Abstract
Twenty one chromogenic thiopeptolide substrates were designed and synthesized as the active site probes and analyzed with each S1 site of mutant residues and enzymes of wild-type MetAP1s. The preliminary enzymatic experiments indicate that cysteine 70 or 202, at either Escherichia coli or human MetAP1, played a crucial role in the methionine hydrolysis.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Aminopeptidases / chemistry*
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Aminopeptidases / genetics
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Aminopeptidases / metabolism*
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Animals
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Binding Sites
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Chromogenic Compounds / chemical synthesis*
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Chromogenic Compounds / chemistry
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Chromogenic Compounds / metabolism*
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Cyclosporins / chemical synthesis
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Cyclosporins / chemistry
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Cyclosporins / metabolism
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Escherichia coli / enzymology
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Humans
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Hydrolysis
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Methionine / metabolism*
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Methionyl Aminopeptidases
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Molecular Sequence Data
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Oligopeptides / chemical synthesis*
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Oligopeptides / chemistry
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Oligopeptides / metabolism*
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Point Mutation
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Sulfhydryl Compounds / analysis
Substances
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Chromogenic Compounds
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Cyclosporins
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Oligopeptides
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Sulfhydryl Compounds
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Methionine
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Aminopeptidases
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Methionyl Aminopeptidases