S-adenosylhomocysteine hydrolase

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<StructureSection load='1xwf' size='450' side='right' caption='Structure of rat S-adenosylhomocysteine hydrolase tetramer complex with NAD and adenine (PDB entry [[1xwf]])' scene='55/552186/Cv/1'>
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<StructureSection load='' size='350' side='right' caption='Structure of rat S-adenosylhomocysteine hydrolase tetramer complex with NAD and adenine (PDB entry [[1xwf]])' scene='55/552186/Cv/1'>
== Function ==
== 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<ref>PMID:15488656</ref>.
'''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<ref>PMID:15488656</ref>.
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== Structural highlights ==
== Structural highlights ==
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The biological assembly of rat S-adenosylhomocysteine hydrolase is <scene name='55/552186/Cv/2'>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>.
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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>
</StructureSection>
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**[[3gvp]] – hAHCH SAHH-like domain + NAD <BR />
**[[3gvp]] – hAHCH SAHH-like domain + NAD <BR />
**[[3d64]] – BpAHCH + NAD – ''Burkholderia pseudmallei''<BR />
**[[3d64]] – BpAHCH + NAD – ''Burkholderia pseudmallei''<BR />
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**[[3x2f]] – AHCH + NADH – ''Thermotoga maritima''<BR />
*S-adenosylhomocysteine hydrolase complex with adenosine derivatives
*S-adenosylhomocysteine hydrolase complex with adenosine derivatives
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**[[3one]] – lAHCH + NAD + adenine <BR />
**[[3one]] – lAHCH + NAD + adenine <BR />
**[[3onf]] – lAHCH + NAD + adenosine derivative <BR />
**[[3onf]] – lAHCH + NAD + adenosine derivative <BR />
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**[[5m66]] – BeAHCH + NAD + adenosine – ''Bradyrhizobium elkanii''<BR />
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**[[5m5k]] – BeAHCH + NAD + adenosine + cordycepin<BR />
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**[[5m67]] – BeAHCH + NAD + adenosine + deoxyadenine<BR />
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**[[3g1u]] – AHCH + NAD + adenosine – ''Leishmania major''<BR />
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*S-adenosylhomocysteine hydrolase other complexes
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**[[5w49]], [[5w4b]] – hAHCH + NAD + inhibitor<BR />
}}
}}
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]
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[[Category:One-carbon metabolism]]

Current revision

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

Drag the structure with the mouse to rotate

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

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Michal Harel, Alexander Berchansky, Karsten Theis, Joel L. Sussman

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