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4.1.1.5: acetolactate decarboxylase

This is an abbreviated version!
For detailed information about acetolactate decarboxylase, go to the full flat file.

Word Map on EC 4.1.1.5

Reaction

(2S)-2-hydroxy-2-methyl-3-oxobutanoate
=
(3R)-3-hydroxybutan-2-one
+
CO2

Synonyms

ADC, ALD, aldB, ALDC, alpha-Acetolactate decarboxylase, AlsD, BudA1, Decarboxylase, acetolactate

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.1 Carboxy-lyases
                4.1.1.5 acetolactate decarboxylase

Engineering

Engineering on EC 4.1.1.5 - acetolactate decarboxylase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E251A
-
site-directed mutagenesis, the mutant shows highly reduced activity
E251Q
-
site-directed mutagenesis, the mutant shows highly reduced activity
E62A
-
site-directed mutagenesis, the mutant shows highly reduced activity
E62Q
-
site-directed mutagenesis, the mutant shows highly reduced activity
R142A
-
site-directed mutagenesis, the mutant shows highly reduced activity
R142K
-
site-directed mutagenesis, the mutant shows 60% reduced activity compared to the wild-type enzyme
T55A
-
site-directed mutagenesis, the mutant shows 2.5fold increased activity compared to the wild-type enzyme
T55S
-
site-directed mutagenesis, the mutant shows 2fold increased activity compared to the wild-type enzyme
K52D
-
the mutant has almost no variation on enzyme activity, but exhibits improved stability over pH 4.0-5.0 compared to the wild type enzyme
K52E
-
the mutant has almost no variation on enzyme activity, but exhibits improved stability over pH 4.0-5.0 compared to the wild type enzyme
N43D
-
the mutant has almost no variation on enzyme activity, but exhibits improved stability over pH 4.0-5.0 compared to the wild type enzyme
N43D/K52D
-
the mutant shows dramatically improved acidic stability with prolonged half-life of 3.5 h (compared to the wild type of 1.5 h) at pH 4.0
additional information