scholarly journals Aspects of regulation of ketoglutarate dehydrogenase activity from ribbed mussel (Modiolus demissus) gills and cauliflower (Brassica oleracea)

1989 ◽  
Author(s):  
George Antun Karam
Keyword(s):  
Brassica Oleracea ◽  
Dehydrogenase Activity ◽  
Ribbed Mussel ◽  
Ketoglutarate Dehydrogenase

The role of sleep disturbances in depressive-like behavior with emphasis on α-ketoglutarate dehydrogenase activity in rats.

2020 ◽  
Vol 224 ◽  
pp. 113023
Author(s):  
Parastou Kordestani-Moghadam ◽  
Mohammad Nasehi ◽  
Salar Vaseghi ◽  
Fariba Khodagholi ◽  
Mohammad-Reza Zarrindast
Keyword(s):  
Dehydrogenase Activity ◽  
Sleep Disturbances ◽  
Ketoglutarate Dehydrogenase

Inhibition of α-ketoglutarate dehydrogenase activity affects adventitious root growth in poplar via changes in GABA shunt

Planta ◽  
2018 ◽  
Vol 248 (4) ◽  
pp. 963-979 ◽  
Author(s):  
Jianyun Yue ◽  
Changjian Du ◽  
Jing Ji ◽  
Tiantian Xie ◽  
Wei Chen ◽  
...  
Keyword(s):  
Root Growth ◽  
Dehydrogenase Activity ◽  
Adventitious Root ◽  
Gaba Shunt ◽  
Ketoglutarate Dehydrogenase

Activities of α-ketoisovalerate, pyruvate, and α-ketoglutarate dehydrogenases in a mutant of Bacillus subtilis

1976 ◽  
Vol 22 (4) ◽  
pp. 592-597
Author(s):  
C. L. Tu ◽  
Toshi Kaneda
Keyword(s):  
Bacillus Subtilis ◽  
Dehydrogenase Activity ◽  
Parent Strain ◽  
Keto Acid ◽  
Carboxylase Activity ◽  
Bacillus Subtilis 168 ◽  
Dihydrolipoyl Dehydrogenase ◽  
Ketoglutarate Dehydrogenase

An acetate-requiring leaky mutant was induced from Bacillus subtilis 168, and activities of its three α-keto acid dehydrogenases were compared with the respective activities of the parent strain. Both pyruvate and α-ketoisovalerate dehydrogenase activities in the mutant were considerably lower, being only 10–17% of those of the parent, but α-ketoglutarate dehydrogenase activity was unchanged. These dehydrogenases are complexes composed of three enzymes: a carboxylase, a lipoic reductase–transacylase, and a dihydrolipoyl dehydrogenase. The carboxylase activity of the affected complexes was no different. Total dihydrolipoyl dehydrogenase activity was only one-third. Thus dihydrolipoyl dehydrogenase is the defective enzyme in the two dehydrogenase complexes; the activity remaining in the mutant is accounted for by the activity of the intact α-ketoglutarate dehydrogenase.

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