Journal
FEBS LETTERS
Volume 544, Issue 1-3, Pages 258-261Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(03)00515-5
Keywords
agmatine intinohydrolase (agmatine deiminase); N-carbamoylputrescine; polyamine biosynthesis; putrescine; Arabidopsis thaliana
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The cloning, expression and characterization of plant agmatine iminohydrolase (AIH, also known as agmatine deiminase, EC 3.5.3.12) is described. Recombinant AIH of Arabidopsis thaliana forms dimers and catalyzes the specific conversion of agmatine to N-carbamoylputrescine and ammonia. Biochemical data suggested that cysteine side chains are involved in catalysis. However, site-directed mutagenesis of the two highly conserved cysteine residues of AIH showed that these cysteines are important but not essential for activity, arguing against a thioester substrate-enzyme intermediate during catalysis. This work represents the completion of the cloning of the arginine decarboxylase pathway genes of higher plants. (C) 2003 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.
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