3.4.16.4: serine-type D-Ala-D-Ala carboxypeptidase

This is an abbreviated version!
For detailed information about serine-type D-Ala-D-Ala carboxypeptidase, go to the full flat file.

Reaction

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

carboxypeptidase I, CPase, D,D-carboxypeptidase, D,D-carboxypeptidase R39, D,D-dipeptidase, D-Ala-D-Ala carboxypeptidase, D-Ala-D-Ala peptidase, D-Ala-D-Ala(D,D) carboxypeptidase, D-alanine carboxypeptidase, D-alanine carboxypeptidase I, D-alanine-carboxypeptidase, D-alanyl carboxypeptidase, D-alanyl-D-alanine carboxypeptidase, D-alanyl-D-alanine carboxypeptidase/transpeptidase, D-Alanyl-D-alanine hydrolase, D-alanyl-D-alanine peptidase, D-alanyl-D-alanine transpeptidase, D-alanyl-D-alanine-carboxypeptidase, D-alanyl-D-alanine-cleaving peptidase, D-alanyl-D-alanine-cleaving-peptidase, D-alanyl-D-alanine-transpeptidase, D-amino acid amidase, DAA, Dac, dacA, DacA-1, DacB, DacC, DacD, DAP, Dbv7, DD-Carboxypeptidase, DD-CPase, DD-CPase1, DD-peptidase, DD-transpeptidase, DD-transpeptidase/penicillin-binding protein, LMM-PBP, low molecular mass penicillin binding protein, PBP, PBP 2, PBP 3, PBP 4, PBP 5, PBP 6, PBP-5*, PBP-6B, PBP1a, PBP1b, PBP2x, PBP3, PBP4, PBP4a, PBP5, PBP6, PBP6a, PBP6b, penicillin binding protein 4, penicillin binding protein 5, penicillin binding proteins, penicillin-binding protein, penicillin-binding protein 1B, penicillin-binding protein 4a, penicillin-binding protein 5, penicillin-binding protein 5a, R39 PBP, SCO4439, serine type D-alanyl-D-alanine carboxypeptidase/transpeptidase, serine-type D-Ala-D-Ala carboxypeptidase, serine-type-D-Ala-D-Ala carboxypeptidase, transpeptidase, VanX, VanXY, VanY, VanY(D) DD-carboxypeptidase, VanYD, VanYn, VC_0947, VP2468, zinc D-Ala-D-Ala carboxypeptidase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.16 Serine-type carboxypeptidases

                3.4.16.4 serine-type D-Ala-D-Ala carboxypeptidase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
7	Activating Compound
97117	AA Sequence
18	Application
1	CAS Registry Number
27	Cloned(Commentary)
28	Crystallization (Commentary)
15	General Information
2	General Stability
21	IC50 Value
222	Inhibitors
6	kcat/KM [mM/s]
27	Ki Value [mM]
84	KM Value [mM]
53	Localization
6	Metals/Ions
18	Molecular Weight [Da]
53	Natural Substrates/ Products (Substrates)
184	Organism
6	Pathway
323	PDB ID
22	pH Optimum
3	pH Range
27	Protein Variants
32	Purification (Commentary)
3	Reaction
27	Reaction Type
142	Reference
4	Source Tissue
10	Specific Activity [micromol/min/mg]
3	Storage Stability
246	Substrates and Products (Substrate)
13	Subunits
232	Synonyms
13	Temperature Optimum [°C]
5	Temperature Stability [°C]
74	Turnover Number [1/s]

General Information

print visible entries

print all entries

Go back to the abbreviated version
of the Enzyme Summary Page.

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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide show all columns Go to General Information Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

malfunction

Escherichia coli

-

loss of penicillin-binding protein 5 enhances beta-lactam susceptibility, the observed susceptibilities for ampicillin, piperacillin, amoxicillin, penicillin G, cefadroxil and cefalexin are enhanced by 4fold and for cefalothin and cefaclor the susceptibilities are at least 8fold higher in the mutants

708741

physiological function

14 entries

physiological function

Corynebacterium jeikeium

-

the beta-lactam-sensitive D,D-carboxypeptidase activity of Pbp4 controls the L,D and D,D transpeptidation pathways in Corynebacterium jeikeium

709996

physiological function

Escherichia coli

-

the DD-carboxypeptidase activity of PBP 5 is responsible for maintaining cell shape

708523

physiological function

Nonomuraea sp.

Q7WZ84

enzyme has a role in removing the last D-Ala from the pentapeptide peptidoglycan precursors and reprogramming cell wall biosynthesis. Isoform C-His6-VanYn over-expression confers glycopeptide resistance to Streptomyces venezuelae. The addition of His6-tag at the N-terminus of the protein abolishes its biological activity either in vitro or in vivo assays

731544

physiological function

Vibrio cholerae

Q9KTF5

Vibrio cholerae lacking isoform DacA-1 displays slow growth, aberrant morphology and altered peptidoglycan homeostasis in Luria-Bertani medium, as well as a profound plating defect. DacA-1 alone among Vibrio cholerae’s low molecular weight penicillin-binding proteins is critical for bacterial growth. The growth and morphology of the dacA-1 mutant are unimpaired in Luria-Bertani media containing reduced concentrations of NaCl of 100 mM or less, and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the dacA-1 mutant contains elevated pentapeptidelevels in standard and low salt media

731725

physiological function

Vibrio parahaemolyticus

Q87LZ0

when the viable but nonculturable state of the bacterium is induced, the rod-shaped cells become coccoid, and various aberrantly shaped intermediates are formed in the initial stage. Among several genes, the expression of dacB, which encodes D-alanyl-D-alanine carboxypeptidase, is enhanced the most. The proportion of aberrantly shaped cells is significantly lower in the dacB mutant strain than in the parent strain, but the proportion is restored in the presence of the complementary dacB gene

731181

physiological function

Escherichia coli

-

D,D-CPases PBP5, PBP6a, and PBP6b change dimer conformation between resting and active states. The isoforms are not redundant but that their balanced activity is required for robust peptidoglycan synthesis

754599

physiological function

Streptomyces coelicolor

Q9KZY7

in a gene disruption mutant, the spores are affected in their resistance to heat and acid and show a dramatic increase in swelling during germination. The mycelium of the mutant is more sensitive to glycopeptide antibiotics vancomycin and teicoplanin. Both the DD-CPase domain and the hydrophobic transmembrane region are essential for complementing the wild type phenotypes in the mutant. In a model for the biological mechanism, DD-CPase releases D-Ala from peptidoglycan precursors, thereby reducing the substrate pool for peptidoglycan crosslinking (transpeptidation)

755422

physiological function

Escherichia coli

-

in an isoform DacC deletion mutant, the extracellular activities and fluorescence value of recombinant amylase, green fluorescent protein, and alpha-galactosidase are increased by 82.3, 29.1, and 37.7%, respectively, compared with that of control cells. The outer membrane permeability and intracellular soluble peptidoglycan accumulation of the deletion mutant are also enhanced. In the poles of the deletion mutant, local transparent bulges are found

753439

physiological function

Escherichia coli

-

overexpression of D,D-carboxypeptidase DacA or DacB promotes the accumulation of intracellular soluble peptidoglycan, alters cell morphology (shape and size) and leads to the formation of transparent globular structures in Escherichia coli cells. Extracellular production of recombinant green fluorescent protein is increased by 1.7- and 2.3fold upon overexpression of DacA and DacB, respectively. Extracellular production of recombinant amylase and apha-galactosidase is increased by 4.5- and 2.8fold, respectively, upon overexpression of DacA, and by 11.9- and 2.5fold, respectively, upon overexpression of DacB. Overexpression of DacA or DacB enhances both the outer and inner membrane permeability of Escherichia coli

752575

physiological function

Bradyrhizobium diazoefficiens

-

peptide uptake transporters BclA and DD-CPase1 act independently in the morphological differentiation of bacteroids induced by Nodule-specific Cysteine-Rich peptides NCR. The nitrogenase activity of plants infected with a DD-CPase1 mutant is strongly reduced, in large part because the mutant induces much less nodules than the wild type. A BclA/DD-CPAse1 double exhibits a similar symbiotic phenotype as the DD-CPase1 single mutant

755483

physiological function

Bradyrhizobium diazoefficiens USDA 110

-

peptide uptake transporters BclA and DD-CPase1 act independently in the morphological differentiation of bacteroids induced by Nodule-specific Cysteine-Rich peptides NCR. The nitrogenase activity of plants infected with a DD-CPase1 mutant is strongly reduced, in large part because the mutant induces much less nodules than the wild type. A BclA/DD-CPAse1 double exhibits a similar symbiotic phenotype as the DD-CPase1 single mutant

-

physiological function

Streptomyces coelicolor ATCC BAA-471

-

in a gene disruption mutant, the spores are affected in their resistance to heat and acid and show a dramatic increase in swelling during germination. The mycelium of the mutant is more sensitive to glycopeptide antibiotics vancomycin and teicoplanin. Both the DD-CPase domain and the hydrophobic transmembrane region are essential for complementing the wild type phenotypes in the mutant. In a model for the biological mechanism, DD-CPase releases D-Ala from peptidoglycan precursors, thereby reducing the substrate pool for peptidoglycan crosslinking (transpeptidation)

-

physiological function

Nonomuraea sp. ATCC 39727

-

enzyme has a role in removing the last D-Ala from the pentapeptide peptidoglycan precursors and reprogramming cell wall biosynthesis. Isoform C-His6-VanYn over-expression confers glycopeptide resistance to Streptomyces venezuelae. The addition of His6-tag at the N-terminus of the protein abolishes its biological activity either in vitro or in vivo assays

-

physiological function

Vibrio cholerae ATCC 39315

-

Vibrio cholerae lacking isoform DacA-1 displays slow growth, aberrant morphology and altered peptidoglycan homeostasis in Luria-Bertani medium, as well as a profound plating defect. DacA-1 alone among Vibrio cholerae’s low molecular weight penicillin-binding proteins is critical for bacterial growth. The growth and morphology of the dacA-1 mutant are unimpaired in Luria-Bertani media containing reduced concentrations of NaCl of 100 mM or less, and also within suckling mice, a model host for the study of cholera pathogenesis. Peptidoglycan from the dacA-1 mutant contains elevated pentapeptidelevels in standard and low salt media

-