S-adenosyl-L-homocysteine hydrolase
| S-adenosyl-L-homocysteine hydrolase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of S-adenosylhomocysteine hydrolase from rat liver.[1] | |||||||||
| Identifiers | |||||||||
| Symbol | Ad_hcy_hydrolase | ||||||||
| Pfam | PF05221 | ||||||||
| InterPro | IPR000043 | ||||||||
| PROSITE | PDOC00603 | ||||||||
| SCOP | 1b3r | ||||||||
| SUPERFAMILY | 1b3r | ||||||||
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| AdoHcyase NAD-binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 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 | ||||||||
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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
- ↑ 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.
- ↑ 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 49494. PMID 1631127.
- ↑ T. Selwood and 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 3298769. PMID 22182754.
This article incorporates text from the public domain Pfam and InterPro IPR000043
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