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Information on EC 1.1.5.B3 - quinone dependent L-lactate dehydrogenase
for references in articles please use BRENDA:EC1.1.5.B3
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preliminary BRENDA-supplied EC number
EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.5 With a quinone or similar compound as acceptor
1.1.5.B3 quinone dependent L-lactate dehydrogenase
The enzyme appears in viruses and cellular organisms
showSynonyms
quinone-dependent l-lactate dehydrogenase, pqq-ldh, pqq-dependent lactate dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
PQQ-dependent lactate dehydrogenase
PQQ-LDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lactate + quinone = pyruvate + quinol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-lactate:quinone oxidoreductase
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lactate + 2,6-dichlorophenol indophenol
pyruvate + reduced 2,6-dichlorophenol indophenol
L-lactate + oxidized 2,6-dichlorophenol indophenol
pyruvate + reduced 2,6-dichlorophenol indophenol
-
Substrates: stereospecific for L-lactate
Products: -
Products: -
?
L-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenol indophenol
pyruvate + reduced 2,6-dichlorophenol indophenol
-
Substrates: reduction of the acceptor 2,6-dichlorophenol indophenol is mediated by phenazine methosulfate
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenol indophenol
pyruvate + reduced 2,6-dichlorophenol indophenol
-
Substrates: reduction of the acceptor 2,6-dichlorophenol indophenol is mediated by phenazine methosulfate
Products: -
Products: -
?
L-lactate + 2,6-dichlorophenol indophenol
pyruvate + reduced 2,6-dichlorophenol indophenol
Gluconobacter sp. DSM 3504 / ATCC 15163
-
Substrates: reduction of the acceptor 2,6-dichlorophenol indophenol is mediated by phenazine methosulfate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lactate + oxidized 2,6-dichlorophenolindophenol
pyruvate + reduced 2,6-dichlorophenolindophenol
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phenazine methosulfate
-
mediates reduction of 2,6-dichlorophenol-indophenol
phenazine methosulfate
-
mediates reduction of 2,6-dichlorophenol-indophenol
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme expression is supressed/regulated by the FadR-type regulator LldR, encoded by NCgl2814, binds to the upstream region of NCgl2816-lldD, L-lactate prevents binding of LldRHis to the NCgl2816-lldD promoter region
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the enzyme expression is induced by a temperature shift and by growth on L-lactate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.3
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
disruption of the ldhD-NCgl2816 operon results in loss of the ability to utilize L-lactate as sole carbon source, the ability can be restored by expression of gene ldhD, overview
additional information
-
overexpression of the regulator gene lldR results in strongly reduced NCgl2816-lldD mRNA levels and strongly reduced LldD activity, and as a consequence, in a severe growth defect was observed in cells grown on L-lactate as the sole carbon and energy source, but not in cells grown on glucose, ribose, or acetate. Deletion of lldR has no effect on growth on these carbon sources but results in high NCgl2816-lldD mRNA levels and high LldD activity in the presence and absence of L-lactate, overview
additional information
-
bioanode fabrication using the partially purified enzyme immobilized on a membrane, usage of carbon fiber paper, overview
additional information
Gluconobacter sp. DSM 3504 / ATCC 15163
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bioanode fabrication using the partially purified enzyme immobilized on a membrane, usage of carbon fiber paper, overview
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from membranes by solubilization with Triton X-100 and anion exchange chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene ldhD, DNA microarray expression analysis, gene ldhD acts in an operon with the permease gene NCgl2816
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
biotechnology
-
the PQQ-dependent lactate dehydrogenase from Gluconobacter is capable of direct electron transfer at carbon and gold electrodes, which makes it useful for application in biosensors or biofuel cells, overview
biotechnology
-
the PQQ-dependent lactate dehydrogenase from Gluconobacter is capable of direct electron transfer at carbon and gold electrodes, which makes it useful for application in biosensors or biofuel cells, overview
biotechnology
Gluconobacter sp. DSM 3504 / ATCC 15163
-
the PQQ-dependent lactate dehydrogenase from Gluconobacter is capable of direct electron transfer at carbon and gold electrodes, which makes it useful for application in biosensors or biofuel cells, overview
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Stansen, C.; Uy, D.; Delaunay, S.; Eggeling, L.; Goergen, J.-L.; Wendisch, V.F.
Characterization of a Corynebacterium glutamicum lactate utilization operon induced during temperature-triggered glutamate production
Appl. Environ. Microbiol.
71
5920-5928
2005
Corynebacterium glutamicum
brenda
Treu, B.L.; Minteer, S.D.
Isolation and purification of PQQ-dependent lactate dehydrogenase from Gluconobacter and use for direct electron transfer at carbon and gold electrodes
Bioelectrochemistry
74
73-77
2008
Gluconobacter oxydans, Gluconobacter sp., Gluconobacter sp. DSM 3504 / ATCC 15163
brenda
Georgi, T.; Engels, V.; Wendisch, V.F.
Regulation of L-lactate utilization by the FadR-type regulator LldR of Corynebacterium glutamicum
J. Bacteriol.
190
963-971
2008
Corynebacterium glutamicum
brenda
EXTERNAL LINKS (specific for EC-Number 1.1.5.B3)
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Release 2023.1 (January 2023)
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