DD-transpeptidase

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Serine-type D-Ala-D-Ala carboxypeptidase
Identifiers
EC number 3.4.16.4
CAS number 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

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. In Gram-positive bacteria, the peptidoglycan molecules are cross-linked by a pentapeptide bridge, whereas, in Gram-negative bacteria, the peptidoglycan molecules are directly covalently bound to each other.

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[edit]

References[edit]

  1. ^ "E.C.3.4.16.4 Serine-type D-Ala-D-Ala carboxypeptidase". Enzyme Structures Database. Retrieved February 26, 2006. 

External links[edit]