Amidohydrolysis of N-methylhydantoin coupled with ATP hydrolysis.
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.
D000255:Adenosine Triphosphate / Q000378:metabolism*; D000581:Amidohydrolases / Q000302:isolation & purification / Q000378:metabolism*; D006827:Hydantoins / Q000378:metabolism*; D006868:Hydrolysis; D008274:Magnesium / Q000494:pharmacology; D011188:Potassium / Q000494:pharmacology; D011549:Pseudomonas / Q000201:enzymology*
D006827:Hydantoins; C032067:1-methylhydantoin; D000255:Adenosine Triphosphate; D000581:Amidohydrolases; C051522:N-methylhydantoin amidohydrolase; D008274:Magnesium; D011188:Potassium