Light-enhanced catalysis by pyridoxal phosphate-dependent aspartate aminotransferase

…, TA Addington, MD Toney, DS Larsen

Index: Hill, Melissa P.; Carroll, Elizabeth C.; Vang, Mai C.; Addington, Trevor A.; Toney, Michael D.; Larsen, Delmar S. Journal of the American Chemical Society, 2010 , vol. 132, # 47 p. 16953 - 16961

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Citation Number: 7

Abstract

The mechanisms of pyridoxal 5′-phosphate (PLP)-dependent enzymes require substrates to form covalent “external aldimine” intermediates, which absorb light strongly between 410 and 430 nm. Aspartate aminotransferase (AAT) is a prototypical PLP-dependent enzyme that catalyzes the reversible interconversion of aspartate and α-ketoglutarate with oxalacetate and glutamate. From kinetic isotope effects studies, it is known that ...