Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.1.2.1: D-alanine-(R)-lactate ligase

This is an abbreviated version!
For detailed information about D-alanine-(R)-lactate ligase, go to the full flat file.

Word Map on EC 6.1.2.1

Reaction

D-alanine
+
(R)-lactate
 +
ATP
=
D-alanyl-(R)-lactate
 +
ADP
 +
phosphate

Synonyms

D-Ala-D-Lac ligase, D-Ala:D-Lac ligase, D-alanine-D-lactate ligase, D-alanine:D-alanine (D-lactate) ligase (ADP), D-alanine:D-lactate ligase, D-alanyl-D-lactate ligase, depsipeptide ligase, VanA, VanB, VanD, VanD4, VanI, VRSA-9 Ddl

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.2 acid-alcohol ligases (ester synthases)
                6.1.2.1 D-alanine-(R)-lactate ligase

Engineering

Engineering on EC 6.1.2.1 - D-alanine-(R)-lactate ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
S150A
-
mutant of D-Ala-D-Ala ligase Ddl, mutant has gained depsipeptide ligase activity, i.e. formation of D-Ala-D-Lac, D-Ala-D-hydroxybutyrate, with dipeptide/depsipeptide partition ratios that mimic the pH behaviour of D-Ala-D-lactate ligase VanA. Mutant displays a clear pH-dependent partitioning between the preferred depsipeptide product at low pH and the dipeptide product at high pH
Y216F
-
mutant of D-Ala-D-Ala ligase Ddl, mutant has gained depsipeptide ligase activity, i.e. formation of D-Ala-D-Lac, D-Ala-D-hydroxybutyrate, with dipeptide/depsipeptide partition ratios that mimic the pH behaviour of D-Ala-D-lactate ligase VanA. Mutant displays a clear pH-dependent partitioning between the preferred depsipeptide product at low pH and the dipeptide product at high pH
F261Y
-
the mutant shows a complete loss of the ability to make D-alanyl-(R)-lactate
Q260K/A283E
S137A
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
S137A/Y207F
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
S137F/Y207F
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
S137G/Y207F
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
S137T/Y207F
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
Y201F/Y207F
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
Y207F
-
site-directed mutagenesis, the mutant D-alanine-D-alanine ligase also shows formation of D-alanyl-D-lactate depsipeptide in contrast to the wild-type enzyme, EC 6.3.2.4, which is inactive with (R)-lactate
additional information