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Information on EC 3.4.16.4 - serine-type D-Ala-D-Ala carboxypeptidase

for references in articles please use BRENDA:EC3.4.16.4

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IUBMB Comments

A membrane-bound, bacterial enzyme inhibited by penicillin and other β-lactam antibiotics, which acylate the active site serine. Examples are known from peptidase families S11, S12 and S13. Distinct from EC 3.4.17.14, zinc D-Ala-D-Ala carboxypeptidase

The enzyme appears in viruses and cellular organisms
Reaction Schemes
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine

Synonyms
transpeptidase, penicillin-binding protein, pbp2x, pbp1a, pbp1b, penicillin binding proteins, pbp 2, pbp 3, pbp 5, dd-peptidase, more

REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Preferential cleavage: (Ac)2-L-Lys-D-Ala-/-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine
show the reaction diagram
PATHWAY SOURCE
PATHWAYS
MetaCyc
peptidoglycan biosynthesis II (staphylococci), peptidoglycan biosynthesis IV (Enterococcus faecium), peptidoglycan maturation (meso-diaminopimelate containing)