at Fixed Saturating Concentration of NADPHa


column_label: Table 3; row 1,4-Naphthoquinones | 2-methyl-; columns app(kcat/Km) (M^-1 s^-1), app kcat (s^-1), and app Km (μM); condition NADPH 50 μM, pH 7.5, 25 °C.

raw_value_unit_evidence: Table 3; 1,4-Naphthoquinones; 2-methyl- row: app(kcat/Km) 300000 M^-1 s^-1; app kcat 63 s^-1; app Km 230 μM.

row_label: 1,4-Naphthoquinones | 2-methyl-


column_label: Table 1; NADH row at 60 μM DCPIP; app(kcat/Km)=50000 ± 10000 M^-1 s^-1, appkcat=13 ± 1 s^-1, and appKm=240 ± 40 μM.

row_label: NADH; [DCPIP]=60 μM

table_label: Table 1. Apparent Steady-State Kinetic Parameters of PA0660 for NADPH or NADH


substrate_name: NADPH

column_label: Table 1; NADPH row at 80 μM DCPIP; app(kcat/Km)=1000000 ± 300000 M^-1 s^-1, appkcat=16 ± 2 s^-1, and appKm=16 ± 5 μM.

row_label: NADPH; [DCPIP]=80 μM


column_label: Table 3; row 1,4-Benzoquinones | 2,3-dimethoxy-5-; columns app(kcat/Km) (M^-1 s^-1), app kcat (s^-1), and app Km (μM); condition NADPH 50 μM, pH 7.5, 25 °C.

raw_value_unit_evidence: Table 3; 1,4-Benzoquinones; 2,3-dimethoxy-5- row: app(kcat/Km) 130000 M^-1 s^-1; app kcat 66 s^-1; app Km 500 μM.

row_label: 1,4-Benzoquinones | 2,3-dimethoxy-5- methyl- (Q0)


column_label: Table 3; row 1,4-Naphthoquinones | 5-hydroxy-; columns app(kcat/Km) (M^-1 s^-1), app kcat (s^-1), and app Km (μM); condition NADPH 50 μM, pH 7.5, 25 °C.

raw_value_unit_evidence: Table 3; 1,4-Naphthoquinones; 5-hydroxy- row: app(kcat/Km) 1100000 M^-1 s^-1; app kcat 82 s^-1; app Km 74 μM.

row_label: 1,4-Naphthoquinones | 5-hydroxy-


column_label: Table 3; 1,4-Benzoquinones section, benzoquinone row; app(kcat/Km)=250000 ± 50000 M^-1 s^-1, appkcat=87 ± 9 s^-1, and appKm=370 ± 70 μM.

row_label: 1,4-Benzoquinones: benzoquinone


proof_lines:
pH 7.5
quinone specificity


organism: Mus musculus

proof_lines:
DT-diaphorase
CB 1954
mouse

enzyme: NAD(P)H dehydrogenase [quinone] 1


assay_conditions_summary: cofactor NADH

proof_lines: DT-diaphorase NAD(P)H mouse


proof_lines:
DT-diaphorase
CB 1954
5-(aziridin-1-yl)-2,4-dinitrobenzamide


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7; cofactor NADH


substrate_name: monodehydroascorbate

substrate: monodehydroascorbate


enzyme_display_name: NADH--cytochrome b5 reductase 1

enzyme: NADH--cytochrome b5 reductase 1

substrate: NADH


enzyme_display_name: Bifunctional cytochrome P450/NADPH--P450 reductase

organism: Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711)

substrate_name: palmitic acid

assay_conditions_summary: pH 7.4; cofactor NADPH

column_label: Table 2; row Palmitic acid; column Km (uM).

row_label: Palmitic acid

table_label: Table 2

substrate: palmitic acid


substrate_name: linoleic acid

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

column_label: Table 2; row Linoleic acid; column Km (uM).

row_label: Linoleic acid

substrate: linoleic acid


proof_lines:
Cytochrome P450foxy
Fusarium oxysporum
fatty-acid hydroxylase


substrate_name: laurate

smiles: CCCCCCCCCCCC(=O)[O-]

substrate: laurate


organism: Pseudomonas sp. WBC-3

substrate_name: p-benzoquinone

column_label: Section PnpB catalyzes reduction of p-benzoquinone to hydroquinone states H6-PnpB Km values for NADPH and benzoquinone were 181.6 +/- 43.5 and 6.7 +/- 2.8 uM, respectively.

raw_value_unit_evidence: Km 6.7 +/- 2.8 uM for benzoquinone.

row_label: H6-PnpB / p-benzoquinone

table_label: Results prose: PnpB catalyzes reduction of p-benzoquinone to hydroquinone

substrate: p-benzoquinone


normalized_value_unit_evidence: Km 0.1816 mM; exported 0.181 mM is rounded/truncated from the paper value.

row_label: H6-PnpB / NADPH

substrate: NADPH


enzyme_display_name: cytochrome-b5 reductase

organism: Badhamia polycephala

column_label: PMID 17341833 abstract/kinetic paragraph, NADH row/segment, apparent Km = 2 uM.

raw_value_unit_evidence: Apparent Km value for NADH was 2 uM.

row_label: NADH substrate

table_label: Abstract and kinetic-properties paragraph for recombinant NADH-cytochrome b5 reductase

source_databases_merged: brenda skid

enzyme: cytochrome-b5 reductase


enzyme_display_name: NADPH--cytochrome P450 reductase 1

organism: Artemisia annua

enzyme: NADPH--cytochrome P450 reductase 1


enzyme_display_name: 2-hydroxy-1,4-benzoquinone reductase

organism: Burkholderia sp

enzyme: 2-hydroxy-1,4-benzoquinone reductase


enzyme_display_name: NADPH--cytochrome P450 reductase 2

substrate_name: NADPH (at pH 7.7 and 28 degrees Celsius)

assay_conditions_summary: pH 7.7; cofactor NADPH

enzyme: NADPH--cytochrome P450 reductase 2


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


enzyme_display_name: NADH-cytochrome b5 reductase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: NADH-cytochrome b5 reductase 1


enzyme_display_name: NADPH-hemoprotein reductase

organism: Locusta migratoria migratorioides

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

proof_lines:
ecdysone 20-monooxygenase
NADPH
cytochrome P-450 reductase

enzyme: NADPH-hemoprotein reductase


enzyme_display_name: Quinone reductase

organism: Pseudomonas putida

substrate_name: chromate (at pH 5 and 50 degrees Celsius)

enzyme: Quinone reductase


enzyme_display_name: Quinone oxidoreductase PIG3

organism: Homo sapiens

enzyme: Quinone oxidoreductase PIG3


enzyme_display_name: Quinone oxidoreductase 2

organism: Escherichia coli (strain K12)

substrate_name: methyl-1,4-benzoquinone (MBQ)

enzyme: Quinone oxidoreductase 2

substrate: methyl-1,4-benzoquinone (MBQ)


proof_lines:
QOR2
NADPH
Rossmann fold


organism: Leishmania major


enzyme_display_name: NADPH:quinone reductase

sequence_variant_note: Mutation signature T53F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

smiles: CCCC=CC=O

enzyme: NADPH:quinone reductase


sequence_variant_note: Mutation signature T59F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


smiles: CCCCCCC=CC=O


smiles: CC/C=C/C=O


smiles: C=CC(C)=O


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 2 (Kinetic analysis of human f-crystallin), 3-Alken-2-ones block, body row '3-Buten-2-one'; column 'Km (lM)' = 35; column 'kcat (min-1)' = 10; column 'kcat/Km (min-1 mM-1)' = 290. The printed caption line is 'Table 2 Kinetic analysis of human f-crystallin'.

normalized_value_unit_evidence: kcat: printed Table 2 cell 10 in a column headed kcat (min-1); 1 min^-1 is 1/60 s^-1, so 10 / 60 = 0.16666666666666666 s^(-1). Km: printed Table 2 cell 35 in a column headed Km (lM), which is micromolar; 1 uM is 0.001 mM, so 35 / 1000 = 0.035 mM. kcat/Km: printed Table 2 cell 290 in a column headed kcat/Km (min-1 mM-1); 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 290 / 60 = 4.833333333333333 s^(-1)*mM^(-1). The exported values are kcat 0.16 s^(-1), Km 0.035 mM and kcat_over_km 4.571428571428571 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, 3-Alken-2-ones block, body row '3-Buten-2-one': Km = 35 in a column headed Km (lM); kcat = 10 in a column headed kcat (min-1); printed kcat/Km = 290 in a column headed kcat/Km (min-1 mM-1). The value printed after the plus/minus sign in each of those three cells is the printed standard error and is not an exported metric.

table_label: Table 2: Kinetic analysis of human f-crystallin (Cell. Mol. Life Sci. 2011, 68:1065-1077). Printed column heads: Km (lM); kcat (min-1); kcat/Km (min-1 mM-1). The printed body is grouped under the substrate-class headings Quinones, 2-Alkenals, 3-Alken-2-ones, Prostaglandins, n-Alkanals and n-Alkenes. In every rendering of this PDF the micro sign of the Km head prints as the letter l, so Km (lM) is the printed Km in micromolar.


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


column_label: Table 2 (Kinetic analysis of human f-crystallin), 3-Alken-2-ones block, body row '3-Nonen-2-one'; column 'Km (lM)' = 940; column 'kcat (min-1)' = 13; column 'kcat/Km (min-1 mM-1)' = 14. The printed caption line is 'Table 2 Kinetic analysis of human f-crystallin'.

normalized_value_unit_evidence: kcat: printed Table 2 cell 13 in a column headed kcat (min-1); 1 min^-1 is 1/60 s^-1, so 13 / 60 = 0.21666666666666667 s^(-1). Km: printed Table 2 cell 940 in a column headed Km (lM), which is micromolar; 1 uM is 0.001 mM, so 940 / 1000 = 0.94 mM. kcat/Km: printed Table 2 cell 14 in a column headed kcat/Km (min-1 mM-1); 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 14 / 60 = 0.23333333333333334 s^(-1)*mM^(-1). The exported values are kcat 0.21 s^(-1), Km 0.94 mM and kcat_over_km 0.22340425531914895 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, 3-Alken-2-ones block, body row '3-Nonen-2-one': Km = 940 in a column headed Km (lM); kcat = 13 in a column headed kcat (min-1); printed kcat/Km = 14 in a column headed kcat/Km (min-1 mM-1). The value printed after the plus/minus sign in each of those three cells is the printed standard error and is not an exported metric.


organism: Triticum monococcum

substrate_name: menadione

proof_lines:
Triticum monococcum
wheat quinone reductases
QR2

substrate: menadione


organism: Botryococcus braunii


organism: Rattus norvegicus

substrate_name: ferricytochrome b5

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

substrate: ferricytochrome b5


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH


enzyme_display_name: UniProt P32340

organism: Saccharomyces cerevisiae

source_license: CC BY-NC-ND 4.0

assay_conditions_summary: pH 6

enzyme: UniProt P32340


enzyme_display_name: UniProt P23457

enzyme: UniProt P23457


substrate_name: ferricytochrome c

substrate: ferricytochrome c


mutation_type: deletion


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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
wild-type enzyme
wild type enzyme, at pH 7.5 and 25°C


enzyme_display_name: NADPH dehydrogenase (quinone)

organism: Bacillus subtilis

substrate_name: duroquinone

enzyme: NADPH dehydrogenase (quinone)

substrate: duroquinone


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


column_label: Table 2 columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row 3-Penten-2-one.

raw_value_unit_evidence: Table 2 row 3-Penten-2-one reports Km 535 +/- 34 uM, kcat 12 +/- 0.2 min^-1, and kcat/Km 22 +/- 1.5 min^-1 mM^-1.

row_label: Table 2 row 3-Penten-2-one under 3-Alken-2-ones

table_label: PMID 20835842, Table 2: Kinetic analysis of human zeta-crystallin


column_label: Table 2 columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row 4-Hydroxy-2-hexenal.

raw_value_unit_evidence: Table 2 row 4-Hydroxy-2-hexenal reports Km 130 +/- 26 uM, kcat 80 +/- 5 min^-1, and kcat/Km 613 +/- 130 min^-1 mM^-1.

row_label: Table 2 row 4-Hydroxy-2-hexenal under 2-Alkenals


substrate_name: propenal

substrate: propenal


column_label: Table 2 columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row Propenal.

raw_value_unit_evidence: Table 2 row Propenal reports Km 1,450 +/- 200 uM, kcat 100 +/- 4 min^-1, and kcat/Km 70 +/- 10 min^-1 mM^-1.

row_label: Table 2 row Propenal under 2-Alkenals


column_label: Table 2 columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1); row 4-Hydroxy-2-nonenal.

raw_value_unit_evidence: Table 2 row 4-Hydroxy-2-nonenal reports Km 550 +/- 136 uM, kcat 69 +/- 7.4 min^-1, and kcat/Km 126 +/- 34 min^-1 mM^-1.

row_label: Table 2 row 4-Hydroxy-2-nonenal under 2-Alkenals


organism: Gluconobacter oxydans

substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH


substrate_name: Unknown

substrate: Unknown


organism: Sus scrofa

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM potassium phosphate; cofactor NADH

proof_lines: mutant P249L, ferricyanide as electron acceptor

proof_lines: mutant enzyme P249L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant enzyme P249L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


organism: Spinacia oleracea

substrate_name: NADPH


proof_lines: mutant P247L, ferricyanide as electron acceptor

proof_lines: mutant enzyme P247L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM potassium phosphate

proof_lines: mutant enzyme P247L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: wild type enzyme, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: lysosome- and detergent-solubilized enzyme


proof_lines: mutant enzyme P247A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant enzyme P248A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines:
native enzyme
in the presence of 2 mM Ca2+


proof_lines: mutant P247A, ferricyanide as electron acceptor

proof_lines: mutant enzyme P247A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant enzyme P249A, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant enzyme P248L, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant P248L, ferricyanide as electron acceptor

proof_lines: mutant enzyme P248L, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant P248A, ferricyanide as electron acceptor

proof_lines: mutant enzyme P248A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


proof_lines: mutant P249A, ferricyanide as electron acceptor

proof_lines: mutant enzyme P249A, using ferricyanide as cosubstrate, in 100 mM potassium phosphate buffer (pH 7.0) at 25°C


organism: Xanthomonas citri

assay_conditions_summary: pH 6; cofactor NADPH


organism: Synechocystis sp.

substrate_name: coenzyme Q10

proof_lines: pH 8.0, 25°C, recombinant His-tagged enzyme

substrate: coenzyme Q10


substrate_name: dibromothymoquinone

substrate: dibromothymoquinone


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


organism: Kluyveromyces marxianus


substrate_name: hydroquinone

substrate: hydroquinone


enzyme_display_name: NADH:quinone reductase

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

proof_lines: kcat is 14 sec(-1) with 5,8-dihydroxy-1,4-naphthoquinone as substrate. kcat is 17 sec(-1) with 5-hydroxy-1,4-naphthoquinone as substrate. kcat is 16 sec(-1) with 2-methyl-5-hydroxy-1,4-naphthoquinone as substrate. kcat is 16 sec(-1) with 2-

enzyme: NADH:quinone reductase


enzyme_display_name: Alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial

organism: Arabidopsis thaliana


enzyme_display_name: Type II NADH:quinone oxidoreductase

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

substrate_name: DMN

smiles: CN(C)N=O

proof_lines: kcat is 67.9 sec(-1) with DMN as substrate. kcat is 69.4 sec(-1) with DDB as substrate. kcat is 68.2 sec(-1) with DQ as substrate.

enzyme: Type II NADH:quinone oxidoreductase

substrate: DMN


substrate_name: DQ

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

substrate: DQ


substrate: NADH


substrate_name: decyl-plastoquinone

enzyme: Alternative NAD(P)H-ubiquinone oxidoreductase C1, chloroplastic/mitochondrial

substrate: decyl-plastoquinone


enzyme_display_name: NADPH dehydrogenase

enzyme: NADPH dehydrogenase


enzyme_display_name: demethylphylloquinone reductase

proof_lines:
pH 7.5, 30°C, recombinant enzyme
kcat is 3.2 sec(-1) for menadione.

enzyme: demethylphylloquinone reductase


assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: pH 7.0, temperature not specified in the publication


organism: Shewanella oneidensis

substrate_name: nitroglycerin

substrate: nitroglycerin


substrate_name: NEM

substrate: NEM


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


organism: Trypanosoma cruzi


enzyme_display_name: Carbonyl reductase [NADPH] 3

organism: Homo sapiens

proof_lines: kcat is 0.55 min(-1) with menadione as substrate (PubMed:18493841). kcat is 0.70 min(-1) with 4-benzoylpyridine as substrate (PubMed:18493841). kcat is 0.59 min(-1) with 4-nitorobenzaldehyde as substrate (PubMed:18493841).

enzyme: Carbonyl reductase [NADPH] 3


substrate_name: isatin

substrate: isatin


substrate_name: oracin

substrate: oracin


organism: Bacillus subtilis (strain 168)

proof_lines: The highest catalytic efficiency was observed with N-ethylmaleimide for which the KM is inferior to 1.0 uM.


substrate_name: menadione

substrate: menadione


organism: Chloroflexus aggregans (strain MD-66 / DSM 9485)

proof_lines: kcat is 2.27 sec(-1) with 4-ketoisophorone as substrate. kcat is 3.82 sec(-1) with 2-cyclohexen-1-one as substrate. kcat is 12.13 sec(-1) with 1-octen-3-one as substrate.


smiles: CCCCCC(=O)C=C


organism: Rattus norvegicus

proof_lines: kcat is 14 min(-1) with 4-benzoylpyridine as substrate (PubMed:18983987). kcat is 0.030 min(-1) with menadione as substrate (PubMed:18983987).


enzyme_display_name: NADH dehydrogenase (quinone)

organism: Plasmodium yoelii yoelii

substrate_name: H+; NADH; Ubiquinone-1

enzyme: NADH dehydrogenase (quinone)

substrate: H+; NADH; Ubiquinone-1


organism: Beta vulgaris

substrate_name: Ubiquinone; NADH; H+

substrate: Ubiquinone; NADH; H+


organism: Escherichia coli (strain K12)

substrate_name: ubiquinone-3 (for NADH:quinone oxidoreductase activity)


organism: Saccharomyces cerevisiae


substrate_name: oxidized nitroblue tetrazolium hydrochloride


substrate_name: NADPH

substrate: NADPH


substrate_name: H+; Menadione; NADPH

assay_conditions_summary: cofactor NADP+

substrate: H+; Menadione; NADPH


substrate_name: Menadione; H+; NADPH

substrate: Menadione; H+; NADPH


substrate_name: Unknown

substrate: Unknown


substrate_name: DDB

substrate: DDB


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y55F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y55S to reconstruct the assayed variant sequence.


organism: Bacillus subtilis

substrate_name: NADPH; Nitroglycerin; H+

assay_conditions_summary: cofactor NADPH

substrate: NADPH; Nitroglycerin; H+


column_label: Official ScienceDirect full-text Table 1, 2,4,6-Trinitrotoluene GST-YqjM row: kcat 0.53 s^-1; KM 123 microM; kcat/KM 0.0043 microM^-1 s^-1.

normalized_value_unit_evidence: 2,4,6-Trinitrotoluene/GST: kcat normalized_value=0.53 normalized_unit=s^-1; KM normalized_value=0.123 normalized_unit=mM; kcat/KM normalized_value=4.3 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: 2,4,6-Trinitrotoluene/GST: kcat raw_value=0.53 raw_unit=s^-1; KM raw_value=123 raw_unit=microM; kcat/KM raw_value=0.0043 raw_unit=microM^-1*s^-1.

row_label: 2,4,6-Trinitrotoluene; GST-YqjM

table_label: Table 1. Steady state kinetic properties of B. subtilis YqjM


column_label: Official ScienceDirect full-text Table 1, trans-Hex-2-enal GST-YqjM row: kcat 1.17 s^-1; KM 1853 microM; kcat/KM 0.00063 microM^-1 s^-1.

normalized_value_unit_evidence: trans-Hex-2-enal/GST: kcat normalized_value=1.17 normalized_unit=s^-1; KM normalized_value=1.853 normalized_unit=mM; kcat/KM normalized_value=0.63 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: trans-Hex-2-enal/GST: kcat raw_value=1.17 raw_unit=s^-1; KM raw_value=1853 raw_unit=microM; kcat/KM raw_value=0.00063 raw_unit=microM^-1*s^-1.

row_label: trans-Hex-2-enal; GST-YqjM


column_label: Official ScienceDirect full-text Table 1, Cyclohex-2-enone GST-YqjM row: kcat 1.20 s^-1; KM 186 microM; kcat/KM 0.0065 microM^-1 s^-1.

normalized_value_unit_evidence: Cyclohex-2-enone/GST: kcat normalized_value=1.20 normalized_unit=s^-1; KM normalized_value=0.186 normalized_unit=mM; kcat/KM normalized_value=6.5 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Cyclohex-2-enone/GST: kcat raw_value=1.20 raw_unit=s^-1; KM raw_value=186 raw_unit=microM; kcat/KM raw_value=0.0065 raw_unit=microM^-1*s^-1.

row_label: Cyclohex-2-enone; GST-YqjM


column_label: Official ScienceDirect full-text Table 1, Nitroglycerin GST-YqjM row: kcat 0.82 s^-1; KM 45.4 microM; kcat/KM 0.0181 microM^-1 s^-1.

normalized_value_unit_evidence: Nitroglycerin/GST: kcat normalized_value=0.82 normalized_unit=s^-1; KM normalized_value=0.0454 normalized_unit=mM; kcat/KM normalized_value=18.1 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Nitroglycerin/GST: kcat raw_value=0.82 raw_unit=s^-1; KM raw_value=45.4 raw_unit=microM; kcat/KM raw_value=0.0181 raw_unit=microM^-1*s^-1.

row_label: Nitroglycerin; GST-YqjM


enzyme_display_name: UniProt P49050

organism: Ogataea angusta

enzyme: UniProt P49050


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: duroquinone (for cupric reductase activity)

assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Metric label Km; Fig. 4B duroquinone concentration dependence; row duroquinone; value 32 +/- 6 microM

raw_value_unit_evidence: duroquinone 32 +/- 6 microM

row_label: Duroquinone concentration curve (Fig. 4B)

table_label: PDF page 146; Characterization of the Cupric Reductase Activity of NDH-2 / Fig. 4 prose


substrate_name: Cu(2+) (in the presence of FAD)

assay_conditions_summary: cofactor FAD

column_label: Metric label Km; row free Cu(II); condition saturating FAD; value 22 +/- 2 pM

raw_value_unit_evidence: free Cu(II) 22 +/- 2 pM

row_label: Free Cu(II) in presence of saturating FAD

table_label: Abstract

substrate: Cu(2+) (in the presence of FAD)


substrate_name: FAD (for cupric reductase activity)

column_label: Metric label Km; Fig. 4A FAD concentration dependence; row FAD; value 102 +/- 18 microM

raw_value_unit_evidence: FAD 102 +/- 18 microM

row_label: FAD concentration curve (Fig. 4A)

substrate: FAD (for cupric reductase activity)


enzyme_display_name: NADPH:quinone oxidoreductase MdaB

enzyme: NADPH:quinone oxidoreductase MdaB


organism: Sus scrofa


assay_conditions_summary: pH 7.2; cofactor NADPH


enzyme_display_name: nitrate reductase (NADH)

substrate_name: nitrate

assay_conditions_summary: pH 7; 295.15 K; cofactor NADH

enzyme: nitrate reductase (NADH)

substrate: nitrate


column_label: Table 1, row Q1, column Km (apparent, microM): 5.9.

normalized_value_unit_evidence: apparent Km = 0.0059 mM.

raw_value_unit_evidence: Table 1 Q1 row: apparent Km = 5.9 microM.

table_label: Table 1: Kinetic parameters for NDH-2 with different substrates


column_label: Table 1, row Q2, column Km (apparent, microM): 2.3.

normalized_value_unit_evidence: apparent Km = 0.0023 mM.

raw_value_unit_evidence: Table 1 Q2 row: apparent Km = 2.3 microM.


substrate_name: idebenone

column_label: Table 1, row Idebenone, column Km (apparent, microM): 1.8.

normalized_value_unit_evidence: apparent Km = 0.0018 mM.

raw_value_unit_evidence: Table 1 Idebenone row: apparent Km = 1.8 microM.

row_label: Idebenone

substrate: idebenone


enzyme_display_name: NADPH dehydrogenase 3

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: cyclohexenone

enzyme: NADPH dehydrogenase 3

substrate: cyclohexenone


proof_lines: A New Old Yellow Enzyme of Saccharomyces cerevisiae


enzyme_display_name: NADPH dehydrogenase 2

enzyme: NADPH dehydrogenase 2


substrate_name: oxygen

smiles: O=O

substrate: oxygen


organism: Cucurbita pepo

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: menadione

substrate: menadione


organism: Rhodobacter capsulatus

proof_lines: reaction with 2,6-dichlorophenol indophenol


proof_lines:
reaction with NADH
reaction with methyl viologen
reaction with bromophenol blue


substrate_name: reduced bromophenol blue

substrate: reduced bromophenol blue


substrate_name: reduced methyl viologen

substrate: reduced methyl viologen


organism: Auxenochlorella pyrenoidosa

substrate_name: FAD

substrate: FAD


enzyme_display_name: Nitrate reductase [NAD(P)H]

organism: Chlorella variegata

enzyme: Nitrate reductase [NAD(P)H]


substrate_name: NADPH

substrate: NADPH


proof_lines:
cofactor NADH
cosubstrate NADPH


organism: [Candida] nitratophila


proof_lines:
cosubstrate NADPH
cofactor NADH


organism: Pyropia yezoensis


enzyme_display_name: NADPH dehydrogenase 1

organism: Saccharomyces pastorianus

substrate_name: alpha-NADPH

enzyme: NADPH dehydrogenase 1

substrate: alpha-NADPH


substrate_name: oxygen (with alpha-NADPH a substrate)

substrate: oxygen (with alpha-NADPH a substrate)


enzyme_display_name: nitrite reductase [NAD(P)H]

organism: Azotobacter chroococcum

enzyme: nitrite reductase [NAD(P)H]


substrate_name: Unknown

substrate: Unknown


organism: Derxia gummosa


proof_lines:
+ NO2-
+ hydroxylamine


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


organism: Thalassiosira pseudonana


organism: Wickerhamomyces anomalus


substrate_name: nitrite

substrate: nitrite


organism: Chlorolobion braunii


enzyme_display_name: nitrate reductase (NADPH)

enzyme: nitrate reductase (NADPH)


substrate_name: ferricyanide

substrate: ferricyanide


proof_lines: as a protector of NADH-cytochrome c reductase activity


organism: Rhodotorula glutinis


proof_lines:
cosubstrate NADPH
apparent KM


organism: Funaria hygrometrica


organism: Skeletonema costatum


organism: Priestia megaterium


organism: Cucurbita maxima


organism: Neurospora crassa


organism: Spinacia oleracea

proof_lines: recombinant flavin domain of nitrate reductase C240A mutant


proof_lines: recombinant flavin domain of nitrate reductase C240G mutant


proof_lines: wild-type recombinant flavin domain of nitrate reductase


proof_lines: recombinant flavin domain of nitrate reductase C240S mutant


proof_lines: recombinant flavin domain of nitrate reductase C17S mutant


proof_lines: recombinant flavin domain of nitrate reductase C54S mutant


proof_lines: recombinant flavin domain of nitrate reductase C62S mutant


organism: Cucurbita sp.

substrate_name: Bromophenol blue

column_label: PMID 16665101 abstract and Results prose: apparent Km for bromphenol blue = 60 micromolar at 10 mM nitrate.

raw_value_unit_evidence: The abstract reports apparent Km values of 60 micromolar for bromphenol blue at 10 millimolar nitrate. Results prose reports 60 uM bromphenol blue and Vmax = 5.6 unit/ml.

row_label: Squash NADH:nitrate reductase with bromphenol blue electron donor

table_label: Abstract and Results prose, kinetic properties of squash NR electron donors

substrate: Bromophenol blue


assay_conditions_summary: pH 7; cofactor NADH

proof_lines: pH 7.0, 25°C, functional FAD-containing domain domain plus heme-containig domain


assay_conditions_summary: pH 7; cofactor FAD

proof_lines: pH 7.0, 25°C, functional FAD-containing domain


proof_lines:
cosubstrate NADPH or NADH
+ dithionite


substrate_name: nitrate

assay_conditions_summary: pH 7.6; buffer 5 mM phosphate

proof_lines: GST-tagged molybdenum domain, 25°C, pH 7.6

proof_lines: His-tagged molybdenum domain, 25°C, pH 7.6

substrate: nitrate


substrate_name: ferricytochrome c

assay_conditions_summary: pH 7; 298.15 K; cofactor FAD

proof_lines: pH 7.0, 25°C, functional FAD-containing domain plus heme-containig domain

substrate: ferricytochrome c


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C240S with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C240G with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C240A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature C62S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


proof_lines: recombinant flavin domain of nitrate reductase wild-type and C17S mutant


sequence_variant_note: Mutation signature C54S could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Nitrate reductase [NADH]

organism: Ulva prolifera

proof_lines: kcat is 4900 sec(-1) for NADH in the ferricyanide reduction by the FAD-binding domain (at ph 7.0 and 25 degrees Celsius).

enzyme: Nitrate reductase [NADH]


organism: Chlorella sp.

substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines:
NDC1
demethylphylloquinone
vitamin K1


organism: Synechocystis sp.


enzyme_display_name: External alternative NADH-ubiquinone oxidoreductase, mitochondrial

organism: Yarrowia lipolytica (strain CLIB 122 / E 150)

proof_lines: external alternative NADH:ubiquinone oxidoreductase


enzyme_display_name: NADPH dehydrogenase (quinone)

organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

enzyme: NADPH dehydrogenase (quinone)


substrate_name: FMN

substrate: FMN


enzyme_display_name: Type II NADH:quinone oxidoreductase

organism: Escherichia coli (strain K12)

substrate_name: NADH (for NADH:quinone oxidoreductase activity)

enzyme: Type II NADH:quinone oxidoreductase


organism: Homo sapiens

substrate_name: NADPH (with homotetramer)

substrate: NADPH (with homotetramer)


assay_conditions_summary: pH 7.4; buffer potassium phosphate; cofactor NADPH

column_label: Table 1 row 9,10-PQ lists Km 1.6 uM.

raw_value_unit_evidence: Km raw_value=1.6 raw_unit=uM

table_label: Table 1. Apparent kinetic constants for quinones.


substrate_name: 1,4-benzoquinone (with homotetramer)

column_label: Table 1 row 1,4-BQ lists Km 1.9 uM.

raw_value_unit_evidence: Km raw_value=1.9 raw_unit=uM

substrate: 1,4-benzoquinone (with homotetramer)


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6

proof_lines: mutant W63F, pH 6, temperature not specified in the publication


proof_lines: mutant M485E, pH 6, temperature not specified in the publication


proof_lines: mutant I459W, pH 6, temperature not specified in the publication


enzyme_display_name: UniProt P41407

organism: Escherichia coli

enzyme: UniProt P41407


enzyme_display_name: UniProt Q831B2

organism: Enterococcus faecalis

substrate_name: Methyl red

enzyme: UniProt Q831B2

substrate: Methyl red


enzyme_display_name: UniProt Q9I5F3

assay_conditions_summary: pH 8

enzyme: UniProt Q9I5F3


substrate_name: balsalazide

substrate: balsalazide


substrate_name: NADH

substrate: NADH


enzyme_display_name: UniProt C0STY1

organism: Bacillus sp. B29

enzyme: UniProt C0STY1


enzyme_display_name: azobenzene reductase

organism: Shewanella oneidensis

enzyme: azobenzene reductase


enzyme_display_name: UniProt P36959

substrate_name: GMP

enzyme: UniProt P36959

substrate: GMP


enzyme_display_name: UniProt Q9P2T1

proof_lines:
Raw SKiD Env: Temp=35°C, pH=8
Raw SKiD Env: Temp=25°C, pH=7.8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q9P2T1


substrate_name: NADPH

substrate: NADPH


substrate_name: NADP+

substrate: NADP+


substrate_name: dGMP

substrate: dGMP


substrate_name: IMP

substrate: IMP


substrate_name: dIMP

substrate: dIMP


proof_lines:
Raw SKiD Env: Temp=35°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.8


enzyme_display_name: NADPH:quinone reductase

enzyme: NADPH:quinone reductase


substrate_name: 9,10-anthraquinone-2-sulfonic acid

substrate: 9,10-anthraquinone-2-sulfonic acid


substrate_name: riboflavin

substrate: riboflavin


enzyme_display_name: cytochrome-b5 reductase

organism: Rattus norvegicus

substrate_name: ferricytochrome b5

enzyme: cytochrome-b5 reductase

substrate: ferricytochrome b5


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

proof_lines:
recombinant wild-type enzyme
pH 7.0, wild type enzyme
wild-type, pH 7.0


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


assay_conditions_summary: pH 6; cofactor NADH

column_label: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row Wild type; column Km (uM); cell 22.7 ± 1.0.

normalized_value_unit_evidence: Km normalized_value=0.0227 normalized_unit=mM from Table 2 Km uM / 1000.

raw_value_unit_evidence: Table 2 row Wild type: Km 22.7 ± 1.0 uM; Vmax 1060 ± 6.1 umol/min/mg.

row_label: Wild type / ubiquinone-1

table_label: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R479K to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.00937 normalized_unit=mM; unit conversion from 9.37 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row R479K; column Km (uM); raw value 9.37 +/- 0.48 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R479A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0115 normalized_unit=mM; unit conversion from 11.5 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row R479A; column Km (uM); raw value 11.5 +/- 0.58 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L487A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0164 normalized_unit=mM; unit conversion from 16.4 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row L487A; column Km (uM); raw value 16.4 +/- 2.2 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L447N to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0179 normalized_unit=mM; unit conversion from 17.9 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row L447N; column Km (uM); raw value 17.9 +/- 1.8 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M485A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0186 normalized_unit=mM; unit conversion from 18.6 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row M485A; column Km (uM); raw value 18.6 +/- 1.1 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y482F to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0233 normalized_unit=mM; unit conversion from 23.3 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row Y482F; column Km (uM); raw value 23.3 +/- 2.0 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R479H to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0235 normalized_unit=mM; unit conversion from 23.5 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row R479H; column Km (uM); raw value 23.5 +/- 1.4 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L444N to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0239 normalized_unit=mM; unit conversion from 23.9 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row L444N; column Km (uM); raw value 23.9 +/- 2.0 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q394A to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0245 normalized_unit=mM; unit conversion from 24.5 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row Q394A; column Km (uM); raw value 24.5 +/- 1.7 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S484F to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row S484F; column Km (uM); raw value 24.5 +/- 3.9 uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S484I to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.025 normalized_unit=mM; unit conversion from 25.0 uM

raw_value_unit_evidence: Table 2. Kinetic parameters of the oxidoreductase activity of wild-type and mutant Ndi1 for ubiquinone-1; row S484I; column Km (uM); raw value 25.0 +/- 1.7 uM