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Information on EC 3.4.17.14 - Zinc D-Ala-D-Ala carboxypeptidase and Organism(s) Escherichia coli and UniProt Accession P24228

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This record set is specific for:
Escherichia coli
UNIPROT: P24228 not found.
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-/-D-alanine
Synonyms
dd-carboxypeptidase, pbp4a, d-alanyl-d-alanine carboxypeptidase, penicillin binding protein 4, dd-carboxypeptidase-transpeptidase, pbp4b, d-alanyl-d-alanine-cleaving carboxypeptidase, penicillin-binding protein 4a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DD-Carboxypeptidase
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penicillin binding protein 4
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D-Alanyl-D-alanine hydrolase
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-
-
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D-Alanyl-D-alanine-cleaving carboxypeptidase
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-
-
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DD-Carboxypeptidase
DD-Carboxypeptidase-transpeptidase
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-
-
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G enzyme
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-
-
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Zn2+ G peptidase
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-
-
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additional information
-
the enzyme belongs to the serine protease family
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
9077-67-2
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Nalpha,Nepsilon-diacetyl-Lys-D-Ala-D-Ala + H2O
Nalpha,Nepsilon-diacetyl-Lys-D-Ala + D-Ala
show the reaction diagram
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-
-
-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
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the DD-carboxypeptidase activity encoded by pbp4B is not essential for the cell growth of Escherichia coli
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-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.03
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sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
the enzyme contains the mutation D261Y, relative to the SwissProt entry P24228; gene dacB
SwissProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
the enzyme contains a 5' leader sequence targeting it to the periplasm
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50978
-
x * 50978, sequence calculation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50978, sequence calculation
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme, wild-type or selenomethionine-labeled, 10-15 mg/ml protein, hanging drop vapour diffusion method, from 0.1 M MES, pH 6.5, and 3-10% PEG 20000, microseeding, 20°C, cryoprotection by 25% v/v glycerol, X-ray diffraction structure determination and analysis at 1.55-1.70 A resolution, modeling
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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construction of gene pbp4B deletion mutants, the enzyme is not not essential for cell division, the strain lacking all known D-alanine carboxypeptidases is viable, overview
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from strain BL21(DE3) by anion exchange and hydrophobic interaction chromatography, followed by gel filtration
recombinant His-tagged enzyme from strain BL21(DE3) membranes by solubilization with 1% Triton X-100 and nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene dacB, expression of the enzyme lacking the 5' leader peptide in strain BL21(DE3)
gene pbp4B, DNA and amino acid sequence determination and analysis, the pbp4B gene is located at the zipA-dapA region, subcloning in strain DH5alpha, expression of N-terminally His-tagged enzyme in strain BL21(DE3) membranes
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Vega, D.; Ayala, J.A.
The DD-carboxypeptidase activity encoded by pbp4B is not essential for the cell growth of Escherichia coli
Arch. Microbiol.
185
23-27
2006
Escherichia coli
Manually annotated by BRENDA team
Kishida, H.; Unzai, S.; Roper, D.I.; Lloyd, A.; Park, S.Y.; Tame, J.R.
Crystal structure of penicillin binding protein 4 (dacB) from Escherichia coli, both in the native form and covalently linked to various antibiotics
Biochemistry
45
783-792
2006
Escherichia coli (P24228), Escherichia coli
Manually annotated by BRENDA team