Abstract
A membrane-bound protein purified from Gluconobacter oxydans M5 was confirmed to be a pyrroloquinoline quinone-dependent D-sorbitol dehydrogenase. Gene disruption and complementation experiments demonstrated that this enzyme is responsible for the oxidation of 1-(2-hydroxyethyl) amino-1-deoxy-D-sorbitol (1NSL) to 6-(2-hydroxyethyl) amino-6-deoxy-L-sorbose (6NSE), which is the precursor of an antidiabetic drug, miglitol.
MeSH terms
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Amino Acid Sequence
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / metabolism*
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Genetic Complementation Test
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Genetic Vectors
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Gluconobacter oxydans / enzymology*
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Gluconobacter oxydans / genetics
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L-Iditol 2-Dehydrogenase / isolation & purification
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L-Iditol 2-Dehydrogenase / metabolism*
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Membrane Proteins / metabolism
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Oxidation-Reduction
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PQQ Cofactor / metabolism*
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Plasmids
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Sorbitol / metabolism
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Sorbose / analogs & derivatives*
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Sorbose / biosynthesis*
Substances
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6-(2-hydroxyethyl) amino-6-deoxy-L-sorbose
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Bacterial Proteins
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Membrane Proteins
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Sorbitol
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PQQ Cofactor
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L-Iditol 2-Dehydrogenase
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Sorbose