Roon R J, Barker H A
J Bacteriol. 1972 Jan;109(1):44-50. doi: 10.1128/jb.109.1.44-50.1972.
Putrescine transcarbamoylase, EC 2.1.3.x (carbamoylphosphate:putrescine transcarbamoylase), has been purified from Streptococcus faecalis 10C1 grown on agmatine as primary energy source. The formation of N-carbamoylputrescine from putrescine and carbamoylphosphate serves as a convenient and sensitive assay for this enzymatic activity. The enzyme catalyzes both the phosphorolysis arsenolysis of N-carbamoylputrescine. Arginine does not induce the synthesis of putrescine transcarbamoylase in S. faecalis. Furthermore, the putrescine transcarbamoylase activity is easily separated from ornithine transcarbamoylase activity by gel filtration on Sephadex G-100 indicating that the two activities are associated with different proteins. The significance of this new enzyme in the fermentation of agmatine and its relation to the other known transcarbamoylases are discussed.
腐胺转氨甲酰酶，EC 2.1.3.x（氨基甲酰磷酸：腐胺转氨甲酰酶），是从以胍丁胺作为主要能量来源生长的粪肠球菌10C1中纯化得到的。由腐胺和氨基甲酰磷酸形成N-氨甲酰腐胺可作为该酶活性便捷且灵敏的检测方法。该酶催化N-氨甲酰腐胺的磷酸解和砷解。精氨酸不会诱导粪肠球菌中腐胺转氨甲酰酶的合成。此外，通过在葡聚糖G-100上进行凝胶过滤，腐胺转氨甲酰酶活性很容易与鸟氨酸转氨甲酰酶活性分离，这表明这两种活性与不同的蛋白质相关。本文讨论了这种新酶在胍丁胺发酵中的意义及其与其他已知转氨甲酰酶的关系。
