S-adenosylhomocysteine hydrolase

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<StructureSection load='3d64' size='350' side='right' caption='Structure of S-adenosylhomocysteine hydrolase dimer complex with NAD (PDB entry [[3d64]])' scene=''>
<StructureSection load='3d64' size='350' side='right' caption='Structure of S-adenosylhomocysteine hydrolase dimer complex with NAD (PDB entry [[3d64]])' scene=''>
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'''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.
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'''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>.
</StructureSection>
</StructureSection>
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**[[3onf]] – lAHCH + NAD + adenosine derivative <BR />
**[[3onf]] – lAHCH + NAD + adenosine derivative <BR />
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 07:16, 21 August 2016

Structure of S-adenosylhomocysteine hydrolase dimer complex with NAD (PDB entry 3d64)

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3D structures of S-adenosylhomocysteine hydrolase

Updated on 21-August-2016

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

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