Comparison of amino acid sequences between phosphoenolpyruvate carboxylases from Escherichiacoli (allosteric) and anacystisnidulans (non-allosteric): Identification of conserved and variable regions

Sumio Ishijima, Fumiaki Katagiri, Tsutomu Kodaki, Katsura Izui, Hirohiko Katsuki, Ken Nishikawa, Hiroshi Nakashima, Tatsuo Ooi

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Abstract

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 languageEnglish (US)
Pages (from-to)436-441
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume133
Issue number2
DOIs
StatePublished - Dec 17 1985

Bibliographical note

Funding 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.

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