1.1.1.27: L-lactate dehydrogenase

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

Reaction

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

Synonyms

A4-LDH, AdhE, anaerobic lactate dehydrogenase, BbLDH, dehydrogenase, lactate, eLDHA, eLDHB, Epsilon crystallin, epsilon-crystallin, H4-L-lactate dehydrogenase, heart LDH, Immunogenic protein p36, L(+)-nLDH, L-(+)-lactate dehydrogenase, L-lactate dehydrogenase B, L-lactic acid dehydrogenase, L-lactic dehydrogenase, L-LDH, lactate dehydrogenase, lactate dehydrogenase A, lactate dehydrogenase B, lactate dehydrogenase NAD-dependent, lactic acid dehydrogenase, lactic dehydrogenase, LctD, LDH, LDH-1, LDH-2, LDH-3, LDH-4, LDH-5, LDH-A, LDH-A4, LDH-m4, LDH1, LDH2, LdhA, LDHB, mLDH, More, muscle LDH, NAD-lactate dehydrogenase, nitric oxideinducible l-lactate dehydrogenase, PfLDH, proteins, specific or class, anoxic stress response, p34, Sa-LDH-1, TeLdhL, Tsac_0416

ECTree

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

Engineering

Engineering on EC 1.1.1.27 - L-lactate dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
I283V |
site-directed mutagenesis, the mutation switches the nature of the residue from Amblyrhynchus cristatus to that of Iguana iguana, another Galapagos marine iguana, the mutation does not affect enzyme kinetics, overview
T9A
site-directed mutagenesis, the mutation switches the nature of the residue from Amblyrhynchus cristatus to that of Iguana iguana, another Galapagos marine iguana, the mutation does not affect enzyme kinetics, overview
T9A/I283V
site-directed mutagenesis, the mutations switch the nature of the residues from Amblyrhynchus cristatus to those of Iguana iguana, another Galapagos marine iguana, the mutation affects enzyme kinetics decreasing Km for pyruvate and kcat, overview
S100M
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
H171C
-
site-directed mutagenesis
C210S
-
crystallization of mutant enzyme
H88X/H226X
substitution of His 88 and 226 of the eLDHA monomer alters the surface charge of equine LDH tetramer, the residues are located in an important region affecting the catalytic kinetics
D38E
-
site-directed mutagenesis, the mutant shows a twofold reduced substrate inhibition by pyruvate compared to the wild-type enzyme
D38R
-
site-directed mutagenesis, the mutant shows a threefold reduced substrate inhibition by pyruvate compared to the wild-type enzyme
F16Q/C81S/N85R
catalytic efficiency is higher than that of wild-type enzyme, utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+
F16Q/I37K/D38S/C81S/N85R
utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+
S100M
-
a hybrid gene is constructed from fragments of the LDH genes from Bacillus stearothermophilus (coding for aa 15-100) and Bacillus megaterium (coding for aa 101-331). The hybrid LDH, named S100M, is more thermostable than Bacillus megaterium LDH, less thermostable than Bacillus stearothermophilus LDH and unlike the two wild-type enzymes, it can not be activated by D-fructose 1,6-bisphosphate
S163L
-
decrease in substrate inhibition, the Km value for pyruvate is increased substantially and the turnover number is 60% that of wild type
D8G
no measurable effect on the Km value for pyruvate, increased thermal stability
additional information