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Literature summary for 1.6.2.2 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
Search for more literature for 1.6.2.2

Cloned(Commentary)

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

Protein Variants

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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