InterPro domain: IPR017754

Agmatine deiminase ( 3.5.3.12 ) catalyses the conversion of agmatine into N-carbamoylputrescine. This enzyme usually functions as part of polyamine biosynthesis, though in some bacterial species, such as Enterococcus faecalis, it can also function in the generation of ATP from agmatine [ 1 , 2 , 3 ]. The E. faecalis enzyme is a homotetramer where each monomer adopts a similar fold to that of the arginine deiminase catalytic domain, a five-bladed fan-like structure where the repeating unit is formed from three beta sheets and an alpha helix [ 4 ].

This entry represents known and putative agmatine deiminases from bacteria and plants. Related deiminases not in this entry include the peptidyl-arginine deiminase ( 3.5.3.15 ) as found in Porphyromonas gingivalis.

1. Identification and characterization of plant agmatine iminohydrolase, the last missing link in polyamine biosynthesis of plants. FEBS Lett. 544, 258-61
2. Identification of the putrescine biosynthetic genes in Pseudomonas aeruginosa and characterization of agmatine deiminase and N-carbamoylputrescine amidohydrolase of the arginine decarboxylase pathway. Microbiology (Reading, Engl.) 149, 707-14
3. Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis. J. Bacteriol. 152, 676-81
4. The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction. J. Bacteriol. 189, 1254-65