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

被引:25
作者
Kim, GJ [1 ]
Park, JH [1 ]
Lee, DC [1 ]
Ro, HS [1 ]
Kim, HS [1 ]
机构
[1] KOREA ADV INST SCI & TECHNOL,DEPT BIOL SCI,TAEJON 305701,SOUTH KOREA
来源
MOLECULAR & GENERAL GENETICS | 1997年 / 255卷 / 02期
关键词
D-hydantoinase; amidohydrolase; Bacillus stearothermophilus SD1;
D O I
10.1007/s004380050483
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:152 / 156
页数:5
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