3.4.17.13: Muramoyltetrapeptide carboxypeptidase
This is an abbreviated version!
For detailed information about Muramoyltetrapeptide carboxypeptidase, go to the full flat file.
Word Map on EC 3.4.17.13
-
3.4.17.13
-
peptidoglycan
-
murein
-
dd-carboxypeptidase
-
homari
-
gaffkya
-
muropeptide
-
sacculus
-
transpeptidation
-
sphaericus
-
udp-murnac-tetrapeptide
-
meso-diaminopimelic
- 3.4.17.13
- peptidoglycan
- murein
- dd-carboxypeptidase
- homari
-
gaffkya
-
muropeptide
-
sacculus
-
transpeptidation
- sphaericus
- udp-murnac-tetrapeptide
-
meso-diaminopimelic
Reaction
hydrolysis of the bond: N-acetyl-D-glucosaminyl-N-acetylmuramoyl-L-Ala-D-glutamyl-6-carboxy-L-lysyl-/-D-alanine =
Synonyms
Carboxypeptidase II, Carboxypeptidase IIW, Carboxypeptidase, lysyl-D-alanine, Carboxypeptidase, muramoyltetrapeptide, cjj81176_0915, DacB, L,D-carboxypeptidase A, L-Lysyl-D-alanine carboxypeptidase, LD-Carboxypeptidase, LdcA, LdcA1, LdcA2, LdcB, muramoyltetrapeptide carboxypeptidase, peptidase U61, Pgp2, Spr0554
ECTree
Advanced search results
Engineering
Engineering on EC 3.4.17.13 - Muramoyltetrapeptide carboxypeptidase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
E217A
site-directed mutagenesis, nearly inactive mutant, lack of activity might possibly be due to a folding defect, no crystallization of the mutant enzyme
H285A
site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect
S115A
site-directed mutagenesis, nearly inactive mutant, lack of activity is not due to a folding defect
additional information
-
an ldcA null mutant strain is constructed by the one-step inactivation method of Datsenko and Wanner
additional information
-
the dacB gene is disrupted in strain MG1363 by single-crossover integration of the pRV300 vector
additional information
-
expression of mecA, encoding a penicillin-binding protein, in Staphylcoccus aureus confers resistance to beta-lactam and leads to increased growth and cell wall synthesis in presence of high concentratin of antibiotic methicillin, the cell wall synthesized is typical for Staphylcoccus aureus and uses the endogenous precursors, but is eventhough completely dependent on the recombinant enzyme from Staphylcoccus sciuri, overview