Article Abstract:
The Corynebacterium glutamicum panD (panD(sub C.g.)) gene encoding L-aspartate-alpha-decarboxylase was identified and its characterization and directed mutagenesis described. It was identified by functional complementation of an Escherichia coli panD mutant. The enhanced expression of panD(sub C.g.) in C glutamicum resulted in the formation of two distinct proteins in sodium dodecyl sulfate-polyacrylamide gel electrophesis. The enhanced expression of panD(sub C.g.) in E coli led to the highest amount of pantothenate in the culture medium.
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Article Abstract:
Inactivation of the glutamate decarboxylase gene is discussed relative to Lactococcus lactis subsp. cremoris, the strains of which do not show glutamate decarboxylase activity although Lactococcus lactis subsp lactis strains do. The gadB gene which encodes glutamate decarboxylase was found in the L. lactis subsp. cremoris genome. It was, however, poorly expressed. It was shown through sequence analysis that the gene is inactivated by the frameshift mutation and encoded in a nonfunctional protein.
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Article Abstract:
A study was conducted to analyze the purification of Lactococcus lactis glutamate decarboxylase (GAD) 114-fold using a three-step procedure and to examine its biochemical properties. Lactococcus lactis subsp. lactis biovar diacetylactis was isolated from a cheese starter. It was then maintained in sterile litmus milk and subcultured once a week. Experimental results indicated only one GAD structural gene in L. lactis.
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