Novel amidohydrolytic reactions in oxidative pyrimidine metabolism: analysis of the barbiturase reaction and discovery of a novel enzyme, ureidomalonase.
Amidohydrolytic reactions in oxidative pyrimidine metabolism were investigated in detail. Barbiturase has been reported to catalyze the amidohydrolysis of barbituric acid to urea and malonic acid. However, purification of the enzyme revealed that it catalyzes the ring-opening of barbituric acid to ureidomalonic acid. The existence of a consecutive enzyme named ureidomalonase, which hydrolyzes ureidomalonic acid to urea and malonic acid, was also discovered during the purification of barbiturase.
Soong
C L
CL
Division of Applied Life Sciences, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Ogawa
J
J
Shimizu
S
S
D000577:Amides / Q000378:metabolism*; D000581:Amidohydrolases / Q000096:biosynthesis / Q000378:metabolism*; D004790:Enzyme Induction; D006868:Hydrolysis; D010084:Oxidation-Reduction; D011743:Pyrimidines / Q000378:metabolism*; D012240:Rhodococcus / Q000201:enzymology / Q000378:metabolism
D000577:Amides; D011743:Pyrimidines; D000581:Amidohydrolases; C434740:ureidomalonase; C434739:barbiturase