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Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA
Address for correspondence: Sidney M. Morris, Jr., Department of Molecular Genetics and Biochemistry University of Pittsburgh School of Medicine, Pittsburgh, PA 15261, USA. Voice: 412-648-9338; fax: 412-624-1401. e-mail: smorris{at}pitt.edu Ann. N.Y. Acad. Sci. 1009: 30-33 (2003).
Whereas agmatine in vertebrates may be derived from multiple sources such as the diet, endogenous synthesis via arginine decarboxylase, and possibly also from enteric bacteria, agmatinase is the only enzyme specific for agmatine catabolism. As it hydrolyzes a guanidino group within agmatine and also contains signature amino acid residues that act as ligand binding sites for the Mn++ cofactor, agmatinase is classified as a member of the arginase superfamily. Very little information is available regarding how much agmatine in vertebrate species is catabolized by agmatinase versus other enzymes such as diamine and amine oxidases. Moreover, comparisons of primary sequences of several vertebrate agmatinases demonstrate that several residues essential for catalytic activity are not conserved in the mouse. This leads to the prediction that the agmatinase protein in mouse has little or no catalytic activity, not only raising questions about the physiologic routes of agmatine disposal in this organism, but also suggesting the existence of species-specific differences in mechanisms for regulating agmatine levels.
Key Words: agmatine • catabolism • mammalian agmatinases • arginine superfamily This article has been cited by other articles:
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