1.1.1.28: D-lactate dehydrogenase

This is an abbreviated version, for detailed information about D-lactate dehydrogenase, go to the full flat file.

Reaction

(R)-lactate
+
NAD+
=
pyruvate
+
NADH
+
H+

Synonyms

D-(-)-lactate dehydrogenase, D-(-)-lactate dehydrogenase (NAD), D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein, D-lactate dehydrogenase, D-lactic acid dehydrogenase, D-lactic dehydrogenase, D-LDH, D-LDH-like enzyme, D-LDH1, D-LDH2, D-LDH3, D-nLDH, D-specific lactic dehydrogenase, dehydrogenase, D-lactate, DLDH, DLDH744, ECBD_2243, ECLDH, Fermentative lactate dehydrogenase, FN0511, FNLDH, lactic acid dehydrogenase, LDH, ldhd, LdhTi, Ljd-LDH, NAD-dependent D-lactate dehydrogenase, PA0927, PALDH, Respiratory D-lactate dehydrogenase, WP_013906894

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.28 D-lactate dehydrogenase

Engineering

Engineering on EC 1.1.1.28 - D-lactate dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D259N
-
56fold reduction in kcat, 5fold lowering of Km, shifting of the enzymatic actvity profile towards the acidic range by two units
E264G
-
shift of 2 units in optimal pH toward the acidic range
F299Y
-
site-directed mutagenesis
H205K
-
125-fold reduction in Kcat
H303K
-
Km for pyruvate increased fourfold
Y52L
-
site-directed mutagenesis
Y52L/F299Y
F299Y
-
site-directed mutagenesis
-
Y52L
-
site-directed mutagenesis
-
Y52L/F299Y
-
site-directed mutagenesis
-
F299G
-
mutation reduces enzyme activity with less marked change in substrate preference
F299S
-
mutation reduces enzyme activity with less marked change in substrate preference
Y52D
-
mutation severely reduces enzyme activity
Y52L
-
site-directed mutagenesis, enhancement of phenyllactic acid biosynthesis by recognition site replacement of D-lactate dehydrogenase from Lactobacillus pentosus
Y52R
-
mutation severely reduces enzyme activity, preference for large aliphatic 2-ketoacids and phenylpyruvate
Y52R/F299G
-
mutation abolishes activity with pyruvate, 2-ketobutyrate, 2-ketovalerate, 2-ketoisovalerate, 2-ketoisocaproate and oxaloacetate, weak activity with 2-ketocaproate, 2-ketoglutarate and phenylpyruvate
Y52T
-
mutation severely reduces enzyme activity
Y52T/F299S
-
mutation abolishes activity with pyruvate, 2-ketobutyrate, 2-ketovalerate, 2-ketoisovalerate, 2-ketoisocaproate, 2-ketoglutarate and oxaloacetate, weak activity with hydroxypyruvate and phenylpyruvate
E263A
site-directed mutagenesis, the mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
F298A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
G79A
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
H295A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
M307A
site-directed mutagenesisthe mutant shows highly reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
R234A
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
Y101A
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
G79A
-
site-directed mutagenesis, almost inactive D-lactate dehydrogenase mutant
-
H295A
-
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
-
R234A
-
site-directed mutagenesis, inactive D-lactate dehydrogenase mutant
-
Y101A
-
site-directed mutagenesis, the mutant shows 50% reduced D-lactate dehydrogenase activity compared to the wild-type enzyme
-
additional information