Catabolism of GABA, succinic semialdehyde or gamma-hydroxybutyrate through the GABA shunt impair mitochondrial substrate-level phosphorylation

2017 ◽  
Vol 109 ◽  
pp. 41-53 ◽  
Author(s):  
Dora Ravasz ◽  
Gergely Kacso ◽  
Viktoria Fodor ◽  
Kata Horvath ◽  
Vera Adam-Vizi ◽  
...  
Keyword(s):  
Succinic Semialdehyde ◽  
Gaba Shunt ◽  
Substrate Level Phosphorylation ◽  
Gamma Hydroxybutyrate ◽  
Substrate Level

scholarly journals Increasing Mitochondrial Substrate-level Phosphorylation Can Rescue Respiratory Growth of an ATP Synthase-deficient Yeast

2005 ◽  
Vol 280 (35) ◽  
pp. 30751-30759 ◽  
Author(s):  
Christine Schwimmer ◽  
Linnka Lefebvre-Legendre ◽  
Malgorzata Rak ◽  
Anne Devin ◽  
Piotr P. Slonimski ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Substrate Level Phosphorylation ◽  
Substrate Level ◽  
Respiratory Growth

scholarly journals Zinc-dependent substrate-level phosphorylation powers Salmonella growth under nitrosative stress of the innate host response

2018 ◽  
Vol 14 (10) ◽  
pp. e1007388 ◽  
Author(s):  
Liam Fitzsimmons ◽  
Lin Liu ◽  
Steffen Porwollik ◽  
Sangeeta Chakraborty ◽  
Prerak Desai ◽  
...  
Keyword(s):  
Host Response ◽  
Nitrosative Stress ◽  
Substrate Level Phosphorylation ◽  
Substrate Level

Decisive role of mitochondrial substrate level phosphorylation on the survival of glutaminolytic cancer cells

2018 ◽  
Vol 1859 ◽  
pp. e102
Author(s):  
Judit Dóczi ◽  
Gergely Horváth ◽  
László Tretter ◽  
Vera Ádám-Vizi ◽  
Christos Chinopoulos
Keyword(s):  
Cancer Cells ◽  
Decisive Role ◽  
Substrate Level Phosphorylation ◽  
Substrate Level

scholarly journals Inhibition of Fructolysis in Boar Spermatozoa by the Male Antifertility Agent (S)-a-Chlorohydrin

1982 ◽  
Vol 35 (6) ◽  
pp. 595 ◽  
Author(s):  
Denise Stevenson ◽  
A RJones
Keyword(s):  
Oxidative Metabolism ◽  
Inhibitory Activity ◽  
Energy Charge ◽  
Substrate Level Phosphorylation ◽  
Charge Potential ◽  
Substrate Level ◽  
Glyceraldehydephosphate Dehydrogenase ◽  
Fructose 1,6 Bisphosphate ◽  
Boar Spermatozoa

The (S)-isomer of the male antifertility agent IX-chlorohydrin strongly inhibited the oxidative metabolism of fructose by boar spermatozoa in vitro. The result of this action, which has been deduced to be an inhibition of glyceraldehydephosphate dehydrogenase, caused an accumulation of fructose- 1,6-bisphosphate and the triosephosphates, and a decrease in substrate-level phosphorylation with a concomitant lowering of the energy charge potential of the spermatozoa. The (R)-isomer of IX-chlorohydrin had no inhibitory activity on fructolysis.

scholarly journals Mitochondrial Target of Nobiletin's Action

2016 ◽  
Vol 11 (12) ◽  
pp. 1934578X1601101 ◽  
Author(s):  
Nino Sharikadze ◽  
Natia Jojua ◽  
Maia Sepashvili ◽  
Elene Zhuravliova ◽  
David G Mikeladze
Keyword(s):  
Oxygen Consumption ◽  
Membrane Potential ◽  
Cell Types ◽  
Bovine Brain ◽  
Oxidoreductase Activity ◽  
Substrate Level Phosphorylation ◽  
Mitochondrial Target ◽  
Substrate Level ◽  
Transient Elevation ◽  
Ketoglutarate Dehydrogenase

Nobiletin is an O-methylated flavonoid found in citrus peels that have anticancer, antiviral, neuroprotective, anti-inflammatory activities and depending on the cell types exhibits both pro- or anti-apoptotic properties. We have found that nobiletin decreases oxygen consumption by bovine brain isolated mitochondria in the presence of glutamate and malate and increases in the presence of succinate. In parallel, nobiletin increases NADH oxidation, a-ketoglutarate dehydrogenase activities and through matrix substrate-level phosphorylation elevates the a-ketoglutarate-dependent production of ATP. In addition, nobiletin reduces the production of peroxides in the presence of complex I substrates and slightly enhances succinate-driven H2O2 formation. Besides, nobiletin induces transient elevation of membrane potential followed by mild depolarization. Affinity purified nobiletin binding proteins revealed one major anti-NDUFV1 positive protein with 52kD and NADH: ubiquinone oxidoreductase activity. This fraction can produce peroxide that is inhibited by nobiletin. We propose that nobiletin may act as a mild “uncoupler”, which through activation of a-ketoglutarate dehydrogenase (a-KGDH)-complex and acceleration of matrix substrate-level phosphorylation maintains membrane potential at an abnormal level. This switch in mitochondrial metabolism could elevate succinate-driven oxygen consumption that may underlay in both pro- and anti-apoptotic effects of nobiletin.

scholarly journals Reconstitution of the Biochemical Activities of the AttJ Repressor and the AttK, AttL, and AttM Catabolic Enzymes of Agrobacterium tumefaciens

2007 ◽  
Vol 189 (9) ◽  
pp. 3674-3679 ◽  
Author(s):  
Yunrong Chai ◽  
Ching Sung Tsai ◽  
Hongbaek Cho ◽  
Stephen C. Winans
Keyword(s):  
Agrobacterium Tumefaciens ◽  
Succinic Semialdehyde ◽  
Metabolic Intermediates ◽  
Acylhomoserine Lactone ◽  
Catabolic Enzymes ◽  
Gamma Hydroxybutyrate ◽  
Gamma Butyrolactone

ABSTRACT The attKLM operon encodes a lactonase (AttM) that hydrolyzes acylhomoserine lactone autoinducers, as well as two putative dehydrogenases (AttK and AttL). Here we show that AttK, AttL, and AttM collectively covert gamma-butyrolactone to succinate. Two metabolic intermediates, gamma-hydroxybutyrate and succinic semialdehyde, inactivated the AttJ repressor in vitro and induced attKLM transcription in vivo.

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