S-adenosylhomocysteine hydrolase

From Proteopedia

spinqualitylabelsall models Structure of rat S-adenosylhomocysteine hydrolase tetramer complex with NAD and adenine (PDB entry 1xwf) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function S-adenosylhomocysteine hydrolase (AHCH) converts S-adenosylhomocysteine (AdoHcy) to L-homocysteine and adenosine. AHCH uses NAD+ as cofactor. AHCH is an essential enzyme in processes like transmethylation, trans-sulfuration and purine metabolism[1]. Disease AHCH deficiency causes a genetic disorder of methionine metabolism[2]. Structural highlights The biological assembly of rat S-adenosylhomocysteine hydrolase is . AHCH structure contains . The [3].

3D structures of S-adenosylhomocysteine hydrolase

Updated on 14-November-2023

References

1. ↑ Altintas E, Sezgin O. S-adenosylhomocysteine hydrolase, S-adenosylmethionine, S-adenosylhomocysteine: correlations with ribavirin induced anemia. Med Hypotheses. 2004;63(5):834-7. PMID:15488656 doi:http://dx.doi.org/10.1016/j.mehy.2004.03.031
2. ↑ Baric I, Fumic K, Glenn B, Cuk M, Schulze A, Finkelstein JD, James SJ, Mejaski-Bosnjak V, Pazanin L, Pogribny IP, Rados M, Sarnavka V, Scukanec-Spoljar M, Allen RH, Stabler S, Uzelac L, Vugrek O, Wagner C, Zeisel S, Mudd SH. S-adenosylhomocysteine hydrolase deficiency in a human: a genetic disorder of methionine metabolism. Proc Natl Acad Sci U S A. 2004 Mar 23;101(12):4234-9. Epub 2004 Mar 15. PMID:15024124 doi:10.1073/pnas.0400658101
3. ↑ Yamada T, Takata Y, Komoto J, Gomi T, Ogawa H, Fujioka M, Takusagawa F. Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89. Int J Biochem Cell Biol. 2005 Nov;37(11):2417-35. PMID:16061414 doi:10.1016/j.biocel.2005.06.009