Primary Information |
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BoMiProt ID | Bomi344 |
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Protein Name | Adenosylhomocysteinase |
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Organism | Bos taurus |
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Uniprot ID | Q3MHL4 |
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Milk Fraction | MFGM, Exosome |
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Ref Sequence ID | NP_001029487.1 |
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Aminoacid Length | 432 |
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Molecular Weight | 47638 |
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FASTA Sequence |
Download |
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Gene Name | AHCY |
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Gene ID | 508158 |
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Protein Existence Status | Reviewed: Experimental evidence at transcript level |
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Secondary Information |
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Protein Function | S-Adenosylhomocysteinase catalyzes the reversible
hydrolysis of S-adenosyl-L-homocysteine (AdoHcy) to
adenosine and L-homocysteine without added cofactors; enzyme catalyzes
the exchange of the 4’-proton of substrate with solvent |
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Biochemical Properties | enzyme contains 1 tightly bound
NAD+ per subunit; the enzyme’s
sedimentation coefficient was determined at 60,000 rpm, 20°C
in 10 mM K+ phosphate, 1 mM KEDTA, 0.2 mu DTT, pH 7.0; Km values for AdoHcy and adenosine are 10.5
pM and 45 PM, respectively; substrate inhibition occurs at high
concentrations of AdoHcy; this inhibition is increased by 5’-
deoxyadenosine, an inhibitor of the enzyme; 4’,5’-dehydroadenosine is added to the enzyme, there
is a slow increase in the 327 nm absorption consistent with
substrate oxidation and NADH formation |
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PTMs | acetylated on two
lysines- Lys401 and Lys408 |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | Acetylation of SAHH may serve to regulate global alterations in cellular methylation |
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Bibliography | 1. Wang, Y. et al. (2014) ‘Regulation of S -Adenosylhomocysteine Hydrolase by Lysine Acetylation’, Journal of Biological Chemistry, 289(45), pp. 31361–31372. doi: 10.1074/jbc.M114.597153. 2. Palmer, J. L. and Abeles, R. H. (1979) ‘The mechanism of action of S-adenosylhomocysteinase.’, The Journal of biological chemistry, 254(4), pp. 1217–26. Available at: http://www.ncbi.nlm.nih.gov/pubmed/762125 (Accessed: 3 October 2019). |