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Literature summary extracted from

  • Parker, N.B.; Yang, X.; Hanke, J.; Mason, K.A.; Schowen, R.L.; Borchardt, R.T.; Yin, D.H.
    Trypanosoma cruzi: molecular cloning and characterization of the S-adenosylhomocysteine hydrolase (2003), Exp. Parasitol., 105, 149-158.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.13.2.1 overexpression in Escherichia coli Trypanosoma cruzi

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.13.2.1 48000
-
4 * 48000, SDS-PAGE Trypanosoma cruzi
3.13.2.1 200000
-
gel filtration Trypanosoma cruzi

Organism

EC Number Organism UniProt Comment Textmining
3.13.2.1 Trypanosoma cruzi Q7YUF0
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.13.2.1
-
Trypanosoma cruzi

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.13.2.1 S-adenosyl-DL-homocysteine + H2O the reversible catalysis depends on the binding of NAD+ to the enzyme Trypanosoma cruzi DL-homocysteine + adenosine
-
?

Subunits

EC Number Subunits Comment Organism
3.13.2.1 tetramer 4 * 48000, SDS-PAGE Trypanosoma cruzi

Synonyms

EC Number Synonyms Comment Organism
3.13.2.1 AdoHyc hydrolase
-
Trypanosoma cruzi

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.13.2.1 1
-
S-adenosyl-DL-homocysteine pH 7.2, 37°C Trypanosoma cruzi
3.13.2.1 3
-
adenosine pH 7.2, 37°C Trypanosoma cruzi
3.13.2.1 3
-
DL-homocysteine pH 7.2, 37°C Trypanosoma cruzi

pI Value

EC Number Organism Comment pI Value Maximum pI Value
3.13.2.1 Trypanosoma cruzi calculation from nucleotide sequence
-
6