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Literature summary extracted from

  • Kawano, M.; Shirabe, K.; Nagai, T.; Takeshita, M.
    Role of carboxyl residues surrounding heme of human cytochrome b5 in the electrostatic interaction with NADH-cytochrome b5 reductase (1998), Biochem. Biophys. Res. Commun., 245, 666-669.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.6.2.2 expression of wild-type, K41A and K125A mutant enzyme in Escherichia coli Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.6.2.2 K125A 5.3fold elevated Km value for cytochrome b5 Homo sapiens
1.6.2.2 K163A 5.7fold elevated Km value for cytochrome b5 Homo sapiens
1.6.2.2 K41A 6.3fold elevated Km value for cytochrome b5 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.6.2.2 0.0362
-
 cytochrome b5 L125A mutant enzyme Homo sapiens
1.6.2.2 0.042
-
 cytochrome b5 L41A mutant enzyme Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.6.2.2 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.6.2.2 recombinant wild-type, K41A, K125A and K163A mutant enzyme Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.6.2.2 NADH + ferricytochrome b5
-
 Homo sapiens NAD+ + H+ + ferrocytochrome b5
-
 r
1.6.2.2 NADH + ferricytochrome b5
-
 Homo sapiens NAD+ + H+ + 2 ferrocytochrome b5
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.6.2.2 125
-
 ferricytochrome b5 L41A mutant enzyme Homo sapiens
1.6.2.2 472
-
 ferricytochrome b5 L125A mutant enzyme Homo sapiens