Literature DB >> 5866654

Lactate dehydrogenase Isozymes: substrate inhibition in various human tissues.

E S Vesell.   

Abstract

The total lactate dehydrogenase (LDH) in whole homogenates of various human tissues reacts more similarly toward pyruvate and lactate at 25 degrees C than expected from the marked differences in substrate inhibition at this temperature between isolated, purified LDH-1, and LDH-5. At 37 degrees C, LDH-5 closely resembles LDH-1 in extent of inhibition by substrate. These results are incompatible with the theory that differences in degree of isozyme inhibition by substrate have resulted in predominance of LDH-5 in aerobic tissues and predominance of LDH-1 in aerobic tissues.

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Year:  1965        PMID: 5866654     DOI: 10.1126/science.150.3703.1590

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  12 in total

1.  A genetically determined variant of the A-subunit of lactic dehydrogenase in the deer mouse.

Authors:  B M Cattanach; J N Perez
Journal:  Biochem Genet       Date:  1969-10       Impact factor: 1.890

2.  Lactate and pyruvate concentrations in exercised ischemic canine muscle: relationship of tissue substrate level to lactate dehydrogenase isozyme pattern.

Authors:  E S Vesell; P E Pool
Journal:  Proc Natl Acad Sci U S A       Date:  1966-04       Impact factor: 11.205

3.  Lactate dehydrogenase isozymes: qualitative and quantitative changes during primate evolution.

Authors:  A L Koen; M Goodman
Journal:  Biochem Genet       Date:  1969-10       Impact factor: 1.890

Review 4.  The nature of isoenzymes.

Authors:  A L Latner
Journal:  J Clin Pathol Suppl (Assoc Clin Pathol)       Date:  1970

5.  Double genetic disruption of lactate dehydrogenases A and B is required to ablate the "Warburg effect" restricting tumor growth to oxidative metabolism.

Authors:  Maša Ždralević; Almut Brand; Lorenza Di Ianni; Katja Dettmer; Jörg Reinders; Katrin Singer; Katrin Peter; Annette Schnell; Christina Bruss; Sonja-Maria Decking; Gudrun Koehl; Blanca Felipe-Abrio; Jérôme Durivault; Pascale Bayer; Marie Evangelista; Thomas O'Brien; Peter J Oefner; Kathrin Renner; Jacques Pouysségur; Marina Kreutz
Journal:  J Biol Chem       Date:  2018-08-29       Impact factor: 5.157

Review 6.  The multiple roles of LDH in cancer.

Authors:  Giuseppina Claps; Sara Faouzi; Virginie Quidville; Feras Chehade; Shensi Shen; Stéphan Vagner; Caroline Robert
Journal:  Nat Rev Clin Oncol       Date:  2022-10-07       Impact factor: 65.011

7.  Structure-based mutational studies of substrate inhibition of betaine aldehyde dehydrogenase BetB from Staphylococcus aureus.

Authors:  Chao Chen; Jeong Chan Joo; Greg Brown; Ekaterina Stolnikova; Andrei S Halavaty; Alexei Savchenko; Wayne F Anderson; Alexander F Yakunin
Journal:  Appl Environ Microbiol       Date:  2014-04-18       Impact factor: 4.792

8.  The isoenzyme pattern of LDH does not play a physiological role; except perhaps during fast transitions in energy metabolism.

Authors:  Bjørn Quistorff; Niels Grunnet
Journal:  Aging (Albany NY)       Date:  2011-05       Impact factor: 5.682

9.  A mechanistic kinetic description of lactate dehydrogenase elucidating cancer diagnosis and inhibitor evaluation.

Authors:  Peifeng Tang; Jianlin Xu; Christopher L Oliveira; Zheng Jian Li; Shijie Liu
Journal:  J Enzyme Inhib Med Chem       Date:  2017-12       Impact factor: 5.051

10.  The cellular and compartmental profile of mouse retinal glycolysis, tricarboxylic acid cycle, oxidative phosphorylation, and ~P transferring kinases.

Authors:  Elda M Rueda; Jerry E Johnson; Anand Giddabasappa; Anand Swaroop; Matthew J Brooks; Irena Sigel; Shawnta Y Chaney; Donald A Fox
Journal:  Mol Vis       Date:  2016-07-23       Impact factor: 2.367

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