Abstract
The nucleotide sequence of the yeast pyruvate carboxylase gene has been determined from a cloned fragment of yeast genomic DNA. The deduced translation product codes for a polypeptide of 1178 amino acids, having a calculated molecular weight of 130,100. The protein shows strong sequence homology to specific regions of other biotin carboxylases, lipoamide transferases, and carbamyl phosphate synthetases. The homologous regions suggest the presence of three subsites in the enzyme: a biotin attachment site, a keto acid-binding site, and an ATP-binding site. Partial proteolysis with a variety of proteases under nondenaturing conditions indicates the presence of structural domains corresponding to these subsites.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Adenosine Triphosphate / metabolism
-
Amino Acid Sequence
-
Base Sequence
-
Binding Sites
-
Carboxyl and Carbamoyl Transferases*
-
Escherichia coli / enzymology
-
Molecular Sequence Data
-
Pyruvate Carboxylase / analysis*
-
Pyruvate Carboxylase / genetics
-
Pyruvate Carboxylase / metabolism
-
Pyruvate Dehydrogenase Complex / analysis
-
Pyruvates / metabolism
-
Pyruvic Acid
-
Saccharomyces cerevisiae / enzymology*
-
Transferases / analysis
Substances
-
Pyruvate Dehydrogenase Complex
-
Pyruvates
-
Pyruvic Acid
-
Adenosine Triphosphate
-
Transferases
-
Carboxyl and Carbamoyl Transferases
-
Methylmalonyl-CoA carboxytransferase
-
Pyruvate Carboxylase
Associated data
-
GENBANK/J03889
-
GENBANK/M16595