Open AccessPeroxisomal and Mitochondrial Carnitine Acetyltransferases in Alkane‐Grown Yeast Candida tropicalis
Author(s) -
UEDA Mitsuyoshi,
TANAKA Atsuo,
FUKUl Saburo
Publication year - 1982
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1982.tb05926.x
Subject(s) - acetyltransferases , biochemistry , yeast , carnitine , peroxisome , acetyltransferase , candida tropicalis , biology , enzyme , acyltransferases , alkane , chemistry , biosynthesis , gene , acetylation , catalysis
Two types of carnitine acetyltransferases (EC 2.3.1.7) were first isolated from a microorganism, alkane‐grown yeast Candidu tropicalis . Carnitine acetyltransferase activity was induced in the alkane‐grown cells, reaching about twenty times higher than that in the glucose‐grown cells. Localization of the enzyme activity was demon‐ strated, at least, in peroxisomes (microbodies), profusely occurred in the alkane‐grown cells. and in mitochondria. Peroxisomal and mitochondrial carnitine acetyltransferases could be separated using the method of DEAE‐ Sephacel column chromatography and both types were found to exist in the alkane‐grown cells of C. tropicalis. Each carnitine acetyltransferase was purified using Sephadex G‐200, Sepharose 6B, DEAE.‐Sephacel and Blue‐ Sepharose CL‐6B. In DEAE‐Sephacel chromatography, peroxisomal carnitine acetyltransferase was eluted below 0.15 M KCI concentration and mitochondrial carnitine acetyltransferase above 0.15 M KCI concentration. Except for the localization, little difference was observed in their kinetic properties, substrate specificity and so on. These two carnitine acetyltransferase preparations were only specific to acetyl and propion I groups, the hubstrate specificity not being so broad as that of carnitine acetyltransferase obtained from maminalian tissues. Roles of these carnitine acetyltransferases in alkane metabolism in yeast are also discussed.