Intramitochondrial Localization of Kynurenine Aminotransferase
نویسندگان
چکیده
منابع مشابه
Intramitochondrial 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...
متن کاملCrystal structure of human kynurenine aminotransferase I.
The kynurenine pathway has long been regarded as a valuable target for the treatment of several neurological disorders accompanied by unbalanced levels of metabolites along the catabolic cascade, kynurenic acid among them. The irreversible transamination of kynurenine is the sole source of kynurenic acid, and it is catalyzed by different isoforms of the 5'-pyridoxal phosphate-dependent kynureni...
متن کاملKynurenine Aminotransferase Isozyme Inhibitors: A Review
Kynurenine aminotransferase isozymes (KATs 1-4) are members of the pyridoxal-5'-phosphate (PLP)-dependent enzyme family, which catalyse the permanent conversion of l-kynurenine (l-KYN) to kynurenic acid (KYNA), a known neuroactive agent. As KATs are found in the mammalian brain and have key roles in the kynurenine pathway, involved in different categories of central nervous system (CNS) disease...
متن کاملCharacteristic Features of Kynurenine Aminotransferase Allosterically Regulated by (Alpha)-Ketoglutarate in Cooperation with Kynurenine
Kynurenine aminotransferase from Pyrococcus horikoshii OT3 (PhKAT), which is a homodimeric protein, catalyzes the conversion of kynurenine (KYN) to kynurenic acid (KYNA). We analyzed the transaminase reaction mechanisms of this protein with pyridoxal-5'-phosphate (PLP), KYN and α-ketoglutaric acid (2OG) or oxaloacetic acid (OXA). 2OG significantly inhibited KAT activities in kinetic analyses, s...
متن کاملPurification and properties of kynurenine aminotransferase from rat kidney.
Previous reports indicated that a single protein exhibits kynurenine aminotransferase (KAT) and alpha-aminoadipate aminotransferase (AadAT) activities. However, recently we discovered that KAT and AadAT activities are associated with two different proteins. KAT from rat kidney supernatant fraction was purified to electrophoretic homogeneity by (NH4)2SO4 fractionation, DEAE-Sephacel and hydroxya...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1970
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)62968-0