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Literature summary for 1.6.2.4 extracted from

  • Hubbard, P.A.; Xia, C.; Shen, A.L.; Kim, J.P.
    Structural and kinetic investigations of the carboxy terminus of NADPH-cytochrome P450 oxidoreductase (2021), Arch. Biochem. Biophys., 701, 108792 .
    View publication on PubMed
Search for more literature for 1.6.2.4

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of mutant DELTAD675/DELTAV676, the overall protein fold of the mutant structure is the same as the wild-type structure Homo sapiens

Protein Variants

Protein Variants Comment Organism
DELTAD675/DELTAV676 tandem deletion variant, about 16% of wild-type activity Homo sapiens
DELTAS678 deletion of Ser678 has no effect on cytochrome c reductase activity or Km values for NADPH or cytochrome c Homo sapiens
DELTAV676 repositioning of Trp677 by deletion of Val676 decreases cytochrome c reductase activity, to about 6% of wild-type levels Homo sapiens
W677A substitution of Trp677 decreases NADPH-dependent cytochrome c reductase activity 25- to 55fold. W677A substitution abolishes the decrease in cytochrome c reductase activity at low pH Homo sapiens
W677G substitution of Trp677 decreases NADPH-dependent cytochrome c reductase activity 25- to 55fold. W677G substitution exhibits only a slight decrease in activity at low pH Homo sapiens
W677G/S678X W677G/S678X substitution exhibits only a slight decrease in activity at low pH Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
2'-AMP competitive Homo sapiens
5'-ADP competitive Homo sapiens
NAD+ competitive Homo sapiens
NADP+ competitive Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P16435
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