Information on EC 3.4.17.14 - Zinc D-Ala-D-Ala carboxypeptidase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.4.17.14
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RECOMMENDED NAME
GeneOntology No.
Zinc D-Ala-D-Ala carboxypeptidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
cleavage of the bond: (Ac)2-L-lysyl-D-alanyl-/-D-alanine
show the reaction diagram
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-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Peptidoglycan biosynthesis
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peptidoglycan biosynthesis V (beta-lactam resistance)
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CAS REGISTRY NUMBER
COMMENTARY hide
9077-67-2
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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Manually annotated by BRENDA team
strain 544, ATCC 23448, a smooth virulent biovar 1 strain, gene dacF
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Manually annotated by BRENDA team
strain G
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Manually annotated by BRENDA team
R39 and R61
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
Acetyl2-L-Lys-D-Ala-D-Ala + H2O
Acetyl2-L-Lys-D-Ala + D-Ala
show the reaction diagram
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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-
?
Nalpha-Acetyl-L-Lys-D-Ala-D-Ala + H2O
Nalpha-Acetyl-L-Lys-D-Ala + D-Ala
show the reaction diagram
peptidoglycan + H2O
?
show the reaction diagram
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hydrolyzes peptidoglycan interpeptide bonds between a D-alanine and another D-amino acid residue in alpha-position to a free carboxylate
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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2-5 mM, optimal activity
Zn2+
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required
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3-Mercaptopropionate
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6-beta-iodopenicillinate
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causes permanent inactivation
beta-Lactams
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weak
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L-3-mercaptoisobutyrate
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000001
3-Mercaptopropionate
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0.000001
L-3-mercaptoisobutyrate
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.03
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sequence calculation
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
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intracellular replication of Brucella abortus within murine macrophages and HeLa cells
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
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22080
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Streptomyces albus, calculation from amino acid sequence
38000
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Streptomyces sp. R61, gel filtration
50978
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x * 50978, sequence calculation
53300
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Streptomyces sp. R39, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 50978, sequence calculation
monomer
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Streptomyces albus
additional information
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the enzyme consists of two globular domains, connected by a single link, the N-terminal domain has three alpha-helices, and the C-terminal domain has three alpha-helices and five beta-strands
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
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Show AA Sequence (164 entries)
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