Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.1.99.40 - (R)-2-hydroxyglutarate-pyruvate transhydrogenase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P39976

for references in articles please use BRENDA:EC1.1.99.40
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P39976
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
Synonyms
D-2-hydroxyglutarate-pyruvate transhydrogenase, DLD3, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-2-hydroxyglutarate-pyruvate transhydrogenase
-
DLD3
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(R)-2-hydroxyglutarate:pyruvate oxidoreductase [(R)-lactate-forming]
The enzyme, characterized in the yeast Saccharomyces cerevisiae, also functions as EC 1.1.2.4, D-lactate dehydrogenase (cytochrome), and is active with oxaloacetate as electron acceptor forming (R)-malate.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + D-lactate
D-2-hydroxyglutarate + pyruvate
show the reaction diagram
-
-
-
r
D-2-hydroxyglutarate + oxaloacetate
2-oxoglutarate + malate
show the reaction diagram
-
-
-
r
D-2-hydroxyglutarate + pyruvate
2-oxoglutarate + D-lactate
show the reaction diagram
-
-
-
r
additional information
?
-
no substrate: L-lactate. The enzyme displays dehydrogenase activity with artificial acceptor dichlorophenolindophenol
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
enzyme is a FAD-dependent transhydrogenase using pyruvate as a hydrogen acceptor
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.005 mM, about 3fold stimulation
Zn2+
0.005 mM, about 3fold stimulation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.111
D-2-hydroxyglutarate
pH 9.5, 30°C
0.45
pyruvate
pH 9.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
D-2-hydroxyglutarate
pH 9.5, 30°C
4.9
pyruvate
pH 9.5, 30°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
36
D-2-hydroxyglutarate
pH 9.5, 30°C
12
pyruvate
pH 9.5, 30°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
a mutant strain lacking cytosolic transhydrogenase Dld3 activity accumulates millimolar levels of D-2-hydroxyglutarate
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein. Purified fractions show a yellow color
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Becker-Kettern, J.; Paczia, N.; Conrotte, J.F.; Kay, D.P.; Guignard, C.; Jung, P.P.; Linster, C.L.
Saccharomyces cerevisiae forms D-2-hydroxyglutarate and couples its degradation to D-lactate formation via a cytosolic transhydrogenase
J. Biol. Chem.
291
6036-6058
2016
Saccharomyces cerevisiae (P39976)
Manually annotated by BRENDA team