DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kim, G.J. | ko |
dc.contributor.author | Park, J.H. | ko |
dc.contributor.author | Lee, D.C. | ko |
dc.contributor.author | Ro, H.S. | ko |
dc.contributor.author | Kim, Hak-Sung | ko |
dc.date.accessioned | 2013-03-03T06:03:33Z | - |
dc.date.available | 2013-03-03T06:03:33Z | - |
dc.date.created | 2012-02-06 | - |
dc.date.created | 2012-02-06 | - |
dc.date.issued | 1997 | - |
dc.identifier.citation | MOLECULAR & GENERAL GENETICS, v.255, no.2, pp.152 - 156 | - |
dc.identifier.issn | 0026-8925 | - |
dc.identifier.uri | http://hdl.handle.net/10203/77551 | - |
dc.description.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. 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. | - |
dc.language | English | - |
dc.publisher | SPRINGER VERLAG | - |
dc.subject | L-AMINO-ACIDS | - |
dc.subject | 5-SUBSTITUTED HYDANTOINS | - |
dc.subject | CLONING | - |
dc.subject | GENE | - |
dc.subject | MICROORGANISMS | - |
dc.subject | PROTEIN | - |
dc.subject | ENZYME | - |
dc.subject | DNA | - |
dc.title | Primary structure, sequence analysis, and expression of the thermostable D-hydantoinase from Bacillus stearothermophilus SD1 | - |
dc.type | Article | - |
dc.identifier.wosid | A1997XJ09400003 | - |
dc.identifier.scopusid | 2-s2.0-0030871790 | - |
dc.type.rims | ART | - |
dc.citation.volume | 255 | - |
dc.citation.issue | 2 | - |
dc.citation.beginningpage | 152 | - |
dc.citation.endingpage | 156 | - |
dc.citation.publicationname | MOLECULAR & GENERAL GENETICS | - |
dc.identifier.doi | 10.1007/PL00008610 | - |
dc.contributor.localauthor | Kim, Hak-Sung | - |
dc.contributor.nonIdAuthor | Kim, G.J. | - |
dc.contributor.nonIdAuthor | Park, J.H. | - |
dc.contributor.nonIdAuthor | Lee, D.C. | - |
dc.contributor.nonIdAuthor | Ro, H.S. | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordAuthor | D-hydantoinase | - |
dc.subject.keywordAuthor | amidohydrolase | - |
dc.subject.keywordAuthor | Bacillus stearothermophilus SD1 | - |
dc.subject.keywordPlus | L-AMINO-ACIDS | - |
dc.subject.keywordPlus | 5-SUBSTITUTED HYDANTOINS | - |
dc.subject.keywordPlus | CLONING | - |
dc.subject.keywordPlus | GENE | - |
dc.subject.keywordPlus | MICROORGANISMS | - |
dc.subject.keywordPlus | PROTEIN | - |
dc.subject.keywordPlus | ENZYME | - |
dc.subject.keywordPlus | DNA | - |
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