Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:6.2.1.1 (ACS)
 78,556 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The Bacillus subtilis acsA (acetyl coenzyme A synthetase) and acuABC (acetoin utilization) genes were previously identified in the region downstream from the ccpA gene, which encodes a protein required for catabolite repression of the amyE (alpha-amylase) gene. The acsA and acuABC genes are divergently transcribed, with only 20 bp separating the -35 sequences of their promoters. Expression of these genes was maximal in stationary phase and was repressed by the addition of glucose to the growth medium. Two sites resembling amyO, the cis-acting regulatory target site for amyE, were identified in the acsA and acuABC promoter regions. Glucose repression of acsA and acuABC transcription was dependent on both CcpA and the amyO-like sequences.
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PMID:Catabolite regulation of Bacillus subtilis acetate and acetoin utilization genes by CcpA. 791 27

Suppression of postprandial hyperglycemia reduces lipogenic enzyme activities in the adipose tissues of normal rats. The present study investigated the expression of genes related to lipogenesis and insulin sensitivity in mesenteric adipose and epididymal adipose tissues to evaluate the effects of wheat albumin (WA) and a crude preparation of WA (CWA) with alpha-amylase inhibitory activity on lipid metabolism. Rats fed 2.5% WA, which had 12.7-fold inhibitory activity compared with CWA, exhibited reduced mRNA levels for G6PDH, ACO, ACS, PEPCK, and LPL in the mesenteric adipose, but not in the epididymal adipose tissue. Linear regression analyses showed that the gene expression levels of FAS, G6PDH, ACS, and LPL were reduced in dose-dependent manners in the mesenteric adipose tissue of rats fed the CWA diet. These results suggest that supplementation with CWA as well as WA reduces the expression of genes related to lipogenesis and insulin sensitivity in mesenteric adipose tissue.
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PMID:Effects of wheat albumin consumption on expression of genes related to lipogenesis and insulin sensitivity in adipose tissues of rats. 1917 May 1

A robust biocatalyst was produced by immobilization of alpha-amylase into mesoporous silica thin films with local order pore structure and 11 nm pore diameter, supported on glass stripes. The activity of this novel catalyst was evaluated for direct starch degradation. The catalyst films show excellent activity, and enhanced stability with respect to free enzyme at extreme conditions of pH and temperature. In addition, they can be easily separated from the reaction media and reused several times.
ACS Appl Mater Interfaces 2010 Feb
PMID:Amylase-functionalized mesoporous silica thin films as robust biocatalyst platforms. 2035 81