Open AccessACETYL COA CARBOXYLASE, II. DEMONSTRATION OF BIOTIN-PROTEIN AND BIOTIN CARBOXYLASE SUBUNITS
Author(s) -
Alfred W. Alberts,
A M Nervi,
P. Roy Vagelos
Publication year - 1969
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.63.4.1319
Subject(s) - biotin , pyruvate carboxylase , acetyl coa carboxylase , carboxylation , protein subunit , biochemistry , chemistry , enzyme , gene , catalysis
Previous work has shown thatEscherichia coli acetyl CoA carboxylase is composed of two dissimilar protein components, Ea which contains covalently bound biotin and forms Ea -CO2 -from HCO3 - and ATP, and Eb which is involved in the transfer of the carboxyl group from Ea -CO2 - to acetyl CoA, forming malonyl CoA. Ea has been dissociated into two subunits at pH 9. One subunit, designated biotin carboxylase, catalyzes a model reaction, the ATP-dependent carboxylation of free (+)-biotin. The other subunit contains covalently bound which is carboxylated by the biotin carboxylase in the course of acetyl CoA carboxylation.