FURTHER STUDIES ON REGULATION OF AMINO SUGAR METABOLISM IN BACILLUS SUBTILIS
FURTHER STUDIES ON REGULATION OF AMINO SUGAR METABOLISM IN BACILLUS SUBTILIS
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DOI：
10.1042/bj0960147
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发表时间：
1965-01-01
影响因子：
4.1
通讯作者：
PASTERNAK, CA
中科院分区：
文献类型：
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作者：
BATES, CJ;PASTERNAK, CA
对枯草杆菌氨基葡萄糖6-磷酸脱氨酶[2-氨基-2-脱氧-D-葡萄糖6-磷酸-酮醇异构酶(脱氨基)，EC 5.3.1.10]进行了部分纯化。它的公里是3.0米[图片]。枯草杆菌的提取物含有N-乙酰氨基葡萄糖6-磷酸脱乙酰酶(KM T.4m[图像])、氨基葡萄糖1-磷酸乙酰基酶和氨基糖激动酶(EC 2.7.1.8和2.7.1.9)。氨基葡萄糖6-磷酸合成酶(L-谷氨酰胺-D-果糖6-磷酸氨基转移酶，EC 2.6.1.16)是枯草杆菌在氨基葡萄糖、N-乙酰氨基葡萄糖、N-丙酰氨基葡萄糖或N-甲酰氨基葡萄糖存在下生长的抑制因子。氨基葡萄糖6-磷酸脱氨酶和N-乙酰氨基葡萄糖6-磷酸脱乙酰酶是由N-乙酰氨基葡萄糖诱导的。氨基糖激酶是由葡萄糖、氨基葡萄糖和N-乙酰氨基葡萄糖诱导的。氨基糖不影响氨基葡萄糖1-磷酸乙酰基酶的合成。生长介质中的葡萄糖可阻止由N-乙酰氨基葡萄糖引起的氨基葡萄糖6-磷酸脱氨酶和N-乙酰氨基葡萄糖6-磷酸脱乙酰酶的诱导；葡萄糖也可减轻氨基糖对氨基葡萄糖6-磷酸合成酶的抑制。在超过指数生长期的细菌中，氨基葡萄糖6-磷酸脱氨酶增加。这种增加可以被葡萄糖阻止。
Glucosamine 6-phosphate deaminase [2-amino-2-deoxy-D-glucose 6-phosphate ketol-isomerase (deaminating), EC 5.3.1.10] of B. subtilis was partially purified. Its Km is 3.0m[image]. Extracts of B. subtilis contain N-acetylglucosamine 6-phosphate deacetylase (Km T.4 m[image]), glucosamine 1 -phosphate acetylase and amino sugar kinases (EC 2.7.1.8 and 2.7.1.9). Glucosamine 6-phosphate synthetase (L-glutamine-D-fructose 6-phosphate aminotransferase, EC 2.6.1.16) is repressed by growth of B. subtilis in the presence of glucosamine, N-acetylglucos-aniine, N-propionylglucosamine or N-formylglucosamine. Glucosamine 6-phosphate deaminase and N-acetylglucosamine 6-phosphate deacetylase are induced by N-acetylglucosamine. Amino sugar kinases are induced by glucose, glucosamine and N-acetylglucosamine. The synthesis of glucosamine 1-phosphate acetylase is unaffected by amino sugars. Glucose in the growth medium prevents the induction of glucosamine 6-phosphate deaminase and N-acetylglucosamine 6-phosphate deacetylase caused by N-acetylglucosamine; glucose also alleviates the repression of glucosamine 6-phosphate synthetase caused by amino sugars. Glucosamine 6-phosphate deaminase increases in bacteria incubated beyond the exponential phase of growth. This increase is prevented by glucose.