1.1.1.103: L-threonine 3-dehydrogenase

This is an abbreviated version, for detailed information about L-threonine 3-dehydrogenase, go to the full flat file.

Reaction

L-threonine
+
NAD+
=
L-2-amino-3-oxobutanoate
+
NADH
+
H+

Synonyms

CLOST_1621, L-ThrDH, L-threonine dehydrogenase, More, orf382, TDG, TDH, Thr dehydrogenase, ThrDH, threonine 3-dehydrogenase, threonine dehydrogenase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.103 L-threonine 3-dehydrogenase

Engineering

Engineering on EC 1.1.1.103 - L-threonine 3-dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G184A
-
the catalytic efficiency of the mutant is 330fold lower than that of the wild type enzyme
L80G
-
the catalytic efficiency of the mutant is 3300fold lower than that of the wild type enzyme
T186N
-
the catalytic efficiency of the mutant is 330fold lower than that of the wild type enzyme
C38D
-
site-directed mutagenesis
M333A
-
inactive
M333E
-
the mutation affects the substrate's affinity for the enzyme
R180K
-
the mutation has little effect on NAD+ binding affinity, whereas affects the substrate's affinity for the enzyme
S133A
-
inactive
T237A
-
inactive
E152A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152C
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152D
-
site-directed mutagenesis, the E152D mutant shows 3-fold higher turnover rate and reduced affinities toward L-threonine and NAD+ compared to wild-type TDH, Glu152 to Asp substitution causes the enhancement of deprotonation of His47 or ionization of zinc-bound water and threonine in the enzyme-NAD+ complex
E152K
-
site-directed mutagenesis, inactive mutant
E152Q
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152S
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E152T
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E199A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
R204A
-
site-directed mutagenesis, the mutant shows altered kinetics compared to the wild-type enzyme
additional information