Summary
WhenA. ureafaciens are grown in a medium containing either creatinine or creatine as the sole source of carbon, an enzyme system capable of catabolizing creatine and creatinine is induced. This enzyme system has been isolated in a cell-free extract and is composed of two separate enzymes. The first, creatinine hydrolase, interconverts creatinine and creatine to form an equilibrium mixture of the two. The second enzyme, creatine amidinohydrolase, splits creatine into equimolar amounts of sarcosine and urea. The former enzyme is heat stable at 55°C for 30 min while the latter enzyme is completely destroyed at this temperature. The two enzymes have different solubilities in ammonium sulfate solutions.
Similar content being viewed by others
References
B. F. Miller, R. Dubos, “Enzyme for decomposition of creatinine and its action on the ‘apparent creatinine’ of blood.” Proc. Soc. Exp. Biol. Med. 35, 335 (1936).
R. Dubos, B. F. Miller, “The production of bacterial enzymes capable of decomposing creatinine.” J. Biol. Chem. 121, 429 (1937).
B. F. Miller, R. Dubos, “Studies on the presence of creatinine in human blood.” J. Biol. Chem. 121, 447 (1937).
B. F. Miller, R. Dubos, “Determination by a specific, enzymatic method of the creatinine content of blood and urine from normal and nephritic individuals.” J. Biol. Chem. 121, 457 (1937).
H. A. Krebs, L. V. Eggleston, “Bacterial urea formation.” Enzymologia 7, 310 (1939).
S. Akamatsu, Y. Kanai, “Bacterial decomposition of creatinine. I. Creatinomutase.” Enzymologia 15, 122 (1951).
S. Akamatsu, R. Miyashita, “Bacterial decomposition of creatine. III. The pathway of creatine decomposition.” Enzymologia 15, 173 (1951).
J. Roche, G. Lacombe, “Sur la spécificité de certaines déguanidases bactériennes génératrices d'urée et sur l'arginine-dihydrolase.” Biochim. Biophys. Acta 6, 210 (1950).
J. Szulmajster, “Bacterial fermentation of creatinine. I. Isolation of N-methyl-hydantoin.” J. Bact. 75, 633 (1958).
J. Szulmajster, “Bacterial degradation of creatinine. II. Creatinine desimidase.” Biochim. Biophys. Acta 30, 154 (1958).
H. G. Van Eyk, R. J. Vermaat, H. J. Leijnse-Ybema, B. Leijnse, “The conversion of creatinine by creatininase of bacterial origin.” Enzymologia 34, 198 (1968).
G. R. Kingsley, R. R. Schaffert, “Creatinine.” Stand. Methods Clin. Chem. 1, 55 (1953).
A. L. Chaney, E. P. Marbach, “Modified reagents for determination of urea and ammonia.” Clin. Chem. 8, 130 (1962).
D. Hunninghake and S. Grisolia, “A sensitive and convenient micromethod for estimation of urea, citrulline and carbamyl derivatives.” Anal. Biochem. 16, 200 (1966).
M. Florkin and E. H. Stotz, Comprehensive Biochemistry, Vol. 13, Elsevier, Amsterdam 1965.
Report of the Commission on Enzymes of the International Union of Biochemistry, Vol. 20, Pergamon Press, New York 1961.
Author information
Authors and Affiliations
Additional information
Predoctoral Fellow supported by NIH Training Grant GM00052.
Submitted in partial fulfillment of the M.S. degree.
Rights and permissions
About this article
Cite this article
Kaplan, A., Naugler, D. Creatinine hydrolase and creatine amidinohydrolase: I. Presence in cell-free extracts of arthrobacter ureafaciens. Mol Cell Biochem 3, 9–15 (1974). https://doi.org/10.1007/BF01660072
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF01660072