Targeted disruption of the kstD gene encoding a 3-ketosteroid delta (super-1)-dehydrogenase isoenzyme of Rodocococcus erythropolis strain SQ1

Article Abstract:

The kstD gene which encodes a 3-ketosteroid delta(super.1)-dehydrogenase isoenzyme of Rodococcus erythropolis strain SQ1 and its targeting disruption are discussed. R. erythropolis was shown to have two activity bands, one of which is not seen in the kstD mutant strain. Inactivation of kstD is not sufficient for inactivation of the delta(super.1) dehydrogenase activity.

Physiological aspects, Genetic aspects, Bacteria, Microbial enzymes

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Targeted disruption of the kstD gene encoding a 3-ketosteroid Delta (super)1 -dehydrogenase isoenzyme of Rhodococcus erythropolis strains SQ1

Article Abstract:

Research has been conducted on the microbial phytosterol degradation. Degradation of these sreroid intermediates initiated by Delta (super)1 -dehydrogenation of the steroid ring structure has been investigated.

Statistical Data Included, Analysis, Gene expression, Microbiological research, Isoenzymes

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Chorismate mutase and 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase of the methylotrophic actinomycete Amycolatopsis methanolica

Article Abstract:

Chorismate mutase (CM) activity in wild-type Amycolatopsis methanolica cells requires two proteins, CMIa and CMIb. Similar is the case with 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase (DS): DSI and DSII. L-phenylalanine and L-tyrosine inhibit the activities of both CMIa and CMIb. These two amino acids and also L-tryptophan inhibit DSI activity. Another homodimeric CM (CMII), with 16 kDa subunits, is insensitive to allosteric inhibition by L-phenylalanine and L-tyrosine.

Observations, Biosynthesis, Enzyme kinetics, Amino acid metabolism, Allosteric enzymes

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