2014
DOI: 10.1139/cjm-2013-0793
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Role of prokaryotic type I and III pantothenate kinases in the coenzyme A biosynthetic pathway ofBacillus subtilis

Abstract: Pantothenate kinases (CoaAs) catalyze the phosphorylation of pantothenate in the first step of the coenzyme A (CoA) biosynthetic pathway. These bacterial enzymes have been categorized into 3 types, the prokaryotic type I, II, and III CoaAs. Bacteria typically carry a single CoaA gene on their genome, but Bacillus subtilis possesses 2 proteins homologous to type I and III CoaAs, known as BsCoaA and BsCoaX, respectively. Both recombinant proteins exhibited the expected kinase activity and the characteristic prop… Show more

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Cited by 10 publications
(8 citation statements)
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“…The addition of gluconates into the medium may also increase the basal level of acetyl-CoA following glycolysis, resulting in the elevated production of PHB. An increase in the production of CoA may also be effective for the overproduction of PHB in the biosynthetic pathway (29). Another approach using synergistic effects, involving increases in the expression of the RNA polymerase sigma factor SigE in the transconjugant 6803GT_ABEC, which may be advantageous for the further overproduction of PHB in future studies (11,30).…”
Section: Metabolite Analysis In Phb Overproductionmentioning
confidence: 99%
“…The addition of gluconates into the medium may also increase the basal level of acetyl-CoA following glycolysis, resulting in the elevated production of PHB. An increase in the production of CoA may also be effective for the overproduction of PHB in the biosynthetic pathway (29). Another approach using synergistic effects, involving increases in the expression of the RNA polymerase sigma factor SigE in the transconjugant 6803GT_ABEC, which may be advantageous for the further overproduction of PHB in future studies (11,30).…”
Section: Metabolite Analysis In Phb Overproductionmentioning
confidence: 99%
“…C. ammoniagenes carries a type I coaA which is highly regulated by CoA and its derivatives. In contrast, type II and III enzymes are insensitive to CoA and its thioesters [27, 28], therefore, in order to reduce feedback inhibition and increase the production of CoA, the type III pantothenate kinase from Pseudomonas putida ( Pp coaA) was selected and overexpressed by the control of the strongest promoter P rpl21 in C. ammoniagenes ATCC 6871 [29, 30].…”
Section: Resultsmentioning
confidence: 99%
“…Previously, it has also been shown that E. coli mutants constitutively expressing DsdA are able to use D-serine as the sole source of carbon and nitrogen (Bloom and McFall, 1975). In B. subtlilis the dsdA gene is located in the yqjP - yqjQ - dsdA - coaA - yqjT operon, containing three genes of unknown function as well as the dsdA and coaA genes, of which the latter encodes the major pantothenate kinase CoaA (Ogata et al, 2014). The genetic context of the dsdA gene strongly suggests that the D-serine deaminase may be involved in the detoxification of D-serine that probably also interferes with pantothenate synthesis in B. subtilis .…”
Section: Poorly Characterized Plp-dependent Enzymesmentioning
confidence: 99%