Arginine<=>Agmatine+CO2

Stable Identifier
R-HSA-350598
Type
Reaction [transition]
Species
Homo sapiens
Compartment
cytosol
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Arginine<=>Agmatine+CO2
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Agmatine is polyamine formed by decarboxylation of L-arginine by arginine decarboxylase (ADC). Human ADC is a 460-amino acid protein that shows about 48% identity to mammalian ornithine decarboxylase (ODC) but has no ODC activity.

Literature References
PubMed ID Title Journal Year
14738999 Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine

Zhu, MY, Iyo, A, Piletz, JE, Regunathan, S

Biochim Biophys Acta 2004
Participants
Input
Output
Participant Of
hasEvent
Catalyst Activity
Catalyst Activity
Title
arginine decarboxylase activity of ADC [cytosol]
Physical Entity
ADC [cytosol]
Activity
arginine decarboxylase activity (0008792)
Orthologous Events
Arginine<=>Agmatine+CO2 (Bos taurus)
Arginine<=>Agmatine+CO2 (Caenorhabditis elegans)
Arginine<=>Agmatine+CO2 (Canis familiaris)
Arginine<=>Agmatine+CO2 (Danio rerio)
Arginine<=>Agmatine+CO2 (Dictyostelium discoideum)
Arginine<=>Agmatine+CO2 (Drosophila melanogaster)
Arginine<=>Agmatine+CO2 (Gallus gallus)
Arginine<=>Agmatine+CO2 (Mus musculus)
Arginine<=>Agmatine+CO2 (Plasmodium falciparum)
Arginine<=>Agmatine+CO2 (Rattus norvegicus)
Arginine<=>Agmatine+CO2 (Saccharomyces cerevisiae)
Arginine<=>Agmatine+CO2 (Schizosaccharomyces pombe)
Arginine<=>Agmatine+CO2 (Sus scrofa)
Arginine<=>Agmatine+CO2 (Xenopus tropicalis)
Cross References
Rhea
Authored
Gopinathrao, G  (2008-05-21)
Reviewed
D'Eustachio, P  (2008-06-12)