Primary Structure, sequence analysis, and expression of the thermostable d - hydantoinase from Bacillus stearothermophilus SD1 |
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Authors: | G-J Kim J-H Park D-C Lee H-S Ro and H-S Kim |
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Institution: | (1) Department of Biological Sciences, Korea Advanced Institute of Science and Technology, 373-1, Kusong-dong Yusong-gu, Taejon 305-701, Korea e-mail: hskim@sorak.kaist.ac.kr, KR |
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Abstract: | 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. stearothermophilus 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.
Received: 20 December 1996 / Accepted: 12 March 1997 |
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Keywords: | D-Hydantoinase Amidohydrolase Bacillus stearothermophilus SD1 |
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