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Conformational stabilization of rat s-adenosylmethionine decarboxylase by putrescine.

Authors: Wada, M  Shirahata, A 
Citation: Wada M and Shirahata A, Biol Pharm Bull. 2010;33(11):1800-5.
Pubmed: (View Article at PubMed) PMID:21048303

The activity and processing of mammalian S-adenosylmethionine decarboxylase (AdoMetDC) is stimulated by putrescine. To obtain new insights into the mechanism through which putrescine stimulates AdoMetDC, we investigated conformational changes in rat prostate AdoMetDC in the presence or absence of putrescine. We examined the reactivity of purified rat prostate AdoMetDC to the SH-reagent iodoacetic acid (IAA) and its susceptibility to proteolysis in the presence or absence of putrescine using matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS). The activity of AdoMetDC treated with IAA in the absence of putrescine was reduced, but about 80% of its activity remained after treatment with IAA in the presence of putrescine. In the presence of putrescine, IAA incorporation was 1.9 mol IAA/mol of AdoMetDC alpha-subunit, while there was no incorporation of IAA in the beta-subunit of AdoMetDC. In the absence of putrescine, 5.0 mol of IAA/mol of alpha-subunit and 0.9 mol of IAA/mol of beta-subunit were incorporated. Only Cys292 and Cys310 were carboxymethylated by IAA in the presence of putrescine. In contrast, in the absence of putrescine all cysteines were carboxymethylated by IAA. In addition, putrescine slowed the rate of AdoMetDC degradation by trypsin. These results demonstrate that the conformation of AdoMetDC purified from rat prostate is stabilized by putrescine.

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CRRD Object Information
CRRD ID: 7242909
Created: 2013-04-25
Species: All species
Last Modified: 2013-04-25
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.