Primary structure, sequence analysis, and expression of the thermostable D-hydantoinase from Bacillus stearothermophilus SD1

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The gene coding for the thermostable D-hydantoinase from the thermophilic bacterium Bacillus stearothermophilus SD1 was cloned and its nucleotide sequence was completely determined. The D-hydantoinase protein showed considerable amino acid sequence homology (20-28%) with other hydantoinases and functionally related allantoinases and dihydroorotases. Strikingly the sequence of the enzyme from B. stearothermophilius SD1 exhibited greater than 89% identity with hydantoinases from thermophilic bacteria, Despite the extremely high amino acid homology among the hydantoinases from thermophiles. the C-terminal regions of the enzymes were completely different in both sequence and predicted secondary structure, implying that the C-terminal region plays an important role in determining the biochemical properties of the enzymes. Alignment of the sequence of the D-hydantoinase from B. stearothermophilus SD1 with those of other functionally related enzymes revealed four conserved regions, and five histidines and an acidic residue were found to be conserved, suggesting a close evolutionary relationship between all these enzymes.
Publisher
SPRINGER VERLAG
Issue Date
1997
Language
English
Article Type
Article
Keywords

L-AMINO-ACIDS; 5-SUBSTITUTED HYDANTOINS; CLONING; GENE; MICROORGANISMS; PROTEIN; ENZYME; DNA

Citation

MOLECULAR & GENERAL GENETICS, v.255, no.2, pp.152 - 156

ISSN
0026-8925
DOI
10.1007/PL00008610
URI
http://hdl.handle.net/10203/77551
Appears in Collection
BS-Journal Papers(저널논문)
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