| Autor: |
SHINJOH, Masako, TOMIYAMA, Noribumi, MIYAZAKI, Taro, HOSHINO, Tatsuo |
| Zdroj: |
Bioscience, Biotechnology, and Biochemistry; January 2002, Vol. 66 Issue: 11 p2314-2322, 9p |
| Abstrakt: |
The D-sorbitol dehydrogenase gene, sldA, and an upstream gene, sldB, encoding a hydrophobic polypeptide, SldB, of Gluconobacter suboxydansIFO 3255 were disrupted in a check of their biological functions. The bacterial cells with the sldAgene disrupted did not produce L-sorbose by oxidation of D-sorbitol in resting-cell reactions at pHs 4.5 and 7.0, indicating that the dehydrogenase was the main D-sorbitol-oxidizing enzyme in this bacterium. The cells did not produce D-fructose from D-mannitol or dihydroxyacetone from glycerol. The disruption of the sldBgene resulted in undetectable oxidation of D-sorbitol, D-mannitol, or glycerol, although the cells produced the dehydrogenase. The cells with the sldBgene disrupted produced more of what might be signal-unprocessed SldA than the wild-type cells did. SldB may be a chaperone-like component that assists signal processing and folding of the SldA polypeptide to form active D-sorbitol dehydrogenase. |
| Databáze: |
Supplemental Index |
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