| pubmed-article:18323628 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0445819 | lld:lifeskim |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0031453 | lld:lifeskim |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0233820 | lld:lifeskim |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0051581 | lld:lifeskim |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0439855 | lld:lifeskim |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:18323628 | lifeskim:mentions | umls-concept:C0125072 | lld:lifeskim |
| pubmed-article:18323628 | pubmed:issue | Pt 3 | lld:pubmed |
| pubmed-article:18323628 | pubmed:dateCreated | 2008-3-7 | lld:pubmed |
| pubmed-article:18323628 | pubmed:abstractText | The crystal structures of D-amino-acid amidase (DAA) from Ochrobactrum anthropi SV3 in complex with L-phenylalanine and with L-phenylalanine amide were determined at 2.3 and 2.2 A resolution, respectively. Comparison of the L-phenylalanine amide complex with the D-phenylalanine complex reveals that the D-stereospecificity of DAA might be achieved as a consequence of three structural factors: (i) the hydrophobic cavity in the region in which the hydrophobic side chain of the substrate is held, (ii) the spatial arrangement of Gln310 O and Glu114 O epsilon2 that fixes the amino N atom of the substrate and (iii) the existence of two cavities that keep the carboxyl/amide group of the substrate near or apart from Ser60 O gamma. | lld:pubmed |
| pubmed-article:18323628 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18323628 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18323628 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18323628 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18323628 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18323628 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18323628 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18323628 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18323628 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:18323628 | pubmed:issn | 0907-4449 | lld:pubmed |
| pubmed-article:18323628 | pubmed:author | pubmed-author:AsanoYasuhisa... | lld:pubmed |
| pubmed-article:18323628 | pubmed:author | pubmed-author:MizushimaTsun... | lld:pubmed |
| pubmed-article:18323628 | pubmed:author | pubmed-author:YamaneTakashi... | lld:pubmed |
| pubmed-article:18323628 | pubmed:author | pubmed-author:SuzukiAtsuoA | lld:pubmed |
| pubmed-article:18323628 | pubmed:author | pubmed-author:KomedaHidenob... | lld:pubmed |
| pubmed-article:18323628 | pubmed:author | pubmed-author:OkazakiSeijiS | lld:pubmed |
| pubmed-article:18323628 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18323628 | pubmed:volume | 64 | lld:pubmed |
| pubmed-article:18323628 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18323628 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18323628 | pubmed:pagination | 331-4 | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:meshHeading | pubmed-meshheading:18323628... | lld:pubmed |
| pubmed-article:18323628 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18323628 | pubmed:articleTitle | Structures of D-amino-acid amidase complexed with L-phenylalanine and with L-phenylalanine amide: insight into the D-stereospecificity of D-amino-acid amidase from Ochrobactrum anthropi SV3. | lld:pubmed |
| pubmed-article:18323628 | pubmed:affiliation | Department of Biotechnology, School of Engineering, Nagoya University, Chikusa, Nagoya 464-8603, Japan. | lld:pubmed |
| pubmed-article:18323628 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18323628 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:18323628 | lld:pubmed |
