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

Topic mentions per year

Topic mentions per year

1975-2017
0102019752017

Papers overview

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2008
2008
Putrescine (1,4-diaminobutane) activates the autoprocessing and decarboxylation reactions of human S-adenosylmethionine… (More)
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2007
2007
The production of polyamines has been shown to be an effective target for a drug against the West African form of sleeping… (More)
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Highly Cited
2006
Highly Cited
2006
Polyamines (PAs), such as putrescine, spermidine, and spermine, are present in all living organism and implicate in a wide range… (More)
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2006
2006
The present study was designed to provide a better understanding of the role played by AdoMetDC (S-adenosylmethionine… (More)
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2003
2003
S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl-dependent enzyme that catalyzes the formation of the aminopropyl… (More)
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2002
2002
S-Adenosylmethionine decarboxylase (AdoMetDC) is a key enzyme in polyamine biosynthesis. We show that the plant AdoMetDC activity… (More)
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2000
2000
Differences in gene expression between salinity-stressed and normally grown rice seedlings were compared by using the… (More)
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2000
2000
The polyamines putrescine, spermidine, and spermine are crucial for cell differentiation and proliferation. Interference with… (More)
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1997
1997
S-Adenosylmethionine decarboxylase (AdoMetDC) is a pyruvoyl enzyme, and the pyruvate is formed in an intramolecular reaction that… (More)
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Highly Cited
1994
Highly Cited
1994
The mRNAs for two key enzymes in polyamine biosynthesis, ornithine decarboxylase (ODC) and S-adenosylmethionine decarboxylase… (More)
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