Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.20 (alpha-glucosidase)
 4,237 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An attempt was made to determine whether sporulation and inducible enzyme synthesis in Bacillus subtilis are controlled by the same mechanism of catabolite repression. By the use of a thymine-requiring strain, it has been shown that, whereas sporulation remained repressed unless chromosome replication proceeded to completion, the induction of the enzymes histidase, sucrase, and alpha-glucosidase proceeded quite normally in the absence of continued deoxyribonucleic acid synthesis. It is concluded that the mechanism for overcoming the repression of sporulation differs qualitatively from that involved in overcoming the repression of inducible enzyme synthesis. Attempts to isolate pleiotropic mutants that would provide additional support for this contention were unsuccessful. A pleiotropic mutant deficient in phosphoenolpyruvate-dependent phosphotransferase activity sporulated quite well, whereas a mutant presumed deficient in glutamate synthetase sporulated poorly under all conditions.
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PMID:Comparative studies on induction of sporulation and synthesis of inducible enzymes in Bacillus subtilis. 421 91

Strain SF22, a glutamine-requiring (Gln-) mutant of Bacillus subtilis SMY, is likely to have a mutation in the structural gene for glutamine synthetase, since this strain synthesized 22 to 55% as much glutamine synthetase antigen as did wild-type cells in a 10-min period but had less than 3% of wild-type glutamine synthetase enzymatic activity. The expression of several genes subject to glucose catabolite repression was altered in the Gln- mutant. The induced levels of alpha-glucosidase, histidase, and aconitase were 3.5- to 4-fold higher in SF22 cells than in wild-type cells grown in glucose-glutamine medium, and citrate synthase levels were 8-fold higher in the Gln- mutant than in wild-type cells. The relief of glucose catabolite repression in the Gln- mutant may result from poor utilization of glucose. Examination of the intracellular metabolite pools of cells grown in glucose-glutamine medium showed that the glucose-6-phosphate pool was 2.5-fold lower, the pyruvate pool was 4-fold lower, and the 2-ketoglutarate pool was 2.5-fold lower in the Gln- cells than they were in wild-type cells. Intracellular levels of glutamine were sixfold higher in the Gln- mutant than in wild-type cells. Measurements of enzymes involved in glutamine transport and utilization showed that the elevated pools of glutamine in the Gln- mutant resulted from a threefold increase in glutamine permease and a fivefold decrease in glutamate synthase. The pleiotropic effect of the gln-22 mutation on the expression of several genes suggests that either the glutamine synthetase protein or its enzymatic product, glutamine, is involved in the regulation of several metabolic pathways in B. subtilis.
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PMID:Bacillus subtilis glutamine synthetase mutants pleiotropically altered in glucose catabolite repression. 614 Nov 56