User:Raad Khidir/sandbox1 Choline Oxidase

From Proteopedia

Introduction

The Oxidoreductase enzyme choline oxidase is a double functional catabolic enzyme that catalyzes the synthesis of glycine betaine from choline through the intermediate betaine aldehyde (Rodwazowski, 1991). Oxidoreductases are enzymes that speed up chemical reactions by employing a mechanism of transferring electron, from electron donating molecules ( Reductants) to electron accepting molecules ( Oxidants). Choline Oxidase catabolyzes the reaction of the two substrates choline and oxygen by transferring electrons from C-OH of the choline substrate to the oxygen atom. The reaction would yield Betaine Aldehyde and Peroxide – through an intermediate Betaine Glycine-. Choline oxidase uses a cofactor, FAD. A cofactor is a non protein substance bound loosely or tightly to an enzyme and mandatory for the enzyme's function . Choline Oxidase uses the cofactor FAD ( Flavin Adenine Dineucleotide) is a redox cofactor that assists in transferring electrons by existing in two forms FAD and FADH. FADH is an energy carrying molecule. Mitochonderia happens to employ it in Oxidative Phosphorylation then FADH2 re oxidizes back to FAD and create a proton gradient for the transfer of the enzyme ATP synthase. Plants adapt to Osmotic fluctuations and temperature differences through forming an osmoprotective layer of organic compounds. Betaine Aldehyde, the intermediate of the reaction is an Osmolyte that helps plants withstand osmotic changes. Betaine Aldehyde along with its precursor are used by microorganisms as carbon and Nitrogen sources (Rodwazowski, 1991).