Literature summary for 2.1.1.2 extracted from

Zhang, X.; Bruice, T.C.
Reaction mechanism of guanidinoacetate methyltransferase, concerted or step-wise (2006), Proc. Natl. Acad. Sci. USA, 103, 16141-16146.

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Organism

Organism	UniProt	Comment	Textmining
Rattus norvegicus	P10868	recombinant enzyme	-

Reaction

Reaction	Comment	Organism	Reaction ID
S-adenosyl-L-methionine + guanidinoacetate = S-adenosyl-L-homocysteine + creatine	computer model of the reaction mechanism: by self-consistent-charge density functional tight binding/molecular mechanics, the bond lengths in the concerted mechanisms transition state is 1.26 A for both the OD1 (Asp-134)-HE (guanidinoacetate) and HE (guanidinoacetate)-NE (guanidinoacetate) bonds, and 2.47 and 2.03 A for the S8 (S-adenosyl-L-methionine)-C9 (S-adenosyl-L-methionine) and C9 (S-adenosyl-L-methionine)-NE (guanidinoacetate) bonds, respectively. The potential-energy barrier (delta E++) determined by single-point B3LYP/6-31+G*//MM is 18.9 kcal/mol. The contributions of the entropy (-TdeltaS++) and zero-point energy corrections delta(ZPE)++ by normal mode analysis are 2.3 kcal/mol and -1.7 kcal/mol, respectively. The activation enthalpy of this concerted mechanism is deltaH++ = 17.2 kcal/mol. The calculated free-energy barrier for the concerted mechanism is deltaG++ = 19.5 kcal/mol.	Rattus norvegicus	a

Source Tissue

Source Tissue	Comment	Organism	Textmining
liver	-	Rattus norvegicus	-

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Release 2023.1 (January 2023)