C-Terminal Regions of D-Hydantoinases Are Nonessential for Catalysis, but Affect the Oligomeric Structure

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Most microbial D-hydantoinases have been reported to have catalytic properties similar to those of mammalian dihydropyrimidinases. Comparison of the primary structures of microbial D-hydantoinases with mammalian dihydropyrimidinases revealed that the amino acid homology is about 37% and functionally important residues are rigidly conserved at identical positions. Interestingly, however, the C-terminal regions mere found to be completely mismatched with each other. In order to investigate the possible role of the C-terminal regions, we deleted the C-terminal regions of the D-hydantoinases from two thermophilic Bacilli and compared the catalytic and structural properties of the mutant enzymes with those of wildtype enzymes. As a result, the C-terminal region was found not to be essential for catalysis, but it does affect the oligomeric structure of the enzyme. (C) 1998 Academic Press.
Publisher
Academic Press Inc Elsevier Science
Issue Date
1998-01
Language
English
Article Type
Article
Keywords

AMINO-ACIDS; MICROBIAL TRANSFORMATION; MICROORGANISMS; PURIFICATION; CLONING; ENZYME; GENE; DIHYDROPYRIMIDINASE; AMIDOHYDROLASE; EXPRESSION

Citation

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.243, no.1, pp.96 - 100

ISSN
0006-291X
URI
http://hdl.handle.net/10203/68330
Appears in Collection
BS-Journal Papers(저널논문)
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