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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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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.[1]

References

  1. Amidohydrolysis of N-methylhydantoin coupled with ATP hydrolysis. Kim, J.M., Shimizu, S., Yamada, H. Biochem. Biophys. Res. Commun. (1987) [Pubmed]
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