TY - JOUR
AU - Dods, R, F
AB - Abstract This and previous papers examine the reasons for the relationship between the concentrations of guanidino-succinate and guanidinoacetate in human urine. With the demonstration here that extracts of human liver-tissue can mediate ureidohomoserine formation from canaline [(2-amino-4-aminooxy)-butyric acid] and carbamoyl phosphate, all steps in a cycle proposed for the production of guanidinoacetate and guanidinosuccinate have been documented. This includes synthesis of canavaninosuccinate from aspartate and ureidohomoserine, reductive cleavage of canavaninosuccinate to form guanidinosuccinate and homoserine, or, alternatively, lytic action on canavaninosuccinate to form fumarate and canavanine, and transamidination to glycine to form guanidinoacetate, regenerating the canaline. We propose that canaline originates from aspartate, but the precise mechanism by which canaline is formed needs to be elucidated. This content is only available as a PDF. © 1977 The American Association for Clinical Chemistry, Inc. This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model)
TI - Canaline carbamoyltransferase in human liver as part of a metabolic cycle in which guanidino compounds are formed.
JF - Clinical Chemistry
DO - 10.1093/clinchem/23.6.960
DA - 1977-06-01
UR - https://www.deepdyve.com/lp/oxford-university-press/canaline-carbamoyltransferase-in-human-liver-as-part-of-a-metabolic-WybFSORHE3
SP - 960
EP - 966
VL - 23
IS - 6
DP - DeepDyve
ER -