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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.
Reaction
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
1.1.1.28 D-lactate dehydrogenaseAdvanced search results
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in table
10
3656
132
243
105
28
11
30
87
Subunits
Subunits on EC 1.1.1.28 - D-lactate dehydrogenase
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SUBUNITS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
dimer
homodimer
homooctamer
8 * 38500, about, sequence calculation, the apparently octameric form of ECLDH is likely an artificial product due to the overexpression, and exhibits slightly but significantly lower specific activity than the tetrameric form
homotetramer
monomer
tetramer
additional information
dimer
biologically significant unit in the D-LDH enzymes is probably a homodimer
homodimer
two identical monomers of DLDH744 are associated at the cofactor binding domain to form the homodimer in one asymmetric unit. The dimer interface is stabilized mainly by hydrogen-bonding interactions between residues from alpha-helices, alpha5(Ser102-Arg119), alpa6(Leu121-Glu130), alpha12(Glu279-Arg285) and connecting loops, structure analysis, overview. His295 is supposed to function as the internal acid-base catalyst in dehydrogenase activity. Glu263 stabilizes the protonated form of His295, and Arg234 forms a hydrogen bond with the nicotinamide ribose ring
homodimer
-
two identical monomers of DLDH744 are associated at the cofactor binding domain to form the homodimer in one asymmetric unit. The dimer interface is stabilized mainly by hydrogen-bonding interactions between residues from alpha-helices, alpha5(Ser102-Arg119), alpa6(Leu121-Glu130), alpha12(Glu279-Arg285) and connecting loops, structure analysis, overview. His295 is supposed to function as the internal acid-base catalyst in dehydrogenase activity. Glu263 stabilizes the protonated form of His295, and Arg234 forms a hydrogen bond with the nicotinamide ribose ring
-
homotetramer
4 * 40000, about, sequence calculation
homotetramer
-
4 * 40000, about, sequence calculation
-
additional information
-
interaction of enzyme with F-actin in vivo and in vitro
Information
