粪肠球菌中胍丁胺降解酶及其合成的调控
Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis.
作者信息
Simon J P, Stalon V
出版信息
J Bacteriol. 1982 Nov;152(2):676-81. doi: 10.1128/jb.152.2.676-681.1982.
Abstract
Streptococcus faecalis ATCC 11700 uses agmatine as its sole energy source for growth. Agmatine deiminase and putrescine carbamoyltransferase are coinduced by growth on agmatine. Glucose and arginine were found to exert catabolite repression on the agmatine deiminase pathway. Four mutants unable to utilize agmatine as an energy source, isolated from the wild-type strain, exhibited three distinct phenotypes. Two of these strains showed essentially no agmatine deiminase, one mutant showed negligible activity of putrescine carbamoyltransferase, and one mutant was defective in both activities. Two carbamate kinases are present in S. faecalis, one belonging to the arginine deiminase pathway, the other being induced by growth on agmatine. These two enzymes have the same molecular weight, 82,000, and seem quite different in size from the kinases isolated from other streptococci.
摘要
粪肠球菌ATCC 11700利用胍丁胺作为其生长的唯一能量来源。胍丁胺脱亚氨酶和腐胺氨基甲酰转移酶在以胍丁胺为碳源生长时被共同诱导。发现葡萄糖和精氨酸对胍丁胺脱亚氨酶途径发挥分解代谢物阻遏作用。从野生型菌株中分离出的四个不能利用胍丁胺作为能量来源的突变体表现出三种不同的表型。其中两个菌株基本没有胍丁胺脱亚氨酶，一个突变体的腐胺氨基甲酰转移酶活性可忽略不计，还有一个突变体在这两种活性方面均有缺陷。粪肠球菌中存在两种氨基甲酸激酶，一种属于精氨酸脱亚氨酶途径，另一种在以胍丁胺为碳源生长时被诱导。这两种酶的分子量相同，均为82,000，而且在大小上似乎与从其他链球菌中分离出的激酶有很大不同。
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