Accession Number:

AD0415464

Title:

THE ENZYMATIC DEGRADATION OF TERPENES.

Descriptive Note:

Final technical rept.,

Corporate Author:

MAX-PLANCK-INSTITUT FUER ZELLCHEMIE MUNICH (WEST GERMANY)

Report Date:

1962-12-14

Pagination or Media Count:

3.0

Abstract:

Pyruvate carboxylase employed in these studies has been purified 550 times from crude extracts of Ps. citronellolis. The enzyme catalyzes the ATP and Mg- dependant carboxylation of pyruvate to oxalacetate. Biotin acts as the prosthetic group of the enzyme. By exchange studies with radioactive compounds a CO2 biotin-enzyme has been shown to participate in the carboxylation of pyruvate. In contrast to the mammalian pyruvate carboxylase the enzyme isolated from bacteria catalyzes the above reaction in the absence of acetyl CoA. The implication of this observation regarding possible different carboxylation mechanisms in bacterial and mammalian systems is discussed. Author

Subject Categories:

Distribution Statement:

APPROVED FOR PUBLIC RELEASE