Sandbox GGC2

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Function

Normally, enzyme is responsible for the synthesis of methionine from the process of transfering a methyl group methyl-cobalamin to homocysteine. The resulting product along with the synthesized methionine is a enzyme-bound cob(I)alamin.

Relevance

Structural highlights

Human methonine synthase exist in a dimeric form which can be seen in , which is different compared to other organism such as E. coli. Ultimately, the structural surface of the enzyme is C-shape which includes 2 polypeptide chains in a specific twisted anti-parallel beta sheet with a beta meander region. of the protein shows that the exterior consists of mainly alpha helices, and the interior consist of mainly beta sheets. This activation domain interacts with the FMN-binding domain of human methionine synthase reductase (hMSR), and the interaction has higher affinity in the presence of the substrate, S-adenosyl-methionine. In the mutant strain, the , D963E and K1071N, weakens the binding between the active domain of the human methionine synthase and human methionine synthase reductase. The active site with the residues are key for the partner binding because it plays a major role n forming reactivation complexes and dimer formation.