Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.16.4 extracted from

  • Llinas, A.; Ahmed, N.; Cordaro, M.; Laws, A.P.; Fr่re, J.M.; Delmarcelle, M.; Silvaggi, N.R.; Kelly, J.A.; Page, M.I.
    Inactivation of bacterial DD-peptidase by beta-sultams (2005), Biochemistry, 44, 7738-7746.
    View publication on PubMed
Search for more literature for 3.4.16.4

Crystallization (Commentary)

Crystallization (Comment) Organism
by hanging drop vapor diffusion, to 1.1 A resolution Streptomyces sp. R61

Inhibitors

Inhibitors Comment Organism Structure
N-benzoyl-beta-sultam time-dependent, irreversible active site directed inhibitor, the rate of inactivation is first order with respect to beta-sultam concentration and second order rate constants show dependence on pH Streptomyces sp. R61
N-p-chloro-beta-sultam
-
 Streptomyces sp. R61
N-p-methoxy-beta-sultam least effective inhibitor Streptomyces sp. R61
N-p-nitro-beta-sultam
-
 Streptomyces sp. R61

Organism

Organism UniProt Comment Textmining
Streptomyces sp. R61 P15555
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzoyl-D-Ala-thio-D-lactate
-
 Streptomyces sp. R61 ?
-
 ?
N-benzoyl-D-Ala-thioglycolate
-
 Streptomyces sp. R61 ?
-
 ?

Synonyms

Synonyms Comment Organism
DD-peptidase
-
 Streptomyces sp. R61

pH Range

pH Minimum pH Maximum Comment Organism
4 9
-
 Streptomyces sp. R61