Open AccessPropionyl‐coenzyme A carboxylase of Mycobacterium smegmatis
Author(s) -
HAASE F. Carl,
BEEGEN Helga,
ALLEN S. H. George
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb08078.x
Subject(s) - protein subunit , pyruvate carboxylase , acetyl coa carboxylase , biotin , chemistry , crystallography , cofactor , biochemistry , biology , stereochemistry , enzyme , gene
Propionyl‐CoA carboxylase has been purified to homogeneity and examined in the electron microscope. The native carboxylase presents a profile with a large central subunit to which smaller subunits are attached. The central subunit has two prominent profiles, one circular (100 Å) with a central hole and the other rectangular (70 × 100 Å). The six polypeptides of this subunit appear to be arranged in a cylindrical structure. Six spherical (50 Å) biotin‐containing peripheral subunits are attached in sets of three to the two opposite circular faces of the central subunit. A model of the 18‐S carboxylase is presented.