Amino acid sequences of phosphoenolpyruvate carboxylases of Escherichiacoli (allosteric) and a cyanobacterium Anacystisnidulans (non-allosteric) were aligned. The pattern of homology suggests that the enzyme molecule is comprised of two distinct regions, namely, a conserved region (C-terminal half) and a variable region (N-terminal half). Among the amino acid residues which have previously been presumed essential for the catalytic activity, three histidine residues were found to be conserved, but cysteine residues were not. Furthermore, the conserved sequence unique to the enzyme was identified by comparison of the enzyme sequence with amino acid sequences in our data bank.
|Original language||English (US)|
|Number of pages||6|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Dec 17 1985|
Bibliographical noteFunding Information:
The authors wish to express their gratitude to Dr. N. Fujita, National Institute of Genetics (present address), for the computer program of hydropathy profile, to Mr. M. Kuriyama and Mr. K. Hirai for preliminary characterization of phosphoenolpyruvate carboxylase of A. nidulans. This work was supported in parts by research grants from the Ministry of Education, Science and Culture of Japan, the Nissan Science Foundation and Sumitomo Chemical Co., Ltd.