Adenosylhomocysteinase

Last updated
S-Adenosylhomocysteine hydrolase
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SAH hydrolase tetramer, Human
Identifiers
SymbolAHCY
NCBI gene 191
HGNC 343
OMIM 180960
RefSeq NM_000687
UniProt P23526
Other data
EC number 3.3.1.1
Locus Chr. 20 q11.22
Search for
Structures Swiss-model
Domains InterPro

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

Contents

S-adenosyl-L-homocysteine + H2O L-homocysteine + adenosine

The enzyme contains one tightly bound NAD+ per subunit. The mechanism involves dehydrogenative oxidation of the 3'-OH of the ribose. The resulting ketone is susceptible to α-deprotonation. The resulting carbanion eliminates thiolate. The a,b-unsaturated ketone is then hydrated, and the ketone is reduced by the NADH.

This enzyme is encoded by the AHCY gene in humans [3] [4] , which is believed to have a prognostic role in neuroblastoma. [5]

Related Research Articles

<i>S</i>-Adenosyl methionine Chemical compound found in all domains of life with largely unexplored effects

S-Adenosyl methionine (SAM), also known under the commercial names of SAMe, SAM-e, or AdoMet, is a common cosubstrate involved in methyl group transfers, transsulfuration, and aminopropylation. Although these anabolic reactions occur throughout the body, most SAM is produced and consumed in the liver. More than 40 methyl transfers from SAM are known, to various substrates such as nucleic acids, proteins, lipids and secondary metabolites. It is made from adenosine triphosphate (ATP) and methionine by methionine adenosyltransferase. SAM was first discovered by Giulio Cantoni in 1952.

<i>S</i>-Adenosyl-<small>L</small>-homocysteine Chemical compound

S-Adenosyl-L-homocysteine (SAH) is the biosynthetic precursor to homocysteine. SAH is formed by the demethylation of S-adenosyl-L-methionine. Adenosylhomocysteinase converts SAH into homocysteine and adenosine.

<span class="mw-page-title-main">Hypermethioninemia</span> Medical condition

Hypermethioninemia is an excess of the amino acid methionine, in the blood. This condition can occur when methionine is not broken down properly in the body.

In enzymology, a carnosine N-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Guanidinoacetate N-methyltransferase</span> Mammalian protein found in Homo sapiens

Guanidinoacetate N-methyltransferase is an enzyme that catalyzes the chemical reaction and is encoded by gene GAMT located on chromosome 19p13.3.

<span class="mw-page-title-main">Magnesium protoporphyrin IX methyltransferase</span>

In enzymology, a magnesium protoporphyrin IX methyltransferase is an enzyme that catalyzes the chemical reaction

mRNA (guanine-N7-)-methyltransferase

In enzymology, a mRNA (guanine-N7-)-methyltransferase also known as mRNA cap guanine-N7 methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a mRNA (nucleoside-2'-O-)-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a phosphatidyl-N-methylethanolamine N-methyltransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a precorrin-4 C11-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Protein-glutamate O-methyltransferase</span>

In enzymology, a protein-glutamate O-methyltransferase is an enzyme that catalyzes the chemical reaction

The isoprenylcysteine o-methyltransferase carries out carboxyl methylation of cleaved eukaryotic proteins that terminate in a CaaX motif. In Saccharomyces cerevisiae this methylation is carried out by Ste14p, an integral endoplasmic reticulum membrane protein. Ste14p is the founding member of the isoprenylcysteine carboxyl methyltransferase (ICMT) family, whose members share significant sequence homology.

In enzymology, a tRNA guanosine-2'-O-methyltransferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">NME1</span> Protein-coding gene in the species Homo sapiens

Nucleoside diphosphate kinase A is an enzyme that in humans is encoded by the NME1 gene. It is thought to be a metastasis suppressor.

In enzymology, an adenosylhomocysteine nucleosidase (EC 3.2.2.9) is an enzyme that catalyzes the chemical reaction

In enzymology, a S-adenosylhomocysteine deaminase (EC 3.5.4.28) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">DPYSL3</span> Protein-coding gene in the species Homo sapiens

Dihydropyrimidinase-related protein 3 is an enzyme that in humans is encoded by the DPYSL3 gene. A recent bioinformatics study suggested that the DPYSL3 gene might have a prognostic role in neuroblastoma.

<span class="mw-page-title-main">MYO1E</span> Protein-coding gene in the species Homo sapiens

Myosin-Ie (Myo1e) is a protein that in humans is encoded by the MYO1E gene.

<span class="mw-page-title-main">S-adenosyl-L-homocysteine hydrolase</span>

S-adenosyl-L-homocysteine hydrolase (AdoHcyase) is an enzyme of the activated methyl cycle, responsible for the reversible hydration of S-adenosyl-L-homocysteine into adenosine and homocysteine.

Diadenosine hexaphosphate hydrolase (AMP-forming) (EC 3.6.1.60, hAps1, NUDT11 (gene), hAps2, NUDT10 (gene)) is an enzyme with systematic name P1,P6-bis(5'-adenosyl)hexaphosphate nucleotidohydrolase (AMP-forming). This enzyme catalyses the following chemical reaction

References

  1. 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. doi: 10.1016/S0021-9258(18)70253-6 . PMID   13641268.
  2. Palmer JL, Abeles RH (February 1979). "The mechanism of action of S-adenosylhomocysteinase". The Journal of Biological Chemistry. 254 (4): 1217–26. doi: 10.1016/S0021-9258(17)34190-X . PMID   762125.
  3. GeneCards.org - AHCY Gene - Adenosylhomocysteinase
  4. NLM - AHCY adenosylhomocysteinase
  5. Chicco, Davide; Sanavia, Tiziana; Jurman, Giuseppe (4 March 2023). "Signature literature review reveals AHCY, DPYSL3, and NME1 as the most recurrent prognostic genes for neuroblastoma". BioData Mining. 16 (1). doi:10.1186/s13040-023-00325-1. eISSN   1756-0381. PMC   9985261 . PMID   36870971.

Further reading