[Localization of tetranitromethane-modified tyrosine residues in the polypeptide chain of cholesterol-hydroxylating cytochrome P-450].
As a continuation of earlier structure-function relationship studies on cholesterol-hydroxylating cytochrome P-450 from the adrenal cortex mitochondria, the present study deals with the distribution of tetranitromethane-modified tyrosine residues in the hemeprotein polypeptide chain. Amino acid residues Tyr-24, -46, -50, -93, -94, -199, -246 are shown to be modified with tetranitromethane. Tyr-93, -94 are supposedly involved in the active site formation of cytochrome P-450.
Pikuleva
I A
IA
Lapko
A G
AG
Akhrem
A A
AA
Usanov
S A
SA
Chashchin
V L
VL
D000302:Adrenal Cortex / Q000201:enzymology / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D002417:Cattle; D003577:Cytochrome P-450 Enzyme System / Q000032:analysis* / Q000302:isolation & purification; D006868:Hydrolysis; D008666:Metalloendopeptidases; D008697:Methane / Q000031:analogs & derivatives*; D008928:Mitochondria / Q000201:enzymology / Q000378:metabolism; D010455:Peptides / Q000032:analysis*; D013774:Tetranitromethane / Q000494:pharmacology*; D014443:Tyrosine / Q000032:analysis* / Q000302:isolation & purification
D010455:Peptides; D014443:Tyrosine; D003577:Cytochrome P-450 Enzyme System; D008666:Metalloendopeptidases; C022653:auR protein, Staphylococcus aureus; D013774:Tetranitromethane; D008697:Methane
Lokalizatsiia modifitsirovannykh tetranitrometanom ostatkov tirozina v polipeptidnoĭ tsepi kholesteringidroksiliruiushchego tsitokhroma P-450.