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Literature summary for 3.4.16.4 extracted from

  • Silvaggi, N.R.; Anderson, J.W.; Brinsmade, S.R.; Pratt, R.F.; Kelly, J.A.
    The crystal structure of phosphonate-inhibited D-Ala-D-Ala peptidase reveals an analogue of a tetrahedral transition state (2003), Biochemistry, 42, 1199-1208.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapor diffusion, crystal structure of the phosphonal enzyme. The 1.1 A resolution structure of the enzyme in complex with phenyl glycyl-L-alpha-aminopimelyl-epsilon-(D-2-aminoethyl)phosphonate shows that the inhibitor is phosphorylated by the catalytic Ser62 Streptomyces sp.

Inhibitors

Inhibitors Comment Organism Structure
phenyl glycyl-L-alpha-aminopimelyl-epsilon-(D-2-aminoethyl)phosphonate
-
Streptomyces sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptomyces sp. the enzyme is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis ?
-
?

Organism

Organism UniProt Comment Textmining
Streptomyces sp. P15555
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information specific substrate binding to the peptidase induces a conformational change in the active site that places Ser62 in an optimal position for catalysis. This activated conformation relaxes as the reaction proceeds Streptomyces sp. ?
-
?
additional information the enzyme is responsible for the final peptidoglycan cross-linking step in bacterial cell wall biosynthesis Streptomyces sp. ?
-
?