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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4
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pubmed:dateCreated |
1994-10-14
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pubmed:abstractText |
Aminopeptidases specifically cleave the amino-terminal residue from polypeptide chains and are involved in the metabolism of biologically active peptides. The family includes zinc-dependent enzymes possessing either one or two zinc ions per active site. Structural studies providing a detailed view of the metal environment may reveal whether the one-zinc and two-zinc enzymes constitute structurally and mechanistically distinct subclasses, and what role the metal ions play in the catalytic process.
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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 |
Apr
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pubmed:issn |
0969-2126
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
2
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
283-91
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8087555-Aeromonas,
pubmed-meshheading:8087555-Allosteric Site,
pubmed-meshheading:8087555-Aminopeptidases,
pubmed-meshheading:8087555-Animals,
pubmed-meshheading:8087555-Bacterial Proteins,
pubmed-meshheading:8087555-Binding Sites,
pubmed-meshheading:8087555-Cattle,
pubmed-meshheading:8087555-Crystallography, X-Ray,
pubmed-meshheading:8087555-Eye Proteins,
pubmed-meshheading:8087555-Leucyl Aminopeptidase,
pubmed-meshheading:8087555-Models, Molecular,
pubmed-meshheading:8087555-Protein Conformation,
pubmed-meshheading:8087555-Zinc
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pubmed:year |
1994
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pubmed:articleTitle |
Crystal structure of Aeromonas proteolytica aminopeptidase: a prototypical member of the co-catalytic zinc enzyme family.
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pubmed:affiliation |
Laboratoire de Biologie Structurale, Institut de Biologie Moléculaire et Cellulaire, Strasbourg, France.
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pubmed:publicationType |
Journal Article,
Comparative Study
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