Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.6.2.2 T66A Km for NADH is not affected, Km for cytochrome b5 is significantly enhanced Sus scrofa
1.6.2.2 T66S Km for NADH is not affected Sus scrofa
1.6.2.2 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.2.2 0.0016
-
ferricyanide pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
1.6.2.2 0.0022
-
ferricyanide pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
1.6.2.2 0.0025
-
ferricyanide pH 7.0, 25°C, wild type enzyme Sus scrofa
1.6.2.2 0.0028
-
NADH pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
1.6.2.2 0.0028
-
NADH pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
1.6.2.2 0.0029
-
NADH pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
1.6.2.2 0.0031
-
NADH pH 7.0, 25°C, wild type enzyme Sus scrofa
1.6.2.2 0.0031
-
ferricyanide pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
1.6.2.2 0.013
-
ferricytochrome b5 pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
1.6.2.2 0.02
-
ferricytochrome b5 pH 7.0, 25°C, wild type enzyme Sus scrofa
1.6.2.2 0.111
-
ferricytochrome b5 pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
1.6.2.2 0.125
-
ferricytochrome b5 pH 7.0, 25°C,T66A mutant enzyme Sus scrofa

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.6.2.2 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

EC Number Organism UniProt Comment Textmining
1.6.2.2 Sus scrofa P83686
-
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.6.2.2 liver
-
Sus scrofa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 2 ferricyanide + NADH
-
Sus scrofa 2 ferrocyanide + NAD+ + H+
-
?
1.6.2.2 2 ferricytochrome b5 + NADH
-
Sus scrofa 2 ferrocytochrome b5 + NAD+ + H+
-
?
1.6.2.2 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]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.2.2 38
-
ferricytochrome b5 pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
1.6.2.2 77
-
ferricyanide pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
1.6.2.2 100
-
NADH pH 7.0, 25°C,T66V mutant enzyme Sus scrofa
1.6.2.2 314
-
ferricytochrome b5 pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
1.6.2.2 684
-
ferricyanide pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
1.6.2.2 705
-
ferricytochrome b5 pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
1.6.2.2 822
-
ferricyanide pH 7.0, 25°C, wild type enzyme Sus scrofa
1.6.2.2 911
-
ferricytochrome b5 pH 7.0, 25°C, wild type enzyme Sus scrofa
1.6.2.2 976
-
ferricyanide pH 7.0, 25°C,T66S mutant enzyme Sus scrofa
1.6.2.2 984
-
NADH pH 7.0, 25°C,T66A mutant enzyme Sus scrofa
1.6.2.2 1100
-
NADH pH 7.0, 25°C, wild type enzyme Sus scrofa
1.6.2.2 1150
-
NADH pH 7.0, 25°C,T66S mutant enzyme Sus scrofa

Cofactor

EC Number Cofactor Comment Organism Structure
1.6.2.2 FAD
-
Sus scrofa
1.6.2.2 NADH
-
Sus scrofa