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4.1.1.50: adenosylmethionine decarboxylase

This is an abbreviated version!
For detailed information about adenosylmethionine decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.50

Reaction

S-adenosyl-L-methionine
=
S-adenosyl 3-(methylsulfanyl)propylamine
+
CO2

Synonyms

Ado-MetDC, AdoMet decarboxylase, AdoMetDC, AdoMetDC/ODC, AMDC, BjSAMDC1, BjSAMDC2, BjSAMDC3, BjSAMDC4, BlsE, Bud2, MdSAMDC1, MdSAMDC2, OsSAMDC, PfAdoMetDC, protein SSO0585, S-adenosyl methionine decarboxylase, S-Adenosyl-L-methionine decarboxylase, S-adenosyl-methionine-decarboxylase, S-adenosylmethionine decarboxy-lase/ornithine decarboxylase, S-Adenosylmethionine decarboxylase, S-adenosylmethionine decarboxylase 1, S-adenosylmethionine decarboxylase 2, S-adenosylmethionine decarboxylase 3, S-adenosylmethionine decarboxylase 4, SAM decarboxylase, SAM-DC, SAMDC, SvPEPC, Tb927.6.4410

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.50 adenosylmethionine decarboxylase

Application

Application on EC 4.1.1.50 - adenosylmethionine decarboxylase

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
-
incubation of the cut flower with water increases both enzyme activity and spermine content 2fold, which are followed by ethylene production. Reaction may be a resistance mechanism against fungal and bacterial infection. Overexpression of enzyme may be a tool to improve rose cultivars for the common usage
analysis
-
development of a simple, economic, and non-radioactive spectrometric enzymatic assay, which can be adapted for experimental high-throughput screening of AdoMetDC inhibitors
biotechnology
overexpression of enzyme is sufficient for accumulation of spermidine in leaves and spermidine and spermine in seeds
medicine
pharmacology
synthesis
coexpression of S-adenosylmethionine decarboxylase with chimeric protein KPf, which is made up of the ATPase domain of Escherichia coli DnaK and the substrate binding domain of Plasmodium falciparum Hsp70, and DnaK in Escherichia coli cells. The recombinant protein exhibits improved activity compared to protein coexpressed with overexpressed DnaK