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

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EC Tree

1 Oxidoreductases

1.1 Acting on the CH-OH group of donors

1.1.99 With unknown physiological acceptors

1.1.99.40 (R)-2-hydroxyglutarate-pyruvate transhydrogenase

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.

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The enzyme appears in viruses and cellular organisms

Reaction Schemes

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(R)-2-hydroxyglutarate

pyruvate

2-oxoglutarate

(R)-lactate

Synonyms

D-2-hydroxyglutarate-pyruvate transhydrogenase, DLD3, show all synonyms

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SYNONYM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D-2-hydroxyglutarate-pyruvate transhydrogenase

Saccharomyces cerevisiae

P39976

740757

DLD3

2 entries

DLD3

Saccharomyces cerevisiae

P39976

740757

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REACTION

REACTION DIAGRAM

COMMENTARY

ORGANISM

UNIPROT

LITERATURE

(R)-2-hydroxyglutarate + pyruvate = 2-oxoglutarate + (R)-lactate

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Go to Pathway Search

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PATHWAY SOURCE

PATHWAYS

KEGG

Pyruvate metabolism

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SYSTEMATIC NAME

IUBMB Comments

(R)-2-hydroxyglutarate:pyruvate oxidoreductase [(R)-lactate-forming]

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SUBSTRATE

PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

COMMENTARY
(Substrate)

LITERATURE
(Substrate)

COMMENTARY
(Product)

LITERATURE
(Product)

Reversibility
r=reversible
ir=irreversible
?=not specified

2-oxoglutarate + D-lactate

D-2-hydroxyglutarate + pyruvate

Saccharomyces cerevisiae

P39976

740757

D-2-hydroxyglutarate + oxaloacetate

2-oxoglutarate + malate

Saccharomyces cerevisiae

P39976

740757

D-2-hydroxyglutarate + pyruvate

2-oxoglutarate + D-lactate

Saccharomyces cerevisiae

P39976

740757

additional information

Saccharomyces cerevisiae

P39976

no substrate: L-lactate. The enzyme displays dehydrogenase activity with artificial acceptor dichlorophenolindophenol

740757

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

FAD

Saccharomyces cerevisiae

P39976

enzyme is a FAD-dependent transhydrogenase using pyruvate as a hydrogen acceptor

740757

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Co2+

Saccharomyces cerevisiae

P39976

0.005 mM, about 3fold stimulation

740757

Zn2+

Saccharomyces cerevisiae

P39976

0.005 mM, about 3fold stimulation

740757

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.111

D-2-hydroxyglutarate

Saccharomyces cerevisiae

P39976

pH 9.5, 30°C

740757

0.45

pyruvate

Saccharomyces cerevisiae

P39976

pH 9.5, 30°C

740757

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

D-2-hydroxyglutarate

Saccharomyces cerevisiae

P39976

pH 9.5, 30°C

740757

4.9

pyruvate

Saccharomyces cerevisiae

P39976

pH 9.5, 30°C

740757

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kcat/KM VALUE [1/mMs^-1]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

D-2-hydroxyglutarate

Saccharomyces cerevisiae

P39976

pH 9.5, 30°C

740757

pyruvate

Saccharomyces cerevisiae

P39976

pH 9.5, 30°C

740757

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

Saccharomyces cerevisiae

740757

P39976

UniProt

brenda

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

cytosol

Saccharomyces cerevisiae

brenda

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

Saccharomyces cerevisiae

P39976

a mutant strain lacking cytosolic transhydrogenase Dld3 activity accumulates millimolar levels of D-2-hydroxyglutarate

740757

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

P46681 pBLAST

DLD2_YEAST

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

530

59268

Swiss-Prot

Show Sequence

Mitochondrion (Reliability: 2)

P39976 pBLAST

DLD3_YEAST

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

496

55225

Swiss-Prot

Show Sequence

other Location (Reliability: 3)

A0A371C0P1 pBLAST

A0A371C0P1_YARLL

Yarrowia lipolytica

541

59774

TrEMBL

Show Sequence

Mitochondrion (Reliability: 1)

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PURIFICATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

recombinant protein. Purified fractions show a yellow color

Saccharomyces cerevisiae

P39976

740757

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

740757

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)

26774271

brenda

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EXTERNAL LINKS (specific for EC-Number 1.1.99.40)

NCBI: PubMed, Protein, Nucleotide, Structure, Gene, OMIM

IUBMB Enzyme Nomenclature

UniProt

PDB

PROSITE Database of protein families and domains

InterPro (database of protein families, domains and functional sites)

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