Adenosylhomocysteinase: Difference between revisions
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{{protein | {{protein | ||
|Name=S- | |Name=''S''-Adenosylhomocysteine hydrolase | ||
|caption=SAH hydrolase tetramer, Human | |caption=SAH hydrolase tetramer, Human | ||
|image=1li4.jpg | |image=1li4.jpg | ||
| Line 18: | Line 18: | ||
|LocusSupplementaryData= | |LocusSupplementaryData= | ||
}} | }} | ||
'''Adenosylhomocysteinase''' ({{EC number|3.3.1.1}}, ''S-adenosylhomocysteine synthase'' | '''Adenosylhomocysteinase''' ({{EC number|3.3.1.1}}, ''S''-adenosylhomocysteine synthase, ''S''-adenosylhomocysteine hydrolase, adenosylhomocysteine hydrolase, ''S''-adenosylhomocysteinase, SAHase, AdoHcyase) is an enzyme that converts [[S-adenosylhomocysteine|''S''-adenosylhomocysteine]] to [[homocysteine]] and [[adenosine]].<ref>{{cite journal | vauthors = De La Haba G, Cantoni GL | title = The enzymatic synthesis of ''S''-adenosyl-<small>L</small>-homocysteine from adenosine and homocysteine | journal = The Journal of Biological Chemistry | volume = 234 | issue = 3 | pages = 603–8 | date = March 1959 | pmid = 13641268 }}</ref><ref>{{cite journal | vauthors = Palmer JL, Abeles RH | title = The mechanism of action of ''S''-adenosylhomocysteinase | journal = The Journal of Biological Chemistry | volume = 254 | issue = 4 | pages = 1217–26 | date = February 1979 | pmid = 762125 }}</ref> This enzyme [[catalysis|catalyses]] the following [[chemical reaction]] | ||
: [[S-adenosyl-L-homocysteine]] + H<sub>2</sub>O < | : [[S-adenosyl-L-homocysteine|''S''-adenosyl-<small>L</small>-homocysteine]] + H<sub>2</sub>O {{eqm}} <small>L</small>-[[homocysteine]] + [[adenosine]] | ||
The enzyme contains one tightly bound NAD<sup>+</sup> per subunit. | The enzyme contains one tightly bound NAD<sup>+</sup> per subunit. | ||
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{{reflist}} | {{reflist}} | ||
==External links== | == External links == | ||
* {{MeshName|Adenosylhomocysteinase}} | * {{MeshName|Adenosylhomocysteinase}} | ||
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{{Enzymes}} | {{Enzymes}} | ||
{{Portal bar|Molecular and Cellular Biology|border=no}} | {{Portal bar|Molecular and Cellular Biology|border=no}} | ||
[[Category:EC 3.3.1]] | [[Category:EC 3.3.1]] | ||
Revision as of 17:38, 21 September 2018
| S-Adenosylhomocysteine hydrolase | |
|---|---|
| File:1li4.jpg SAH hydrolase tetramer, Human | |
| Identifiers | |
| Symbol | AHCY |
| Entrez | 191 |
| HUGO | 343 |
| OMIM | 180960 |
| RefSeq | NM_000687 |
| UniProt | P23526 |
| Other data | |
| EC number | 3.3.1.1 |
| Locus | Chr. 20 q11.22 |
Adenosylhomocysteinase (EC 3.3.1.1, S-adenosylhomocysteine synthase, S-adenosylhomocysteine hydrolase, adenosylhomocysteine hydrolase, S-adenosylhomocysteinase, SAHase, AdoHcyase) is an enzyme that converts S-adenosylhomocysteine to homocysteine and adenosine.[1][2] This enzyme catalyses the following chemical reaction
- S-adenosyl-L-homocysteine + H2O ⇌ L-homocysteine + adenosine
The enzyme contains one tightly bound NAD+ per subunit.
References
- ↑ De La Haba G, Cantoni GL (March 1959). "The enzymatic synthesis of S-adenosyl-L-homocysteine from adenosine and homocysteine". The Journal of Biological Chemistry. 234 (3): 603–8. PMID 13641268.
- ↑ Palmer JL, Abeles RH (February 1979). "The mechanism of action of S-adenosylhomocysteinase". The Journal of Biological Chemistry. 254 (4): 1217–26. PMID 762125.
External links
- Adenosylhomocysteinase at the US National Library of Medicine Medical Subject Headings (MeSH)