Properties of Human and Rodent S-Adenosylmethionine Decarboxylase

The Pivotal Roles of the Plant S-Adenosylmethionine Decarboxylase 5′ Untranslated Leader Sequence in Regulation of Gene Expression at the Transcriptional and Posttranscriptional Levels

“…The presence of introns is necessary for the SAMDC up-regulation process when the internal spermidine level is low. Our results suggest that plants have evolved one network to adjust SAMDC activity through their 5# leader sequences, through which transcriptional regulation is combined with an extensive posttranscriptional control circuit.S-Adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key enzyme in higher polyamine (PA) biosynthesis (Janne et al, 1978;Pegg et al, 1988). An understanding of how SAMDC genes are regulated is important for elucidating the molecular basis of PA biosynthesis and the role of PAs in plant growth and development.…”

“…Similarly, information regarding transcriptional regulation of SAMDC also was limited. As plant SAMDCs turn over very rapidly in vivo (Pegg et al, 1988), we posed the questions of whether and how their unique 5# untranslated leader sequences regulate SAMDC activity in general.By isolating SAMDC genes from the mustard (Brassica juncea) cDNA library, we found that SAMDC in mustard is encoded by a gene family, which was further confirmed by Southern analysis. All these members showed similar expression patterns when mustard was treated with external stimuli.…”

“…S-Adenosylmethionine decarboxylase (SAMDC; EC 4.1.1.50) is a key enzyme in higher polyamine (PA) biosynthesis (Janne et al, 1978;Pegg et al, 1988). An understanding of how SAMDC genes are regulated is important for elucidating the molecular basis of PA biosynthesis and the role of PAs in plant growth and development.…”

Identification of the Primary Structure and Post-translational Modification of Rat S-Adenosylmethionine Decarboxylase

“…11) Two apparently different forms of AdoMetDC have been purified from rat liver and rat psoas muscle, with differences observed in isoelectric point (pI), extent of activation by putrescine, S-adenosylmethionine substrate K m , and methylglyoxal bis(guanyl)hydrazone affinity, 12) suggesting differences in post-translational modification. 5) In addition, no amino terminal residue could be detected when either the bovine 11) or rat enzyme was subjected to Edman degradation, suggesting that the b-subunit must be blocked by modification, 13) since the pyruvate residue is located at the a-subunit amino terminus.…”

Overproduction of S‐adenosylmethionine decarboxylase in ethylglyoxal‐bis(guanylhydrazone)‐resistant mouse FM3A cells

“…Its product, decarboxylated S-adenosylmethionine, serves as an amino propyl donor in spermidine and spennine synthesis [l, 21. The activity of AdoMetDC is regulated negatively by spermidine and spermine [3], and polyamine depletion leads to an increase in the amount of AdoMetDC protein, caused by both a decreased rate of degradation and an increased rate of synthesis. The increased synthesis has been shown to be partly due to an enhanced translational efficiency [4].…”