Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants

FEBS Letters

Janowitz, Tim²  Kneifel, Helmut¹  Piotrowski, Markus² 

[1]Institute for Chemistry and Dynamics of the Geosphere, Institute III: Phytosphere, Forschungszentrum Jülich GmbH, D-52425 Jülich, Germany

[2]Department of Plant Physiology, Ruhr-Universität, Universitätsstr. 150, D-44801 Bochum, Germany

关键词: Agmatine iminohydrolase (agmatine deiminase);    N-Carbamoylputrescine;    Polyamine biosynthesis;    Putrescine;    Arabidopsis thaliana;    ADC;    arginine decarboxylase;    AIH;    agmatine iminohydrolase;    CPA;    N-carbamoylputrescine amidohydrolase;    ODC;    ornithine decarboxylase;   

DOI  :  10.1016/S0014-5793(03)00515-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown