Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89.
Yamada T, Takata Y, Komoto J, Gomi T, Ogawa H, Fujioka M, Takusagawa F.
Yamada T, et al. Among authors: ogawa h.
Int J Biochem Cell Biol. 2005 Nov;37(11):2417-35. doi: 10.1016/j.biocel.2005.06.009.
Int J Biochem Cell Biol. 2005.
PMID: 16061414
The crystal structure of the K185N mutated enzyme, which has weak catalytic activity (0.1%), has been determined at 2.8 A resolution and supports the previously predicted mechanism [Takata, Y., Yamada, T., Huang, Y., Komoto, J., Gomi, T., Ogawa, H., Fujioka, M., &am …
The crystal structure of the K185N mutated enzyme, which has weak catalytic activity (0.1%), has been determined at 2.8 A resolution and sup …