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Literature summary extracted from

  • Narayanan, S.R.; Borchardt, R.T.
    Purification of bovine liver S-adenosylhomocysteine hydrolase by affinity chromatography on blue dextran-agarose (1988), Biochim. Biophys. Acta, 965, 22-28.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.13.2.1 medicine antiviral drug design Bos taurus
3.13.2.1 medicine chemotherapeutic drug design Bos taurus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.13.2.1 S-adenosyl-L-homocysteine + H2O Bos taurus
-
adenosine + L-homocysteine
-
r

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.13.2.1 3250fold to homogeneity Bos taurus

Reaction

EC Number Reaction Comment Organism Reaction ID
3.13.2.1 S-adenosyl-L-homocysteine + H2O = L-homocysteine + adenosine reaction equilibrium is in vitro strongly in direction of synthesis of S-adenosyl-L-homocysteine Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.13.2.1 liver
-
Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.13.2.1 1.3
-
-
Bos taurus

Storage Stability

EC Number Storage Stability Organism
3.13.2.1 -20°C, with 5% glycerol Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.13.2.1 S-adenosyl-L-homocysteine + H2O
-
Bos taurus adenosine + L-homocysteine
-
r

Subunits

EC Number Subunits Comment Organism
3.13.2.1 tetramer
-
Bos taurus

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 NAD+
-
Bos taurus