Abstract
The structure of shikimate 5-dehydrogenase, the fourth enzyme in the shikimate biosynthesis pathway and a member of a large enzyme family without clear structural peer, reveals a novel topological fold for the substrate binding domain and, through homology modeling, expands the possibilities for antimicrobial and herbicide design.
Publication types
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Comparative Study
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Comment
MeSH terms
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Alcohol Oxidoreductases / chemistry*
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Alcohol Oxidoreductases / genetics
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Amino Acid Sequence
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Binding Sites
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Crystallography, X-Ray
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Databases, Factual
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Escherichia coli / enzymology
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Evolution, Molecular
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Genetic Variation
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Haemophilus influenzae / enzymology
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Ligands
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Micrococcus / enzymology
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Micrococcus / genetics
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Models, Molecular
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NADP / metabolism
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Protein Folding*
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Reproducibility of Results
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Shikimic Acid / metabolism
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Structure-Activity Relationship
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Substrate Specificity
Substances
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Ligands
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Shikimic Acid
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NADP
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Alcohol Oxidoreductases
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Shikimate dehydrogenase