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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.

Word Map on EC 1.1.1.28

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-LDH0653, D-LDH1, D-LDH2, D-LDH3, D-LDH82319, D-nLDH, D-specific lactic dehydrogenase, dehydrogenase, D-lactate, DLD1, DLDH, DLDH744, ECBD_2243, ECLDH, FD35_GL001981, Fermentative lactate dehydrogenase, FN0511, FNLDH, lactic acid dehydrogenase, ldb0101, Ldb1010, LDH, LdhA, ldhd, LDHD1, LDHD2, LDHD3, LdhTi, Ljd-LDH, MGG_01202, NAD-dependent D-lactate dehydrogenase, PA0927, PALDH, Respiratory D-lactate dehydrogenase, SO_0968, tp0037, 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

Application

Application on EC 1.1.1.28 - D-lactate dehydrogenase

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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
construction of a metabolically engineered Saccharomyces cerevisiae that produces D-lactic acid efficiently. Two copies of the D-lactate dehydrogenase gene from Leuconostoc mesenteroides subsp. mesenteroides strain NBRC3426 are introduced into the genome. The D-lactate production reaches 61.5 g/l, the amount of glucose being transformed into D-lactic acid is 53.0% under non-neutralizing conditions. The D-lactic acid is of extremely high optical purity of 99.9% or higher
diagnostics
-
the enzyme is useful for selective determination of D,L-lactic acid in wines using peroxidase-based biosensors, method optimization, overview
molecular biology
synthesis
additional information
-
protocol for undergraduate molecular biology and biochemistry laboratory courses spanning two semesters that is organized around the LdhA gene from the yogurt-fermenting bacterium Lactobacillus bulgaricus, using commercially available yogurt. Curriculum starts with cloning the LdhA gene into a prokaryotic expression vector, followed by mRNA isolation and characterization of recombinant gene expression levels using RT-PCR. The biochemistry module begins with overexpression of the cloned LdhA gene and guides students through the process of affinity purification, biochemical characterization of the purified LdhA protein, and analysis of enzyme kinetics using various substrates and an inhibitor, concluding with a guided inquiry investigation of structure-function relationships in the three-dimensional structure of LdhA using molecular visualization software