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3.4.13.22: D-Ala-D-Ala dipeptidase

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

Word Map on EC 3.4.13.22

Reaction

D-Ala-D-Ala
+
H2O
= 2 D-Ala

Synonyms

AAD, D-, D-dipeptidase, D-Ala-D-Ala amino dipeptidase, D-Ala-D-Ala dipeptidase, D-Ala-D-Ala dipeptidase VanX, D-Ala-D-Ala-dipeptidase, D-alanyl-D-alanine dipeptidase, M15.011, MAB1843, Vancomycin B-type resistance protein vanX, VanX, VanXY, VanXYc

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.13 Dipeptidases
                3.4.13.22 D-Ala-D-Ala dipeptidase

Engineering

Engineering on EC 3.4.13.22 - D-Ala-D-Ala dipeptidase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D59A
-
73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate
D59S
-
50% increase in ratio kcat/KM for D-Ala-D-Ala substrate
D59A
-
73% decrease in ratio kcat/KM for D-Ala-D-Ala substrate
-
D59S
-
50% increase in ratio kcat/KM for D-Ala-D-Ala substrate
-
C78S/C157S
-
site-directed mutagenesis, reduced activity
D123A
-
site-directed mutagenesis, inactive, nearly no remaining Zn2+
D145A/E146A
-
site-directed mutagenesis, 6fold lowered kcat compared to wild-type, 11% reduced zinc content compared to wild-type
E181A
-
site-directed mutagenesis, inactive, 21.8% reduced zinc content compared to wild-type
H116A
-
site-directed mutagenesis, inactive, 92.1% reduced zinc content compared to wild-type
H116A/H184A
-
site-directed mutagenesis, inactive, 97.5% reduced zinc content compared to wild-type
H13A
-
site-directed mutagenesis, activity equivalent to wild-type, 8.3% reduced zinc content compared to wild-type
H149A
-
site-directed mutagenesis, equivalent to wild-type
H149A/H150A
-
site-directed mutagenesis, 11fold lowered kcat, 14.9% reduced zinc content compared to wild-type
H150A
-
site-directed mutagenesis, equivalent to wild-type
H184A
-
site-directed mutagenesis, inactive, 99.08% reduced zinc content compared to wild-type
additional information
-
an aad knockout mutant (MD119) is constructed in NZ7100 using a two-step homologous recombination procedure. Aad inactivation results in the stable replacement of the aad open reading frame (encoding 180 amino acid residues out of 185) by an erythromycin resistance cassette