| 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 homotetramer. AHCH structure contains 3 domains: catalytic, NAD-binding and C-terminal domain. The 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[3].
- ↑ 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:https://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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3D structures of S-adenosylhomocysteine hydrolase
Updated on 14-November-2023
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- S-adenosylhomocysteine hydrolase
- 1ky4 – rAHCH + NAD - rat
- 1ky5 – rAHCH (mutant) + NAD
- 1b3r – rAHCH catalytic domain + NAD
- 1a7a – hAHCH + NAD – human
- 3gvp – hAHCH SAHH-like domain + NAD
- 3d64 – BpAHCH + NAD – Burkholderia pseudmallei
- 3x2f – AHCH + NADH – Thermotoga maritima
- S-adenosylhomocysteine hydrolase complex with adenosine derivatives
- 1d4f, 1xwf – rAHCH (mutant) + NAD + adenosine
- 1k0u, 2h5l – rAHCH + NAD + adenosine analog
- 1li4, 3nj4 – hAHCH + NAD + adenosine derivative
- 1v8b – AHCH + NAD + adenosine – Plasmodium falciparum
- 3dhy, 2ziz, 2zj0, 2zj1 – MtAHCH + NAD + adenosine derivative – Mycobacterium tuberculosis
- 3ce6 – MtAHCH + NAD + adenosine
- 3glq – BpAHCH + NAD + adenosine derivative
- 3n58 – AHCH + NAD + adenosine – Brucella melitensis
- 3ond – lAHCH + NAD + adenosine – lupin
- 3one – lAHCH + NAD + adenine
- 3onf – lAHCH + NAD + adenosine derivative
- 5m66 – BeAHCH + NAD + adenosine – Bradyrhizobium elkanii
- 5m5k – BeAHCH + NAD + adenosine + cordycepin
- 5m67 – BeAHCH + NAD + adenosine + deoxyadenine
- 3g1u – AHCH + NAD + adenosine – Leishmania major
- S-adenosylhomocysteine hydrolase other complexes
References
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