1.1.2.3: L-lactate dehydrogenase (cytochrome)

This is an abbreviated version!
For detailed information about L-lactate dehydrogenase (cytochrome), go to the full flat file.

Word Map on EC 1.1.2.3

Reaction

(S)-lactate
+ 2 ferricytochrome c =
pyruvate
+ 2 ferrocytochrome c + 2 H+

Synonyms

Cyb2, cytochrome b2, cytochrome c oxido reductase, FC b2, Fcb2, flavocytochrome b, flavocytochrome b2, iLDH, L(+)-lactate:cytochrome c oxidoreductase, L-(+)-lactate ferricytochrome c oxidoreductase, L-lactate cytochrome c oxidoreductase, L-lactate cytochrome c reductase, L-lactate dehydrogenase [Cytochrome], L-lactate ferricytochrome C oxidoreductase, L-lactate-cytochrome c oxidoreductase, L-lactate-cytochrome c-oxidoreductase, L-lactate: cytochrome c oxidoreductase, L-lactate:cytochrome c oxidoreductase, L-lactate:cytochrome c-oxidoreductase, L-LCR, L-LDH (FMN-dependent), lactate dehydrogenase (cytochrome), lactic acid dehydrogenase, lactic cytochrome c reductase, NAD+ - independent LDH

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.2 With a cytochrome as acceptor
                1.1.2.3 L-lactate dehydrogenase (cytochrome)

Engineering

Engineering on EC 1.1.2.3 - L-lactate dehydrogenase (cytochrome)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
a L-lactate-selective microbial biosensor is developed using permeabilized cells of gene-engineered thermotolerant methylotrophic yeast Hansenula polymorpha, over-producing FCb2. The HpCYB2 gene, encoding FCb2, under the control of the strong Hansenula polymorpha alcohol oxidase promoter in the frame of a plasmid for multicopy integration is transformed to the recipient strain Hansenula polymorpha C-105 (gcr1 catX) impaired in glucose repression and devoid of catalase activity. The biosensor based on recombinant yeast cells exhibit a higher Km value (Km: 3.02 mM) and hence expanded linear range toward l-lactate as compared to a similar sensor based on the initial cells of Hansenula polymorpha C-105 (Km: 0.33 mM)
A198G
-
turnover reduced to 50%
A198G/L230A
D282N
-
site-directed mutagenesis, while the wild-type mutant has residue R289 in a distal or a proximal conformation, the mutant shows R289 only in a distal conformation
E91K
-
mutation has no effect on the rate of cytochrome c reduction, no significantly different behavior with regard to inhibition by ferrocytochrome c
F52A
-
mutation has no effect on the rate of cytochrome c reduction
H373Q
L230A
L230A/A198G
-
the double mutant enzyme has a 6fold greater catalytic efficiency with L-mandelate than with L-lactate
R289K
-
kcat (1/sec) (substrate: L-lactate): 8.6 (in 200 mM phosphate: 9.2, in 400 mM potassium acetate: 8.8, in 400 mM KCl: 9.2, in 400 mM KBr: 7.8), Km (mM) (substrate: L-lactate): 7.0 (in 200 mM phosphate: 8.7, in 400 mM potassium acetate: 9.2, in 400 mM KCl: 6.5, in 400 mM KBr: 5.8). Mutant is not sensitive for excess lactate concentration. In contrast to the wild-type enzyme high concentrations of acetate, phosphate, chloride and bromide show no influence on the mutant enzyme
R376K
-
mutant enzyme shows no activity
R38E
-
activity and inhibitory profile similar to wild type
Y143F
Y254del
-
deletion mutant
Y254F
Y254L
additional information