Source:http://linkedlifedata.com/resource/pubmed/id/20977999
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
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| pubmed:dateCreated |
2010-11-12
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| pubmed:abstractText |
Pseudomonas stutzeri l-rhamnose isomerase (l-RhI) is capable of catalyzing the isomerization between various aldoses and ketoses, showing high catalytic activity with broad substrate-specificity compared with Escherichia coli l-RhI. In a previous study, the crystal structure of P. stutzeri l-RhI revealed an active site comparable with that of E. coli l-RhI and d-xylose isomerases (d-XIs) with structurally conserved amino acids, but also with a different residue seemingly responsible for the specificity of P. stutzeri l-RhI, though the residue itself does not interact with the bound substrate. This residue, Ser329, corresponds to Phe336 in E. coli l-RhI and Lys294 in Actinoplanes missouriensis d-XI. To elucidate the role of Ser329 in P. stutzeri l-RhI, we constructed mutants, S329F (E. coli l-RhI type), S329K (A. missouriensis d-XI type), S329L and S329A. Analyses of the catalytic activity and crystal structure of the mutants revealed a hydroxyl group of Ser329 to be crucial for catalytic activity via interaction with a water molecule. In addition, in complexes with substrate, the mutants S329F and S329L exhibited significant electron density in the C-terminal region not observed in the wild-type P. stutzeri l-RhI. The C-terminal region of P. stutzeri l-RhI has flexibility and shows a flip-flop movement at the inter-molecular surface of the dimeric form.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Aldose-Ketose Isomerases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Hexoses,
http://linkedlifedata.com/resource/pubmed/chemical/L-rhamnose isomerase,
http://linkedlifedata.com/resource/pubmed/chemical/Serine
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
1741-0134
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| pubmed:author | |
| pubmed:issnType |
Electronic
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| pubmed:volume |
23
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
919-27
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| pubmed:dateRevised |
2011-11-17
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| pubmed:meshHeading |
pubmed-meshheading:20977999-Aldose-Ketose Isomerases,
pubmed-meshheading:20977999-Amino Acid Sequence,
pubmed-meshheading:20977999-Bacterial Proteins,
pubmed-meshheading:20977999-Biocatalysis,
pubmed-meshheading:20977999-Catalytic Domain,
pubmed-meshheading:20977999-Escherichia coli,
pubmed-meshheading:20977999-Hexoses,
pubmed-meshheading:20977999-Molecular Sequence Annotation,
pubmed-meshheading:20977999-Molecular Sequence Data,
pubmed-meshheading:20977999-Mutagenesis, Site-Directed,
pubmed-meshheading:20977999-Mutation,
pubmed-meshheading:20977999-Protein Structure, Tertiary,
pubmed-meshheading:20977999-Pseudomonas stutzeri,
pubmed-meshheading:20977999-Sequence Analysis, Protein,
pubmed-meshheading:20977999-Sequence Homology, Amino Acid,
pubmed-meshheading:20977999-Serine,
pubmed-meshheading:20977999-Structure-Activity Relationship,
pubmed-meshheading:20977999-Substrate Specificity,
pubmed-meshheading:20977999-X-Ray Diffraction
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| pubmed:year |
2010
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| pubmed:articleTitle |
Elucidation of the role of Ser329 and the C-terminal region in the catalytic activity of Pseudomonas stutzeri L-rhamnose isomerase.
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| pubmed:affiliation |
Division of Structural Biology, Life Science Research Center and Faculty of Medicine, Kagawa University, 1750-1 Ikenobe, Miki-cho, Kita-gun, Kagawa 761-0793, Japan.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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