Regulation of aspartokinase in Lactobacillus plantarum

Adebawo, Olugbenga O.; Ruiz-Barba, José Luis; Warner, Philip J.; Oguntimein, Gbekeloluwa B.

doi:10.1111/j.1365-2672.1997.tb02850.x

Cited by 2 publications

(4 citation statements)

References 13 publications

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Section: Regulation Of Enzymes By Amino Acidscontrasting

confidence: 99%

“…Our results are thus at variance with the report of Adebawo et al (1997), who found that aspartokinase in L. plantarum was not inhibited by amino acids of the aspartate family. Despite that difference, the activation of aspartokinase by L-methionine observed in this study (Tables 2 and 3) was also reported by Adebawo et al (1997). The regulation of aspartokinase in L. plantarum was found to differ from that in other organisms such as E. coli (Patte et al, 1967;Theze et al, 1974), Bacillus subtilis (Graves & Switzer, 1990;Rosner & Paulus, 1971) and C. glutamicum (Nakayama et al, 1966).…”

Section: Regulation Of Enzymes By Amino Acidscontrasting

confidence: 99%

“…In L. plantarum, only the regulation of aspartokinase has been reported to date (Adebawo et al, 1997); that study was done with cell extract of L. plantarum. Because aspartokinase in L. plantarum may be present as an isozyme, as indicated in the genome sequence (Kleerebezem et al, 2003), the study of enzyme regulation using cell extracts of L. plantarum may not be appropriate; the aspartokinases should be separated when the regulation of the enzyme is studied.…”

Section: Introductionmentioning

confidence: 99%

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Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum

et al. 2006

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The use of a lysine-overproducing strain of Lactobacillus plantarum in food or feed fermentations may lead to the production of lysine-rich products. The availability of functional genes and information on the regulation of lysine biosynthesis are required to develop a lysine-overproducing strain. The genome sequence of L. plantarum revealed putative lysine biosynthetic genes, some of which may produce isozymes. This study examined the functionality of the genes and the regulation of the first four enzymes of lysine biosynthesis, together with homoserine dehydrogenase, in L. plantarum. The genes were expressed in Escherichia coli, and the regulation of the enzymes was studied in cell extracts of both recombinant E. coli and L. plantarum. Among seven lysine biosynthetic genes studied (aspartokinase genes, thrA1 and thrA2; aspartate semialdehyde dehydrogenase genes, asd1 and asd2; dihydrodipicolinate synthase genes, dapA1 and dapA2; and the dihydrodipicolinate reductase gene, dapB) plus two homoserine dehydrogenase genes (hom1 and hom2), the products of six genes, i.e. thrA2, asd2, dapA1, dapB, hom1 and hom2, showed obvious enzyme activities in vitro. The product of one of the homoserine dehydrogenase genes, hom1, exhibited both homoserine dehydrogenase and aspartokinase activities. However, the aspartokinase activity was mainly due to ThrA2 and was inhibited by L-lysine and repressed by L-threonine, and the homoserine dehydrogenase activity was mainly due to Hom2 and was inhibited by L-threonine. The aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase were not regulated by the end-products of the pathway.

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Section: Regulation Of Enzymes By Amino Acidscontrasting

confidence: 99%

Section: Regulation Of Enzymes By Amino Acidscontrasting

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum

et al. 2006

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“…Lysine and tryptophan contents of cereal grains increase owing to synthesis by micro-organisms during fermentation. [30][31][32][33] The concentrations of these amino acids were higher in ogi from fermented malt, because germination also increases the lysine and tryptophan contents of grains. 30 Tsai et al 30 observed increases of over 50% in lysine and tryptophan when maize was germinated.…”

Section: Protein Qualitymentioning

confidence: 99%

Changes in the physical and biochemical properties of pearl millet (Pennisetum americanum) on conversion to ogi

et al. 2002

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Millet was converted into ogi, a naturally fermented cereal product, by the traditional wet milling/wet sieving process and by fermenting millet meal and ground millet malt. Proximate chemical composition, flavanol content, vitamin A and B 2 contents, energy value, protein and starch availabilities and Brabender paste viscosity of millet grain and ogi were determined. Yields of ogi ranged from 67.5 to 96.5%. Protein, ether extract, ash and crude fibre contents were reduced in ogi by 2.3-24, 3.9-25.5, 14.3-28.6 and 6.6-42.3% respectively, while the soluble carbohydrate content of the grain (68.2 AE 12 g kg À1 ) was retained. Flavanol content of millet (1.025 g c-glycosylflavanol equivalent kg À1 grain) was reduced in ogi (0.643-0.872 g c-glycosylflavanol equivalent kg À1 grain). Vitamin A content was reduced by 21.4-53.4% and vitamin B 2 content was increased by 85.7-242.8% on conversion of millet into ogi. Apparent protein availability increased by 91.3-144.9% with papain digestion and by 47.6-109.5% without papain. However, changes in tryptophan (5.6%) and lysine (5.2%) were less marked, except in ogi from malt, which showed 22.2 and 20.8% increases in tryptophan and lysine contents respectively. Apparent carbohydrate availability increased (by 17-93%) but energy value generally remained the same (highest increase 3.4%) when millet was converted to ogi. Conversion of grain to ogi reduced paste viscosity.

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Regulation of aspartokinase in Lactobacillus plantarum

Cited by 2 publications

References 13 publications

Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum

Regulation of aspartokinase, aspartate semialdehyde dehydrogenase, dihydrodipicolinate synthase and dihydrodipicolinate reductase in Lactobacillus plantarum

Changes in the physical and biochemical properties of pearl millet (Pennisetum americanum) on conversion to ogi

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