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| Serine-type D-Ala-D-Ala carboxypeptidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Structure of the streptomyces K15 DD-transpeptidase | |||||||||
| Identifiers | |||||||||
| EC no. | 3.4.16.4 | ||||||||
| CAS no. | 9077-67-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
DD-transpeptidase (EC 3.4.16.4, DD-peptidase, DD-transpeptidase, DD-carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanine carboxypeptidase, D-alanyl carboxypeptidase, and serine-type D-Ala-D-Ala carboxypeptidase.[1]) is a bacterial enzyme that catalyzes the transfer of the R-L-αα-D-alanyl moiety of R-L-αα-D-alanyl-D-alanine carbonyl donors to the γ-OH of their active-site serine and from this to a final acceptor.[2] It is involved in bacterial cell wall biosynthesis, namely, the transpeptidation that crosslinks the peptide side chains of peptidoglycan strands.[3]
The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate.[4] Because of the interaction between penicillin and transpeptidase, this enzyme is also known as penicillin-binding protein (PBP).
- ^ "E.C.3.4.16.4 Serine-type D-Ala-D-Ala carboxypeptidase". Enzyme Structures Database. Archived from the original on May 17, 2006. Retrieved February 26, 2006.
- ^ Grandchamps J, Nguyen-Distèche M, Damblon C, Frère JM, Ghuysen JM (1995). "Streptomyces K15 active-site serine DD-transpeptidase: specificity profile for peptide, thiol ester and ester carbonyl donors and pathways of the transfer reactions". Biochem J. 307 ( Pt 2) (2): 335–9. doi:10.1042/bj3070335. PMC 1136653. PMID 7733866.
- ^ Yocum RR, Waxman DJ, Rasmussen JR, Strominger JL (1979). "Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases". Proc Natl Acad Sci U S A. 76 (6): 2730–4. Bibcode:1979PNAS...76.2730Y. doi:10.1073/pnas.76.6.2730. PMC 383682. PMID 111240.
- ^ Gordon E, Mouz N, Duée E, Dideberg O (June 2000). "The crystal structure of the penicillin-binding protein 2x from Streptococcus pneumoniae and its acyl-enzyme form: implication in drug resistance". Journal of Molecular Biology. 299 (2): 477–85. doi:10.1006/jmbi.2000.3740. PMID 10860753.