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Literature summary extracted from

  • Porcelli, M.; Fusco, S.; Inizio, T.; Zappia, V.; Cacciapuoti, G.
    Expression, purification, and characterization of recombinant S-adenosylhomocysteine hydrolase from the thermophilic archaeon Sulfolobus solfactorius (2000), Protein Expr. Purif., 18, 27-35.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.13.2.1 medicine antiviral drug design Saccharolobus solfataricus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.13.2.1 into Escherichia coli Saccharolobus solfataricus

General Stability

EC Number General Stability Organism
3.13.2.1 unusual stability in protein denaturants and detergents, complete recombinant enzyme Saccharolobus solfataricus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.13.2.1 0.014
-
S-adenosyl-L-homocysteine complete recombinant enzyme Saccharolobus solfataricus
3.13.2.1 0.016
-
S-adenosyl-L-homocysteine truncated recombinant enzyme Saccharolobus solfataricus
3.13.2.1 0.04
-
adenosine complete recombinant enzyme Saccharolobus solfataricus
3.13.2.1 0.042
-
adenosine truncated recombinant enzyme Saccharolobus solfataricus
3.13.2.1 0.148
-
L-homocysteine truncated recombinant enzyme Saccharolobus solfataricus
3.13.2.1 0.152
-
L-homocysteine complete recombinant enzyme Saccharolobus solfataricus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.13.2.1 190000
-
recombinant enzymes, gel filtration Saccharolobus solfataricus

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 Saccharolobus solfataricus
-
adenosine + L-homocysteine
-
r

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Saccharolobus solfataricus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.13.2.1 truncated recombinant enzyme: 71.7fold, complete recombinant enzyme: to homogeneity Saccharolobus solfataricus

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 Saccharolobus solfataricus

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 0.163
-
complete recombinant enzyme Saccharolobus solfataricus
3.13.2.1 0.165
-
truncated recombinant enzyme, wild-type Saccharolobus solfataricus

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.13.2.1 tetramer homotetramer, recombinant enzymes, SDS-PAGE Saccharolobus solfataricus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.13.2.1 75
-
recombinant enzymes Saccharolobus solfataricus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.13.2.1 additional information
-
truncated recombinant enzyme Saccharolobus solfataricus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.13.2.1 88
-
melting temperature, truncated recombinant enzyme Saccharolobus solfataricus
3.13.2.1 95
-
melting temperature, complete recombinant enzyme Saccharolobus solfataricus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.13.2.1 7.5
-
complete recombinant enzyme Saccharolobus solfataricus

Cofactor

EC Number Cofactor Comment Organism Structure
3.13.2.1 NAD+
-
Saccharolobus solfataricus