Journal Article

PreJuSER-31323

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants

Janowitz, T. ; Kneifel, H.FZJ* ; Piotrowski, M.

2003
Elsevier Amsterdam [u.a.]

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Please use a persistent id in citations: doi:10.1016/S0014-5793(03)00515-5

Abstract: 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.

Keyword(s): J ; agmatine intinohydrolase (agmatine deiminase) (auto) ; N-carbamoylputrescine (auto) ; polyamine biosynthesis (auto) ; putrescine (auto) ; Arabidopsis thaliana (auto)

Note: Record converted from VDB: 12.11.2012

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Contributing Institute(s):

1. Phytosphäre (ICG-III)

Research Program(s):

1. Chemie und Dynamik der Geo-Biosphäre (U01)

Appears in the scientific report 2003

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