Pyruvate carboxylase in the yeast pyc mutant.

Abstract:

:Pyruvate carboxylase deficiency was previously reported to be the biochemical lesion in a yeast mutant, designated pyc, which cannot utilize ethanol, acetate, pyruvate, aspartate, or oxaloacetate as the sole carbon source [C. Wills and T. Melham (1985) Arch. Biochem. Biophys. 236, 782-791; C. Wills et al. (1986) Arch. Biochem. Biophys. 246, 306-320]. We present evidence here that the level of pyruvate carboxylase activity as well as the native and subunit molecular weights of this enzyme are identical in the mutant and the wild type. In addition we have used immunocytochemical labeling to demonstrate the exclusively cytosolic localization of this enzyme in both the mutant and wild-type yeast.

journal_name

Arch Biochem Biophys

authors

Lim F,Rohde M,Morris CP,Wallace JC

doi

10.1016/0003-9861(87)90343-2

subject

Has Abstract

pub_date

1987-10-01 00:00:00

pages

259-64

issue

1

eissn

0003-9861

issn

1096-0384

pii

0003-9861(87)90343-2

journal_volume

258

pub_type

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