Kim J M, Shimizu S, Yamada H
Biochem Biophys Res Commun. 1987 Feb 13;142(3):1006-12. doi: 10.1016/0006-291x(87)91514-2.
A new enzyme, N-methylhydantoin amidohydrolase, was highly purified from Pseudomonas putida 77: it catalyzes the hydrolysis of N-methylhydantoin to N-carbamoylsarcosine with the concomitant stoichiometric cleavage of ATP to ADP and orthophosphate. The enzyme absolutely requires ATP, MG2+ and K+ for the N-methylhydantoin hydrolysis. The rapid and complete degradation of N-methylhydantoin during the cultivation of P. putida 77, which rapidly degrades creatinine via only N-methylhydantoin and which shows high activities of the enzymes involved in creatinine degradation (Yamada et al. (1985) FEMS Microbiol. Lett. 30, 337-340), seems to be due to the continuous ATP-generation during cultivation.
一种新的酶，N-甲基乙内酰脲酰胺水解酶，从恶臭假单胞菌77中被高度纯化：它催化N-甲基乙内酰脲水解为N-氨甲酰基肌氨酸，同时伴随着ATP化学计量地裂解为ADP和正磷酸盐。该酶催化N-甲基乙内酰脲水解时绝对需要ATP、Mg2+和K+。恶臭假单胞菌77在培养过程中能快速且完全地降解N-甲基乙内酰脲，它仅通过N-甲基乙内酰脲快速降解肌酐，并且显示出参与肌酐降解的酶具有高活性（Yamada等人（1985年），《FEMS微生物学快报》30卷，337 - 340页），这似乎是由于培养过程中持续产生ATP所致。
