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Literature summary for 3.4.17.14 extracted from

  • Dideberg, O.; Charlier, P.; Dive, G.; Joris, B.; Frere, J.M.; Ghuysen, J.M.
    Structure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution (1982), Nature, 299, 469-470.
    View publication on PubMed
Search for more literature for 3.4.17.14

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Streptomyces albus

Inhibitors

Inhibitors Comment Organism Structure
beta-lactams weak Streptomyces albus

Metals/Ions

Metals/Ions Comment Organism Structure
Zinc a zinc enzyme Streptomyces albus
Zinc the Zn2+ ion is ligated by three histidine residues and located in a cleft in the C-terminal domain Streptomyces albus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptomyces albus involved in bacterial cell wall metabolism ?
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces albus
-
 G
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information mechanism Streptomyces albus ?
-
 ?
additional information involved in bacterial cell wall metabolism Streptomyces albus ?
-
 ?

Subunits

Subunits Comment Organism
More the enzyme consists of two globular domains, connected by a single link, the N-terminal domain has three alpha-helices, and the C-terminal domain has three alpha-helices and five beta-strands Streptomyces albus