Nicotinate Phosphoribosyltransferase of Human Erythrocytes
نویسندگان
چکیده
منابع مشابه
Crystal structure of a nicotinate phosphoribosyltransferase from Thermoplasma acidophilum.
We have determined the crystal structure of nicotinate phosphoribosyltransferase from Themoplasma acidophilum (TaNAPRTase). The TaNAPRTase has three domains, an N-terminal domain, a central functional domain, and a unique C-terminal domain. The crystal structure revealed that the functional domain has a type II phosphoribosyltransferase fold that may be a common architecture for both nicotinic ...
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Nicotinamide adenine dinucleotide (NAD) is a cofactor in redox reactions and a substrate for NAD-consuming enzymes, such as PARPs and sirtuins. As cancer cells have increased NAD requirements, the main NAD salvage enzymes in humans, nicotinamide phosphoribosyltransferase (NAMPT) and nicotinate phosphoribosyltransferase (NAPRT), are involved in the development of novel anti-cancer therapies. Kno...
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We have determined the crystal structure of porcine quinolinate phosphoribosyltransferase (QAPRTase) in complex with nicotinate mononucleotide (NAMN), which is the first crystal structure of a mammalian QAPRTase with its reaction product. The structure was determined from protein obtained from the porcine kidney. Because the full protein sequence of porcine QAPRTase was not available in either ...
متن کاملHuman Hypoxanthine Phosphoribosyltransferase
Hypoxanthine phosphoribosyltransferase (inosine monophosphate: pyrophosphate phosphoribosyltransferase EC 2.4.2.8) has been purified SO-fold from an acid-treated lysate of human erythrocytes. The average particle weight of the enzyme was estimated by gel filtration at 60,000. Between the pH values of 7.1 and 9.1 no marked difference in the initial velocity of IMP synthesis was observed. Kinetic...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1973
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)43957-4