Biochemical and structural characterization of mouse mitochondrial aspartate aminotransferase, a newly identified kynurenine aminotransferase-IV
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چکیده
منابع مشابه
Kynurenine aminotransferase and glutamine transaminase K of Escherichia coli: identity with aspartate aminotransferase.
The present study describes the isolation of a protein from Escherichia coli possessing kynurenine aminotransferase (KAT) activity and its identification as aspartate aminotransferase (AspAT). KAT catalyses the transamination of kynurenine and 3-hydroxykynurenine to kynurenic acid and xanthurenic acid respectively, and the enzyme activity can be easily detected in E. coli cells. Separation of t...
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The activity of aspartate aminotransferase (AST) in human serum has been widely determined as a diagnostic aid in liver disease. In this study, the effect of aluminium on AST isoenzymes in relation to aluminium intoxified patients has been investigated. Using gel filtration chromatography technique with Sephacryl S-300, mitochondrial aminotransferase (m-AST) and cytosolic aminotransferase (c-AS...
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Kynurenic acid (KYNA) can act as an endogenous modulator of excitatory neurotransmission and has been implicated in the pathogenesis of several neurological and psychiatric diseases. To evaluate its role in the brain, we disrupted the murine gene for kynurenine aminotransferase II (KAT II), the principal enzyme responsible for the synthesis of KYNA in the rat brain. mKat-2(-/-) mice showed no d...
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Aspartate: 2-oxoglutarate aminotransferase from the anaerobic protozoon Trichomonas vaginalis was purified to homogeneity and characterized. It is a dimeric protein of overall Mr approx. 100000. Only a single isoenzyme was found in T. vaginalis. The overall molecular and catalytic properties have features in common with both the vertebrate cytoplasmic and mitochondrial isoenzymes. The purified ...
متن کاملIntramitochondrial localization of kynurenine aminotransferase.
Comparisons with the distribution of intramitochondrial marker enzymes have indicated that kynurenine aminotransferase is present in the inner membrane fraction of rat liver mitochondria. It appears to be weakly bound to the inner membrane because it is easily solubilized by increasing the concentration of digitonin. With the use of a-ketoglutarate or oxalacetate as amino group acceptor, the am...
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ژورنال
عنوان ژورنال: Bioscience Reports
سال: 2011
ISSN: 0144-8463,1573-4935
DOI: 10.1042/bsr20100117