Open AccessMethionine Metabolism and Cephalosporin C Synthesis in Cephalosporium acremonium d ‐Amino Acid Oxidase
Author(s) -
Benz F.,
Liersch M.,
Nüuesch J.,
Treichler H. J.
Publication year - 1971
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1971.tb01365.x
Subject(s) - norleucine , cephalosporin c , biochemistry , acremonium , norvaline , amino acid , enzyme , methionine , biosynthesis , oxidase test , isoleucine , chemistry , phenylalanine , leucine , biology , stereochemistry , cephalosporin , antibiotics , botany
The d ‐amino acid oxidase was produced during the growth cycle of Cephalosporium acremo‐nium in submerged culture. The enzyme is strictly sterospecific for d ‐amino acids as substrates. It was isolated from the mycelial crude extract and purified 18‐fold. A relatively small number of d ‐monoamino acids were deaminated. With d ‐methionine as substrate the enzyme had a pH optimum of 8.5 and it was competitively inhibited by the d ‐stereoisomers of norleucine, norvaline, leucine, isoleucine, phenylalanine and lysine. The properties of the C. Acremonium enzyme are compared with those of other fungi and mammalian d ‐amino acid oxidases. Its possible influence on the biosynthesis of the antibiotic Cephalosporin C is discussed.