3.4.17.14: Zinc D-Ala-D-Ala carboxypeptidase
This is an abbreviated version!
For detailed information about Zinc D-Ala-D-Ala carboxypeptidase, go to the full flat file.
Word Map on EC 3.4.17.14
-
3.4.17.14
-
peptidoglycan
-
beta-lactams
-
exocellular
-
benzylpenicillin
-
muropeptide
-
actinomadura
-
dd-peptidase
-
penicillin-sensitive
-
dd-cpases
-
murein
-
dd-endopeptidase
-
transpeptidation
-
ld-carboxypeptidase
-
genapol
-
peptidoglycan-mimetic
-
bocillin
-
homari
-
zn2+-containing
-
gaffkya
- 3.4.17.14
- peptidoglycan
- beta-lactams
-
exocellular
- benzylpenicillin
-
muropeptide
- actinomadura
- dd-peptidase
-
penicillin-sensitive
- dd-cpases
- murein
-
dd-endopeptidase
-
transpeptidation
- ld-carboxypeptidase
-
genapol
-
peptidoglycan-mimetic
-
bocillin
- homari
-
zn2+-containing
-
gaffkya
Reaction
cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-/-D-alanine =
Synonyms
D-alanyl-D-alanine carboxypeptidase, D-Alanyl-D-alanine hydrolase, D-Alanyl-D-alanine-cleaving carboxypeptidase, DAP, DD-Carboxypeptidase, DD-Carboxypeptidase-transpeptidase, G enzyme, KM endopeptidase, More, PBP4, PBP4a, PBP4B, penicillin binding protein 4, penicillin-binding protein 4a, zinc D-Ala-D-Ala carboxypeptidase, Zn2+ G peptidase
ECTree
Advanced search results
Metals Ions
Metals Ions on EC 3.4.17.14 - Zinc D-Ala-D-Ala carboxypeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Zinc
Zinc
-
Zn2+ cofactor is required for both DD-carboxypeptidase activity and binding of benzyl-penicillin
Zinc
-
the Zn2+ ion is ligated by three histidine residues and located in a cleft in the C-terminal domain