Search by BoMiProt ID - Bomi344


Primary Information

BoMiProt ID Bomi344
Protein Name Adenosylhomocysteinase
Organism Bos taurus
Uniprot IDQ3MHL4
Milk FractionMFGM, Exosome
Ref Sequence ID NP_001029487.1
Aminoacid Length 432
Molecular Weight 47638
FASTA Sequence Download
Gene Name AHCY
Gene ID 508158
Protein Existence Status Reviewed: Experimental evidence at transcript level

Secondary Information

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
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
PTMs acetylated on two lysines- Lys401 and Lys408
Site(s) of PTM(s)

N-glycosylation, O-glycosylation,
Phosphorylation
Predicted Disorder Regions NA
DisProt Annotation
TM Helix Prediction No TM helices
Significance of PTMs Acetylation of SAHH may serve to regulate global alterations in cellular methylation
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).