Theoretical study of the methyl transfer in guanidinoacetate methyltransferase
2006 (English)In: Journal of Physical Chemistry B, ISSN 1520-6106, E-ISSN 1520-5207, Vol. 110, no 1, 16-19 p.Article in journal (Refereed) Published
The reaction mechanism of the guanidinoacetate methyltransferase (GAMT) enzyme has been investigated by means of density functional theory using the B3LYP hybrid functional. GAMT catalyzes the S-adenosyl-l-methionine (SAM)-dependent methylation of guanidinoacetate (GAA) to form creatine. A quantum chemical model was built on the basis of the recent crystal structure of GAMT complexed with S-adenosylhomocysteine (SAH) and GAA. The methyl group transfer from SAM to NE of GAA is shown to occur concertedly with a proton transfer from NE to the neighboring OD1 of Asp134. Good agreement is found between the calculated barrier and the experimental rate.
Place, publisher, year, edition, pages
2006. Vol. 110, no 1, 16-19 p.
Catalysis; Crystal structure; Enzymes; Hybrid computers; Probability density function; Propylene; Structural analysis; Creatine; Guanidinoacetate methyltransferase; Methylation; S-adenosylhomocysteine (SAH)
IdentifiersURN: urn:nbn:se:kth:diva-5571DOI: 10.1021/jp055120dISI: 000234520700006OAI: oai:DiVA.org:kth-5571DiVA: diva2:9980
QC 201007272008-12-042008-12-042010-09-27Bibliographically approved