3.4.17.8: muramoylpentapeptide carboxypeptidase

This is an abbreviated version!
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]

Engineering

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Engineering on EC 3.4.17.8 - muramoylpentapeptide carboxypeptidase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D344S

Enterococcus faecium

-

the mutant shows highly reduced activity compared to the wild-type

683630

D59A

Enterococcus gallinarum

-

73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity

668456

D59S

Enterococcus gallinarum

-

strong increase in ratio kcat/KM for EC 3.4.17.8 activity, 50% increase in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity

668456

D59A

Enterococcus gallinarum BM4174

-

73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity

-

D59S

Enterococcus gallinarum BM4174

-

strong increase in ratio kcat/KM for EC 3.4.17.8 activity, 50% increase in ratio kcat/KM for D-Ala-D-Ala substrate, EC3.4.13.B1 activity

-

K172N/R173N

Enterococcus hirae

-

site-directed mutagenesis, M1 mutant, the mutant enzyme shows altered complementation of the pbp3-deficient mutant strain SL2 compared to the wild-type enzyme, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1, overview

683602

K199Q

Enterococcus hirae

-

site-directed mutagenesis, M5 mutant, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1

683602

K199Q/K203Q

Enterococcus hirae

-

site-directed mutagenesis, M2 mutant, the mutant enzyme shows altered complementation of the pbp3-deficient mutant strain SL2 compared to the wild-type enzyme, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1, overview

683602

K203Q

Enterococcus hirae

-

site-directed mutagenesis, M3 mutant, the mutant enzyme shows altered complementation of the pbp3-deficient mutant strain SL2 compared to the wild-type enzyme, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1, overview

683602

R173N

Enterococcus hirae

-

site-directed mutagenesis, M4 mutant, the mutant enzyme shows complementation of the pbp5-deficient mutant strain SL1

683602

S422A

Enterococcus hirae

-

site-directed mutagenesis, M6 mutant, inactive mutant

683602

C115S

Escherichia coli

-

site-directed mutagenesis, truncated mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme

683158

K213C/C115S

Escherichia coli

-

site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme

683158

K47C/C115S

Escherichia coli

-

site-directed mutagenesis, truncated double mutant of PBP5, pH-dependency, kinetics, and activity compared to the wild-type enzyme

683158

additional information

8 entries

additional information

Enterococcus faecium

-

construction of spontaneous mutants M512, M9, and G9 from mutant D344S with reduced enzyme activity, but less as for the parental mutant D344S, overview

683630

additional information

Escherichia coli

-

construction of a PBP5-deletion mutant which shows high levels of muramoylpentapeptide, an additional mutation of amiC, encoding muramyl-L-alanine amidase C, leads to long chains of unseparated cells to a higher percentage than with an amiC mutation alone, twisted cell chains appear only when the PBP 5 gene, dacA, is deleted in concert with mutations of amiA and amiC, overview

683609

additional information

Escherichia coli

-

construction of mutant strains lacking PBP5, strain AV-21-10, or PBP5 and PBP7, strain AV23-1, inhibition of FtsZ and MreB simultaneously in strain AV 23-1results in cells balloon outward but retain conspicuous rod-shaped extensions at sites representing the original poles, phenotypes, overview

683610

additional information

Escherichia coli

-

exchange of active site residues Lys47 and Lys213 for gamma-thialysine, pH-dependency, kinetics, and activity compared to the wild-type enzyme

683158

additional information

Escherichia coli MG1655

-

construction of mutant strains lacking PBP5, strain AV-21-10, or PBP5 and PBP7, strain AV23-1, inhibition of FtsZ and MreB simultaneously in strain AV 23-1results in cells balloon outward but retain conspicuous rod-shaped extensions at sites representing the original poles, phenotypes, overview

-

additional information

Mammaliicoccus sciuri

-

expression of mecA, encoding a penicillin-binding protein, in Staphylocccus 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

669108

additional information

Pseudomonas aeruginosa

G3XD74

expression of recombinant protein as soluble version by deletion of its C-terminal membrane anchor. Under in vitro conditions, the soluble enzyme demonstrates both D,D-carboxypeptidase and expanded-spectrum beta-lactamase activities

731142

additional information

Pseudomonas aeruginosa ATCC 15692

-

expression of recombinant protein as soluble version by deletion of its C-terminal membrane anchor. Under in vitro conditions, the soluble enzyme demonstrates both D,D-carboxypeptidase and expanded-spectrum beta-lactamase activities

-