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Literature summary for 3.4.13.20 extracted from

  • Unno, H.; Yamashita, T.; Ujita, S.; Okumura, N.; Otani, H.; Okumura, A.; Nagai, K.; Kusunoki, M.
    Structural basis for substrate recognition and hydrolysis by mouse carnosinase CN2 (2008), J. Biol. Chem., 283, 27289-27299.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain BL21(DE3)pLysS Mus musculus

Crystallization (Commentary)

Crystallization (Comment) Organism
complexed with bestatin together with Zn2+, hanging drop vapour diffusion method, using 20% polyethylene glycol 3350 and 0.2 M potassium fluoride Mus musculus

Protein Variants

Protein Variants Comment Organism
H228A inactive Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
bestatin
-
Mus musculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the enzymatic activity of carnosinase CN2 requires Mn2+ Mus musculus
additional information Zn2+ is not required for enzymatic activity Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
glutathione-Sepharose bead chromatography and Superdex 200 gel filtration Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
beta-Ala-L-His + H2O i.e. carnosine Mus musculus beta-Ala + L-His
-
?

Subunits

Subunits Comment Organism
homodimer x-ray crystallography Mus musculus

Synonyms

Synonyms Comment Organism
carnosinase
-
Mus musculus
CN2
-
Mus musculus