3.4.17.8: muramoylpentapeptide carboxypeptidase

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For detailed information about muramoylpentapeptide carboxypeptidase, go to the full flat file.

Reaction

cleavage of the bond UDP-N-acetylmuramoyl-L-alanyl-D-gamma-glutamyl-6-carboxy-L-lysyl-D-alanyl-/-D-alanine =

Synonyms

carboxypeptidase D-alanyl-D-alanine, carboxypeptidase I, carboxypeptidase, muramoylpentapeptide, D-alanine carboxypeptidase, D-alanine carboxypeptidase I, D-alanine-D-alanine-carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine peptidase, DacC, DD-Carboxypeptidase, DD-CPase, DD-peptidase, EC 3.4.12.6, Metallo DD-peptidase, msmeg_2432, msmeg_2433, PBP 5, PBP5, PdcA, penicillin binding protein 5, penicillin-binding protein 5, UDP-N-acetylmuramoyl-tetrapeptidyl-D-alanine alanine-hydrolase, VanX, VanXYc, VanY, Zn DD-peptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.17 Metallocarboxypeptidases

                3.4.17.8 muramoylpentapeptide carboxypeptidase

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Results	in table
1	Activating Compound
25	AA Sequence
2	Application
1	CAS Registry Number
5	Cloned(Commentary)
5	Crystallization (Commentary)
1	Expression
2	General Information
39	Inhibitors
2	kcat/KM [mM/s]
7	Ki Value [mM]
14	KM Value [mM]
12	Localization
12	Metals/Ions
3	Molecular Weight [Da]
10	Natural Substrates/ Products (Substrates)
72	Organism
1	PDB ID
6	pH Optimum
1	pH Range
1	pI Value
22	Protein Variants
3	Purification (Commentary)
3	Reaction
1	Reaction Type
34	Reference
13	Source Tissue
2	Specific Activity [micromol/min/mg]
1	Storage Stability
53	Substrates and Products (Substrate)
1	Subunits
44	Synonyms
3	Temperature Optimum [°C]
1	Temperature Stability [°C]
4	Turnover Number [1/s]

Expression

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Expression on EC 3.4.17.8 - muramoylpentapeptide carboxypeptidase

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EXPRESSION

ORGANISM

UNIPROT

LITERATURE

PBP5 mRNA and protein levels are increased in subclade A1 and A2 ampicillin-resistant strains compared to those in clade B and subclade A2 ampicillin-susceptible strains. There is evidence of major clade-associated rearrangements in the region upstream of PBP5, including large DNA fragment insertions, deletions, and single nucleotide polymorphisms, that may be associated with the differential regulation of PBP5 levels between the Enterococcus faecium clades

Enterococcus faecium

A0A075Q0W3

752508