Source:http://linkedlifedata.com/resource/pubmed/id/11239087
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
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| pubmed:dateCreated |
2001-3-12
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| pubmed:abstractText |
To facilitate an understanding of structure-function relationships, chimeric xylanases were constructed by module shuffling between the catalytic domains of the FXYN from Streptomyces olivaceoviridis E-86 and the Cex from Cellulomonas fimi. In the family F/10 xylanases, the modules M4 and M5 relate to substrate binding so that modules M4 and M5 of the FXYN were replaced with those of the Cex and the chimeric enzymes denoted FCF-C4, FCF-C5 and FCF-C4,5 were constructed. The k(cat) value of FCF-C5 for p-nitrophenyl-beta-D-cellobioside was similar to that of the FXYN (2.2 s(-1)); however, the k(cat) value of FCF-C4 for p-nitrophenyl-beta-D-cellobioside was significantly higher (7.0 s(-1)). The loss of the hydrogen bond between E46 and S22 or the presence of the I49W mutation would be expected to change the position of Q88, which plays a pivotal role in discriminating between glucose and xylose, resulting in the increased k(cat) value observed for FCF-C4 acting on p-nitrophenyl-beta-D-cellobioside since module M4 directly interacts with Q88. To investigate the synergistic effects of the different modules, module M10 of the FCF-C4 chimera was replaced with that of the Cex. The effects of replacement of module M4 and M10 were almost additive with regard to the K:(m) and k(cat) values.
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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/Glycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Xylan Endo-1,3-beta-Xylosidase,
http://linkedlifedata.com/resource/pubmed/chemical/Xylosidases,
http://linkedlifedata.com/resource/pubmed/chemical/beta-Glucosidase
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| pubmed:status |
MEDLINE
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| pubmed:month |
Dec
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| pubmed:issn |
0269-2139
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
13
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
873-9
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:11239087-Amino Acid Sequence,
pubmed-meshheading:11239087-Binding Sites,
pubmed-meshheading:11239087-Circular Dichroism,
pubmed-meshheading:11239087-Escherichia coli,
pubmed-meshheading:11239087-Glycosides,
pubmed-meshheading:11239087-Hydrogen Bonding,
pubmed-meshheading:11239087-Kinetics,
pubmed-meshheading:11239087-Models, Molecular,
pubmed-meshheading:11239087-Molecular Sequence Data,
pubmed-meshheading:11239087-Mutagenesis, Site-Directed,
pubmed-meshheading:11239087-Mutation,
pubmed-meshheading:11239087-Protein Structure, Secondary,
pubmed-meshheading:11239087-Protein Structure, Tertiary,
pubmed-meshheading:11239087-Recombinant Fusion Proteins,
pubmed-meshheading:11239087-Sequence Alignment,
pubmed-meshheading:11239087-Streptomyces,
pubmed-meshheading:11239087-Substrate Specificity,
pubmed-meshheading:11239087-Xylan Endo-1,3-beta-Xylosidase,
pubmed-meshheading:11239087-Xylosidases,
pubmed-meshheading:11239087-beta-Glucosidase
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| pubmed:year |
2000
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| pubmed:articleTitle |
Module shuffling of a family F/10 xylanase: replacement of modules M4 and M5 of the FXYN of Streptomyces olivaceoviridis E-86 with those of the Cex of Cellulomonas fimi.
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| pubmed:affiliation |
National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8642, Japan. sakaneko@nfri.affrc.go.jp
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| pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, Non-U.S. Gov't
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