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Literature summary for 3.13.2.1 extracted from

  • Kloor, D.; Fuchs, S.; Petroktistis, F.; Delabar, U.; Muhlbauer, B.; Quast, U.; Osswald, H.
    Effects of ions on adenosine binding and enzyme activity of purified S-adenosylhydrolase from bovine kidney (1998), Biochem. Pharmacol., 56, 1493-1496.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
phosphate
-
Bos taurus

Application

Application Comment Organism
medicine antiviral drug design Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
CaCl2 reduces adenosine binding Bos taurus
Na+ reduces adenosine binding Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0054
-
adenosine phosphate added Bos taurus
0.0101
-
adenosine no phosphate added Bos taurus
0.0103
-
S-adenosyl-L-homocysteine phosphate added Bos taurus
0.0125
-
S-adenosyl-L-homocysteine no phosphate added Bos taurus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bos taurus

Reaction

Reaction Comment Organism Reaction ID
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

Source Tissue Comment Organism Textmining
kidney
-
Bos taurus
-

Storage Stability

Storage Stability Organism
-20°C Bos taurus

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
tetramer
-
Bos taurus

Cofactor

Cofactor Comment Organism Structure
NAD+ essential for adenosine binding Bos taurus