Abstract
TenA catalyzes the hydrolysis of 4-amino-5-aminomethyl-2-methylpyrimidine and participates in the salvage of base-degraded thiamin. Here, we describe mutagenesis of the active site of TenA guided by structures of the enzyme complexed to a substrate analog and to the product. Catalytic roles for each of the active site residues are identified and a mechanism for the reaction is described.
Publication types
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Research Support, N.I.H., Extramural
MeSH terms
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Bacillus subtilis / enzymology*
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Binding Sites
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Catalysis
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Hydrolases / chemistry
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Hydrolases / genetics*
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Hydrolases / isolation & purification
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Hydrolysis
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Models, Molecular
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Molecular Structure
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Mutagenesis, Site-Directed
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Structure-Activity Relationship
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Thiamine / chemistry
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Thiamine / metabolism*
Substances
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Hydrolases
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thiaminase II
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Thiamine