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BRENDA support

Literature summary for 3.4.17.14 extracted from

  • Dideberg, O.; Joris, B.; Frere, J.M.; Ghuysen, J.M.; Weber, G.; Robaye, R.; Delbrouck, J.M.; Roelandts, I.
    The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2+) enzyme (1980), FEBS Lett., 117, 215-218.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Streptomyces albus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 2-5 mM, optimal activity Streptomyces albus
Zinc a zinc enzyme Streptomyces albus
Zinc 1 Zn2+ bound per enzyme molecule Streptomyces albus
Zinc Zn2+ cofactor is required for both DD-carboxypeptidase activity and binding of benzyl-penicillin Streptomyces albus

Organism

Organism UniProt Comment Textmining
Streptomyces albus
-
G
-