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Literature summary for 3.13.2.1 extracted from

  • Kloor, D.; Kurz, J.; Fuchs, S.; Faust, B.; Osswald, H.
    S-adenosylhomocysteine-hydrolase from bovine kidney: Enzymatic and binding properties (1996), Kidney Blood Press. Res., 19, 100-108.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
2'-deoxyadenosine
-
Bos taurus
adenine
-
Bos taurus
adenosine
-
Bos taurus
adenosine-5'-monophosphate
-
Bos taurus
ATP
-
Bos taurus
cAMP
-
Bos taurus
Inosine
-
Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.005
-
S-adenosyl-L-homocysteine
-
Bos taurus
0.0056
-
adenosine
-
Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
190000
-
gel filtration 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
205fold to homogeneity 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
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.25
-
-
Bos taurus

Storage Stability

Storage Stability Organism
-20°C, stability of the adenosine binding site is reduced from Kd 6.8 to 29 nM within 4 months 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