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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1997-4-4
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pubmed:abstractText |
We describe here a sub-family of enzymes related both structurally and functionally to N-acetylneuraminate lyase. Two members of this family (N-acetylneuraminate lyase and dihydrodipicolinate synthase) have known three-dimensional structures and we now proceed to show their structural and functional relationship to two further proteins, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase and D-4-deoxy-5-oxoglucarate dehydratase. These enzymes are all thought to involve intermediate Schiff-base formation with their respective substrates. In order to understand the nature of this intermediate, we have determined the three-dimensional structure of N-acetylneuraminate lyase in complex with hydroxypyruvate (a product analogue) and in complex with one of its products (pyruvate). From these structures we deduce the presence of a closely similar Schiff-base forming motif in all members of the N-acetylneuraminate lyase sub-family. A fifth protein, MosA, is also confirmed to be a member of the sub-family although the involvement of an intermediate Schiff-base in its proposed reaction is unclear.
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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 |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Borohydrides,
http://linkedlifedata.com/resource/pubmed/chemical/Carbon-Carbon Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Hydro-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/MosA protein, Rhizobium meliloti,
http://linkedlifedata.com/resource/pubmed/chemical/N-acetylneuraminate lyase,
http://linkedlifedata.com/resource/pubmed/chemical/Oxo-Acid-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyruvates,
http://linkedlifedata.com/resource/pubmed/chemical/dihydrodipicolinate synthase,
http://linkedlifedata.com/resource/pubmed/chemical/hydroxypyruvic acid
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-2836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
381-99
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9047371-Amino Acid Sequence,
pubmed-meshheading:9047371-Bacterial Proteins,
pubmed-meshheading:9047371-Binding Sites,
pubmed-meshheading:9047371-Borohydrides,
pubmed-meshheading:9047371-Carbon-Carbon Lyases,
pubmed-meshheading:9047371-Clostridium perfringens,
pubmed-meshheading:9047371-Conserved Sequence,
pubmed-meshheading:9047371-Enzyme Inhibitors,
pubmed-meshheading:9047371-Escherichia coli,
pubmed-meshheading:9047371-Hydro-Lyases,
pubmed-meshheading:9047371-Models, Molecular,
pubmed-meshheading:9047371-Molecular Sequence Data,
pubmed-meshheading:9047371-Oxo-Acid-Lyases,
pubmed-meshheading:9047371-Protein Conformation,
pubmed-meshheading:9047371-Protein Structure, Tertiary,
pubmed-meshheading:9047371-Pyruvates,
pubmed-meshheading:9047371-Sequence Homology, Amino Acid,
pubmed-meshheading:9047371-Substrate Specificity
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pubmed:year |
1997
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pubmed:articleTitle |
Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
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pubmed:affiliation |
Biomolecular Research Institute, Parkville, Victoria, Australia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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