S-adenosylhomocysteine hydrolase

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Revision as of 12:36, 1 September 2019

Structure of rat S-adenosylhomocysteine hydrolase tetramer complex with NAD and adenine (PDB entry 1xwf)

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Updated on 01-September-2019

↑ 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
↑ 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
↑ 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

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 == Structural highlights ==
-The biological assembly of rat S-adenosylhomocysteine hydrolase is <scene name='55/552186/Cv/5'>homotetramer</scene>. AHCH structure contains <scene name='55/552186/Cv/3'>3 domains: catalytic, NAD-binding and C-terminal domain</scene>.  The <scene name='55/552186/Cv/4'>active site is located in a cleft between the catalytic domain and the NAD-binding domain and it contains the cofactor NAD and the product adenine</scene><ref>PMID:16061414</ref>.
+The biological assembly of rat S-adenosylhomocysteine hydrolase is <scene name='55/552186/Cv/6'>homotetramer</scene>. AHCH structure contains <scene name='55/552186/Cv/7'>3 domains: catalytic, NAD-binding and C-terminal domain</scene>. The <scene name='55/552186/Cv/8'>active site is located in a cleft between the catalytic domain and the NAD-binding domain and it contains the cofactor NAD and the product adenine</scene><ref>PMID:16061414</ref>.
 </StructureSection>