DD-transpeptidase
| Serine-type D-Ala-D-Ala carboxypeptidase | |||||||||
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| Identifiers | |||||||||
| EC number | 3.4.16.4 | ||||||||
| CAS number | Template:CAS | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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A 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 cross-links peptidoglycan chains to form rigid cell walls.
The antibiotic penicillin irreversibly binds to and inhibits the activity of the transpeptidase enzyme by forming a highly stable penicilloyl-enzyme intermediate. Because of the interaction between penicillin and transpeptidase, this enzyme is also known as penicillin-binding protein (PBP).
See also
- Vancomycin, an antibiotic that binds the D-ala-D-ala residues, inhibiting elongation via glycosyltransferase
References
- ↑ Lua error in package.lua at line 80: module 'strict' not found.
External links
- The MEROPS online database for peptidases and their inhibitors: S11.001
- EC 3.4.16.4
- Serine-Type D-Ala-D-Ala Carboxypeptidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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