| pubmed-article:19146406 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C1006886 | lld:lifeskim |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C0034263 | lld:lifeskim |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C0034503 | lld:lifeskim |
| pubmed-article:19146406 | lifeskim:mentions | umls-concept:C0102447 | lld:lifeskim |
| pubmed-article:19146406 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:19146406 | pubmed:dateCreated | 2009-2-3 | lld:pubmed |
| pubmed-article:19146406 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:abstractText | Alpha-amino-epsilon-caprolactam (ACL) racemase (ACLR) from Achromobacter obae catalyzes the interconversion of l- and d-ACL. ACLR belongs to the fold-type I group of pyridoxal 5'-phosphate (PLP) dependent enzymes. In this study, the first crystal structures of a fold-type I racemase are solved for the native form and epsilon-caprolactam-complexed form of ACLR at 2.21 and 2.40 A resolution, respectively. Based on the location of epsilon-caprolactam in the complex structure, the substrate-binding site is assigned between Trp49 and Tyr137. The carboxyl group of Asp210 is a reasonable candidate that recognizes the nitrogen atom of a lactam or amide in the substrate. Based on a structural comparison with fold-type III alanine racemase, Tyr137 is potentially the acid/base catalytic residue that is essential for the two-base racemization mechanism. The overall structure of ACLR is similar to that of fold-type I enzymes. A structural comparison with these enzymes explains the different reaction specificities. | lld:pubmed |
| pubmed-article:19146406 | pubmed:language | eng | lld:pubmed |
| pubmed-article:19146406 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:19146406 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:19146406 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:19146406 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:19146406 | pubmed:issn | 1520-4995 | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:AsanoYasuhisa... | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:MizushimaTsun... | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:YamaneTakashi... | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:KawanoTakeshi... | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:SuzukiAtsuoA | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:KomedaHidenob... | lld:pubmed |
| pubmed-article:19146406 | pubmed:author | pubmed-author:OkazakiSeijiS | lld:pubmed |
| pubmed-article:19146406 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:19146406 | pubmed:day | 10 | lld:pubmed |
| pubmed-article:19146406 | pubmed:volume | 48 | lld:pubmed |
| pubmed-article:19146406 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:19146406 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:19146406 | pubmed:pagination | 941-50 | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:meshHeading | pubmed-meshheading:19146406... | lld:pubmed |
| pubmed-article:19146406 | pubmed:year | 2009 | lld:pubmed |
| pubmed-article:19146406 | pubmed:articleTitle | The novel structure of a pyridoxal 5'-phosphate-dependent fold-type I racemase, alpha-amino-epsilon-caprolactam racemase from Achromobacter obae. | lld:pubmed |
| pubmed-article:19146406 | pubmed:affiliation | Department of Biotechnology, Graduate School of Engineering, Nagoya University, Chikusa, Nagoya 464-8603, Japan. | lld:pubmed |
| pubmed-article:19146406 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:19146406 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:19146406 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
