| pubmed-article:18566346 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18566346 | lifeskim:mentions | umls-concept:C0319878 | lld:lifeskim |
| pubmed-article:18566346 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:18566346 | lifeskim:mentions | umls-concept:C1413154 | lld:lifeskim |
| pubmed-article:18566346 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:18566346 | pubmed:dateCreated | 2008-7-31 | lld:pubmed |
| pubmed-article:18566346 | pubmed:abstractText | A novel short-chain (S)-1-phenyl-1,2-ethanediol dehydrogenase (SCR) from Candida parapsilosis exhibits coenzyme specificity for NADPH over NADH. It catalyzes an anti-Prelog type reaction to reduce 2-hydroxyacetophenone into (S)-1-phenyl-1,2-ethanediol. The coding gene was overexpressed in Escherichia coli and the purified protein was crystallized. The crystal structure of the apo-form was solved to 2.7 A resolution. This protein forms a homo-tetramer with a broken 2-2-2 symmetry. The overall fold of each SCR subunit is similar to that of the known structures of other homologous alcohol dehydrogenases, although the latter usually form tetramers with perfect 2-2-2 symmetries. Additionally, in the apo-SCR structure, the entrance of the NADPH pocket is blocked by a surface loop. In order to understand the structure-function relationship of SCR, we carried out a number of mutagenesis-enzymatic analyses based on the new structural information. First, mutations of the putative catalytic Ser-Tyr-Lys triad confirmed their functional role. Second, truncation of an N-terminal 31-residue peptide indicated its role in oligomerization, but not in catalytic activity. Similarly, a V270D point mutation rendered the SCR as a dimer, rather than a tetramer, without affecting the enzymatic activity. Moreover, the S67D/H68D double-point mutation inside the coenzyme-binding pocket resulted in a nearly 10-fold increase and a 20-fold decrease in the k(cat) /K(M) value when NADH and NADPH were used as cofactors, respectively, with k(cat) remaining essentially the same. This latter result provides a new example of a protein engineering approach to modify the coenzyme specificity in SCR and short-chain dehydrogenases/reductases in general. | lld:pubmed |
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| pubmed-article:18566346 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18566346 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18566346 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18566346 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18566346 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18566346 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18566346 | pubmed:issn | 1469-896X | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:KlosIu SIuS | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:BartlamMarkM | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:RaoZiheZ | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:ZhangRongzhen... | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:LiXuemeiX | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:ZhuGuangyuG | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:ZhangXuejun... | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:CaoShengS | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:OuXianjinX | lld:pubmed |
| pubmed-article:18566346 | pubmed:author | pubmed-author:ZhangWenchiW | lld:pubmed |
| pubmed-article:18566346 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18566346 | pubmed:volume | 17 | lld:pubmed |
| pubmed-article:18566346 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18566346 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18566346 | pubmed:pagination | 1412-23 | lld:pubmed |
| pubmed-article:18566346 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:18566346 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18566346 | pubmed:articleTitle | Crystal structure of a carbonyl reductase from Candida parapsilosis with anti-Prelog stereospecificity. | lld:pubmed |
| pubmed-article:18566346 | pubmed:affiliation | Key Laboratory of Industrial Biotechnology of Ministry of Education and School of Biotechnology, Jiangnan University, Wuxi 214122, People's Republic of China. | lld:pubmed |
| pubmed-article:18566346 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18566346 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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