Genomics | Bioinorganic Chemistry | Biocatalysis | Macromolecular Chemistry | Protein Chemistry & Proteomics | Medical Genetics
Molecular characterization of buffalo xanthine oxidoreductase: A major fraction (>85%) is catalytically defective
Gadave Kaustubh Subhash, Surender Singh, K Sudarshan, Ashok K Mohanty, Druba Malakar, Jai K Kaushik*
*Corresponding author: Jai K Kaushik
Animal Biotechnology Centre, National Dairy Research Institute, Haryana, India
F1000Posters 2011, 2: 86 (poster) [ENGLISH]
Poster [887.73 KB]
79th Society of Biological Chemists (India) meeting 2010, 13 - 15 Dec 2010, R001
Xanthine oxidoreductase (XOR) is a complex molybdoflavin enzyme present in bacteria of higher eukaryotes. XOR is best known as an evolutionarily conserved housekeeping enzyme. In the Asian subcontinent a sizable amount of milk comes from the buffalo; buffalo milk contains a higher fat percentage in comparison to cattle. Its consumption may have a certain effect on its consumer’s health due to the implication of XOR in gout. Given that XOR is closely associated with MFGM, lactogenesis and several other diseases involving hyper activity of XOR or functional deletion due to mutation in the XOR gene, it is important to understand the molecular properties of this important enzyme in buffalo’s milk as it is an important source of nutrients in India.
Studies on the molecular characterization of buffalo XOR would help understand this important enzyme with respect to its physiochemical & biochemical properties, as well as sequence variation in comparison with other species.
Studies of XOR show that the xanthine oxidase (XO) activity of buffalo was lower than that of cattle XO. A lower amount of Mo and Mo=S as compared to cattle could be the reason for the lower activity in buffalo XOR.
Further studies are required to determine XOR’s structure and its Molybdopterin biosynthetic pathways.
No relevant conflicts of interest declared.
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