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Literature summary for 1.6.2.2 extracted from

  • Kimura, S.; Kawamura, M.; Iyanagi, T.
    Role of Thr(66) in porcine NADH-cytochrome b5 reductase in catalysis and control of the rate-limiting step in electron transfer (2003), J. Biol. Chem., 278, 3580-3589.
    View publication on PubMed
Search for more literature for 1.6.2.2

Cloned(Commentary)

Cloned (Comment) Organism
all mutants expressed in soluble form in Escherichia coli BL21 Sus scrofa

Protein Variants

Protein Variants Comment Organism
T66A Km for NADH is not affected, Km for cytochrome b5 is significantly enhanced Sus scrofa
T66S Km for NADH is not affected Sus scrofa
T66V turnover is reduced to 10% of the native enzyme, Km for NADH is not affected, Km for cytochrome b5 is significantly enhanced Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0016
-
 ferricyanide pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
0.0022
-
 ferricyanide pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
0.0025
-
 ferricyanide pH 7.0, 25°C, wild type enzyme Sus scrofa
0.0028
-
 NADH pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
0.0028
-
 NADH pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
0.0029
-
 NADH pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
0.0031
-
 NADH pH 7.0, 25°C, wild type enzyme Sus scrofa
0.0031
-
 ferricyanide pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
0.013
-
 ferricytochrome b5 pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
0.02
-
 ferricytochrome b5 pH 7.0, 25°C, wild type enzyme Sus scrofa
0.111
-
 ferricytochrome b5 pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
0.125
-
 ferricytochrome b5 pH 7.0, 25°C,T66A mutant enzyme Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 ferricytochrome b5 + NADH Sus scrofa involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Sus scrofa P83686
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzymes from Escherichia coli Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 ferricyanide + NADH
-
 Sus scrofa 2 ferrocyanide + NAD+ + H+
-
 ?
2 ferricytochrome b5 + NADH
-
 Sus scrofa 2 ferrocytochrome b5 + NAD+ + H+
-
 ?
2 ferricytochrome b5 + NADH involved in the synthesis of fatty acids and cholesterol, and in the oxidation of xenobiotics Sus scrofa 2 ferrocytochrome b5 + NAD+ + H+
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
38
-
 ferricytochrome b5 pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
77
-
 ferricyanide pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
100
-
 NADH pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
314
-
 ferricytochrome b5 pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
684
-
 ferricyanide pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
705
-
 ferricytochrome b5 pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
822
-
 ferricyanide pH 7.0, 25°C, wild type enzyme Sus scrofa
911
-
 ferricytochrome b5 pH 7.0, 25°C, wild type enzyme Sus scrofa
976
-
 ferricyanide pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
984
-
 NADH pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
1100
-
 NADH pH 7.0, 25°C, wild type enzyme Sus scrofa
1150
-
 NADH pH 7.0, 25°C,T66S mutant enzyme Sus scrofa

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Sus scrofa
NADH
-
 Sus scrofa