Information on EC 1.1.99.40 - (R)-2-hydroxyglutarate-pyruvate transhydrogenase

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.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

top print hide
EC NUMBER
COMMENTARY hide
1.1.99.40
-
top print hide
RECOMMENDED NAME
GeneOntology No.
(R)-2-hydroxyglutarate-pyruvate transhydrogenase
-
top print hide
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate
show the reaction diagram
-
-
-
-
top print hide
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pyruvate metabolism
-
-
top print hide
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.
top
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
top print hide
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
a mutant strain lacking cytosolic transhydrogenase Dld3 activity accumulates millimolar levels of D-2-hydroxyglutarate
top print hide
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
-
-
-
top print hide
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
enzyme is a FAD-dependent transhydrogenase using pyruvate as a hydrogen acceptor
top print hide
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
0.005 mM, about 3fold stimulation
Zn2+
0.005 mM, about 3fold stimulation
top print hide
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
top print hide
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
top print hide
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
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein. Purified fractions show a yellow color
top
top
top
LINKS TO OTHER DATABASES (specific for EC-Number 1.1.99.40)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)