LDH tetramer reduces PYR to LACT

Stable Identifier
R-HSA-71849
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
Pyruvate + NADH + H+ <=> (S)-Lactate + NAD+
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
Cytosolic lactate dehydrogenase (LDH) catalyzes the freely reversible reaction of pyruvate (PYR) and NADH + H+ to form lactate (LACT) and NAD+ (reviewed in Khan et al., 2020). In liver parenchymal cells, this reaction allows lactate from red blood cells and exercising muscle to be converted to pyruvate which in turn is typically used for gluconeogenesis which also consumes the NADH from the reaction.

Lactate dehydrogenase is active as a tetramer. Two isoforms of lactate dehydrogenase, A and B, are widely expressed in human tissues, and all five tetramers - A4, A3B, A2B2, AB3, and B4 - are found (Read et al. 2001; Sakai et al. 1987; Yu et al. 2001). A third isoform, C, and its tetramer, C4, are found in testis (Millan et al. 1987; LeVan & Goldberg 1991). A fourth isoform, LDHAL6A, is less fully characterized than these others but limited data suggest that it may be testis-specific (Chen et al. 2009). LDH activity, but not protein level, is negatively regulated by ubiquitination of the LDHA subunit (Maitland et al., 2021).

Literature References
PubMed ID Title Journal Year
3435492 The cDNA and protein sequences of human lactate dehydrogenase B

Sharief, FS, Li, SS, Pan, YC, Sakai, I

Biochem J 1987
18351441 Identification of a novel human lactate dehydrogenase gene LDHAL6A, which activates transcriptional activities of AP1(PMA)

Wang, Y, Yu, L, Yuan, J, Gu, X, Zhong, Z, Wan, B, Shan, Y, Tang, W, Huang, W, Chen, X

Mol. Biol. Rep. 2009
2440048 Epitopes of human testis-specific lactate dehydrogenase deduced from a cDNA sequence

Millan, JL, Driscoll, CE, LeVan, KM, Goldberg, E

Proc. Natl. Acad. Sci. U.S.A. 1987
11377399 Selective active site inhibitors of human lactate dehydrogenases A4, B4, and C4

Vander Jagt, DL, Royer, RE, Deck, LM, Hunsaker, LA, Deck, JA, Yu, Y, Goldberg, E

Biochem Pharmacol 2001
1996957 Properties of human testis-specific lactate dehydrogenase expressed from Escherichia coli

LeVan, KM, Goldberg, E

Biochem. J. 1991
34383978 Proteomic analysis of ubiquitination substrates reveals a CTLH E3 ligase complex-dependent regulation of glycolysis

Schild-Poulter, C, Kuljanin, M, Lajoie, GA, Maitland, MER, Wang, X

FASEB J 2021
31886754 The Biochemical and Clinical Perspectives of Lactate Dehydrogenase: An Enzyme of Active Metabolism

Alhumaydhi, FA, Khan, AA, Rahmani, AH, Allemailem, KS, Gowder, SJT

Endocr Metab Immune Disord Drug Targets 2020
11276087 Structural basis for altered activity of M- and H-isozyme forms of human lactate dehydrogenase

Eszes, CM, Brady, RL, Read, JA, Winter, VJ, Sessions, RB

Proteins 2001
Participants
Participates
Event Information
Catalyst Activity

L-lactate dehydrogenase activity of LDH tetramer [cytosol]

This event is regulated
Negatively by
Orthologous Events
Cross References
RHEA
Rhea
Reviewed
Cite Us!