S-adenosyl-L-homocysteine hydrolase

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S-adenosyl-L-homocysteine hydrolase
PDB 1b3r EBI.jpg
Structure of S-adenosylhomocysteine hydrolase from rat liver.[1]
Identifiers
Symbol Ad_hcy_hydrolase
Pfam PF05221
InterPro IPR000043
PROSITE PDOC00603
SCOP 1b3r
SUPERFAMILY 1b3r
AdoHcyase NAD-binding domain
PDB 1ky5 EBI.jpg
d244e mutant s-adenosylhomocysteine hydrolase refined with noncrystallographic restraints
Identifiers
Symbol AdoHcyase_NAD
Pfam PF00670
Pfam clan CL0063
InterPro IPR015878
PROSITE PDOC00603
SCOP 1b3r
SUPERFAMILY 1b3r

S-adenosyl-L-homocysteine hydrolase (EC 3.3.1.1) (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine.

AdoHcyase is a ubiquitous enzyme which binds and requires NAD+ as a cofactor. AdoHcyase is a highly conserved protein[2] of about 430 to 470 amino acids. The family contains a glycine-rich region in the central part of AdoHcyase; a region thought to be involved in NAD-binding.

This protein may use the morpheein model of allosteric regulation.[3]

References[edit]

  1. ^ Hu Y, Komoto J, Huang Y, et al. (June 1999). "Crystal structure of S-adenosylhomocysteine hydrolase from rat liver". Biochemistry. 38 (26): 8323–33. doi:10.1021/bi990332k. PMID 10387078. 
  2. ^ Sganga MW, Aksamit RR, Cantoni GL, Bauer CE (1992). "Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus". Proc. Natl. Acad. Sci. U.S.A. 89 (14): 6328–6332. doi:10.1073/pnas.89.14.6328. PMC 49494Freely accessible. PMID 1631127. 
  3. ^ T. Selwood; E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769Freely accessible. PMID 22182754. 

This article incorporates text from the public domain Pfam and InterPro IPR000043