RGD Reference Report - Synthetic decarboxylated S-adenosyl-L-methionine as a substrate for aminopropyl transferases. - Rat Genome Database

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Synthetic decarboxylated S-adenosyl-L-methionine as a substrate for aminopropyl transferases.

Authors: Dejima, H  Kobayashi, M  Takasaki, H  Takeda, N  Shirahata, A  Samejima, K 
Citation: Dejima H, etal., Biol Pharm Bull 2003 Jul;26(7):1005-8.
RGD ID: 1359042
Pubmed: PMID:12843627   (View Abstract at PubMed)

Synthetic decarboxylated S-adenosyl-L-methionine (dcAdoMet), a mixture of the absolute configuration of S and R at the sulfonium center, was evaluated as a substrate for the measurement of spermidine synthase activity. The diastereomers were separated by HPLC with an isocratic elution, and the constant for racemization at the sulfur was determined to be 2.4x10(-6) s(-1) at 37 degrees C and pH 1.5 for the first-eluted biologically active isomer (S-dcAdoMet) and 2.0x10(-6) s(-1) for the second-eluted biologically inactive isomer (R-dcAdoMet). The peak area ratio of S-dcAdoMet to R-dcAdoMet of 48 to 52 in HPLC supported the different racemization constants. Similar substrate activity of dcAdoMet to that of S-dcAdoMet was demonstrated by enzymatic spermidine synthesis. It was shown from the result that the racemized [methyl-(14)C]dcAdoMet prepared in this report was useful for measuring spermidine synthase activity.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
SrmRatspermidine biosynthetic process  IDA  RGD 

Molecular Function

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
SrmRatspermidine synthase activity  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Srm  (spermidine synthase)


Additional Information