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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
18
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pubmed:dateCreated |
2009-6-17
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pubmed:abstractText |
The Michaelis complex of the beta-mannosidase Man2A shows distortion to a (1)S(5) conformation adding to the growing body of evidence supporting catalysis through a boat conformation.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
1359-7345
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
14
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2484-6
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pubmed:meshHeading |
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pubmed:year |
2009
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pubmed:articleTitle |
Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis.
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pubmed:affiliation |
Department of Chemistry, The University of York, Heslington, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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