Xylulokinase
From Wikipedia, the free encyclopedia
Xylulokinase (EC 2.7.1.17) is an enzyme that catalyzes the chemical reaction
It was first characterised from Pasteurella pestis and Lactobacillus pentosus and converts the pentose sugar, D-xylulose, to D-xylulose 5-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1][2] The enzyme is also found in mammalian liver, where it is an important component of carbohydrate metabolism.[3][4][5]
This enzyme is a transferase, specifically one transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-xylulose 5-phosphotransferase. Other names in common use include xylulokinase (phosphorylating), and D-xylulokinase.[6]
