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S-Adenosylmethionine Decarboxylase Proenzyme

Known as: AdoMetDC, S-Adenosylmethionine Decarboxylase 1, SAMDC 
S-adenosylmethionine decarboxylase proenzyme (334 aa, ~38 kDa) is encoded by the human AMD1 gene. This protein is involved in polyamine metabolism.
National Institutes of Health

Papers overview

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Highly Cited
2014
Highly Cited
2014
Switchgrass (Panicum virgatum) has received a lot of attention as a forage and bioenergy crop during the past few years. Gene… 
Review
2011
Review
2011
Polyamines (PAs) are essential metabolites in eukaryotes, participating in a variety of proliferative processes, and in… 
Highly Cited
2008
Highly Cited
2008
Polyamines (PAs) exert a protective effect against stress challenges, but their molecular role in this remains speculative. In… 
Highly Cited
2008
Highly Cited
2008
In an attempt to understand the molecular basis of salt-stress response in the aromatic rice Gobindobhog, a comprehensive… 
Highly Cited
2006
Highly Cited
2006
Polyamines are implicated in regulating various developmental processes in plants, but their exact roles and how they govern… 
Review
2003
Review
2003
As soon as the natural polyamines (PAs), putrescine (Put), spermidine (Spd) and spermine (Spm), were recognized as ubiquitous… 
Highly Cited
2002
Highly Cited
2002
Treatment of the first leaves of barley (Hordeum vulgare L. cv. Golden Promise) seedlings with methyl jasmonate (MJ) led to small… 
Highly Cited
2001
Highly Cited
2001
Synthesis of S-adenosylmethionine decarboxylase (AdoMetDC), a key regulated enzyme in the pathway of polyamine biosynthesis, is… 
Highly Cited
1994
Highly Cited
1994
The mRNAs for two key enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase…