Branched Chain Keto-Acids Exert Biphasic Effects on α-Ketoglutarate-Stimulated Respiration in Intact Rat Liver Mitochondria

2007 ◽  
Vol 32 (4-5) ◽  
pp. 947-951 ◽  
Author(s):  
Alexander I. Shestopalov ◽  
Bruce S. Kristal
Keyword(s):  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Keto Acids ◽  
Branched Chain ◽  
Branched Chain Keto Acids

Transamination of Ring-Substituted L-Phenylalanines by an Extract from Rat Liver Mitochondria

1973 ◽  
Vol 51 (4) ◽  
pp. 407-411 ◽  
Author(s):  
J. H. Tong ◽  
B. A. Stoochnoff ◽  
A. D'Iorio ◽  
N. Leo Benoiton
Keyword(s):  
Amino Acids ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Tyrosine Aminotransferase ◽  
Rat Liver Mitochondria ◽  
Amino Group ◽  
Mitochondrial Enzyme ◽  
Soluble Enzyme ◽  
Keto Acids ◽  
Mitochondrial Extract

The L- and D-isomers of m-tyrosine, o-tyrosine, p-chlorophenylalanine (p-CP), and p-fluorophenylalanine (p-FP) were tested as substrates for the soluble tyrosine aminotransferase and a mitochondrial extract of rat liver by measuring the amino acids formed with 2-oxoglutarate, oxaloacetate, and pyruvate as acceptors. None of the above were substrates for the soluble enzyme. L-m-Tyrosine, L-p-CP, and L-p-FP were transaminated at substantial rates (16–25% of the rate for L-tyrosine) by the mitochondrial enzyme with all three keto acids as amino group acceptors. A slow but definite transamination of L-o-tyrosine by the mitochondrial enzyme was demonstrated using labeled 2-oxoglutarate as acceptor.

scholarly journals Regulation of branched‐chain alpha‐ketoacid dehydrogenase (BCKDH) kinase by a Mn2+‐dependent factor in rat liver mitochondria

2013 ◽  
Vol 27 (S1) ◽  
Author(s):  
Takahiro Katayama ◽  
Yuya Itami ◽  
Zhen Hongmin ◽  
Takanari Toyota ◽  
Yasuyuki Kitaura ◽  
...  
Keyword(s):  
Rat Liver ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Branched Chain ◽  
Ketoacid Dehydrogenase ◽  
Dependent Factor
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