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Ureide catabolism in soybeans. III. Ureidoglycolate amidohydrolase and allantoate amidohydrolase are activities of an allantoate degrading enzyme complex

Journal Article · · Plant Physiology; (USA)
DOI:https://doi.org/10.1104/pp.86.4.1084· OSTI ID:6994849

The authors demonstrate that allantoate is catabolized in soybean seedcoat extracts by an enzyme complex that has allantoate amidohydrolase and ureidoglycolate amidohydrolase activities. Soybean seedcoat extracts released {sup 14}CO{sub 2} from (ureido-{sup 14}C)ureidoglycolate under conditions in which urease is not detectable. CO{sub 2} and glyoxylate are enzymatically released in a one to one ratio indicating that ureidoglycolate amidohydrolase is the responsible activity. Ureidoglycolate amidohydrolase has a K{sub m} of 85 micromolar for ureidoglycolate. Glyoxylate and CO{sub 2} are enzymatically released from allantoate at linear rates in a one to 2.3 ratio from 5 to 30 min. That ({sup 14}C)urea production from (2,7-{sup 14}C)allantoate is not detectable indicates that allantoate-dependent glyoxylate production is enzymic and not a result of nonenzymatic hydrolysis of a ureido intermediate (nonenzymatic hydrolysis releases urea). The results suggest that soybeans have a second amidohydrolase reaction that follows allantoate amidohydrolase in allantoate catabolism. The rate of {sup 14}CO{sub 2} release from (2,7-{sup 14}C)allantoate is not reduced when the volume of the reaction mixture is increased, suggesting that the release of {sup 14}CO{sub 2} is not dependent on the accumulation of free intermediates. That (2,7-{sup 14}C)allantoate dependent {sup 14}CO{sub 2} release is not proportionally diluted by unlabeled ureidoglycoalte indicates that the reaction is carried out by an enzyme complex.

OSTI ID:
6994849
Journal Information:
Plant Physiology; (USA), Journal Name: Plant Physiology; (USA) Vol. 86:4; ISSN 0032-0889; ISSN PLPHA
Country of Publication:
United States
Language:
English