ADIPOSE PYRUVATE-CARBOXYLASE - AMINO-ACID-SEQUENCE AND DOMAIN-STRUCTURE DEDUCED FROM CDNA SEQUENCING

作者：ZHANG J; XIA WL; BREW K; AHMAD F

来源：Proceedings of the National Academy of Sciences of the United States of America, 1993, 90(5): 1766-1770.

DOI：10.1073/pnas.90.5.1766

• BIOTIN ENZYME
• PRIMARY STRUCTURE
• CATALYTIC SUBSITES

The complete amino acid sequence of 3T3-L1 adipocyte pyruvate carboxylase (PC) [pyruvate:carbon-dioxide ligase (ADP-forming), EC 6.4.1.1] has been deduced from sequencing overlapping cDNA clones obtained from an adipocyte cDNA library constructed in the lambda Zap vector. The encoding mRNA for PC protomer contains 4067 nt, including a 3534-nt coding sequence and noncoding regions of 100 and 433 nt at the 5' and 3' ends, respectively. The biotinylated lysine of the encoded PC protomer (1178 amino acids with a calculated M(r) of apocarboxylase = 129,784) is located 35 residues from the COOH-terminal end and, as in most other biotin enzymes, is in the consensus sequence AMKM. The adipocyte PC is closely similar (53% identity) to the yeast enzyme and contains different segments that are homologous with regions from the biotin carboxylase component of Escherichia coli acetyl-CoA carboxylase, the keto acid-binding subunits of Propionibacterium shermanii oxaloacetate transcarboxylase and Klebsiella pneumoniae oxaloacetate decarboxylase, and to the biotin carboxyl-carrier protein of the bacterial biotin enzymes. In addition to the putative mitochondrial targeting signal, functional domains are readily identifiable in the sequence and are in the following order: biotin carboxylase-carboxyltransferase-biotin carboxyl-carrier protein, as proposed for yeast PC [Lim, F., Morris, C. P., Occhiodoro, F. & Wallace, J. C. (1988) J. Biol. Chem. 263, 11493-11497].

• 出版日期1993-3-1