|
Phosphopentose epimerase (also known as ribulose-phosphate 3-epimerase and ribulose 5-phosphate 3-epimerase)() is a metalloprotein that catalyzes the interconversion between D-ribulose 5-phosphate and D-xylulose 5-phosphate.〔 :D-ribulose 5-phosphate D-xylulose 5-phosphate This reversible conversion is required for carbon fixation in plants – through the Calvin cycle – and for the nonoxidative phase of the pentose phosphate pathway. This enzyme has also been implicated in additional pentose and glucuronate interconversions. In ''Alcaligenes eutrophus'' two copies of the gene coding for PPE are known, one is chromosomally encoded , the other one is on a plasmid . PPE has been found in a wide range of bacteria, archaebacteria, fungi and plants. All the proteins have from 209 to 241 amino acid residues. The enzyme has a TIM barrel structure. == Nomenclature == The systematic name of this enzyme class is D-ribulose-5-phosphate 3-epimerase. Other names in common use include * phosphoribulose epimerase, * erythrose-4-phosphate isomerase, * phosphoketopentose 3-epimerase, * xylulose phosphate 3-epimerase, * phosphoketopentose wpimerase, * ribulose 5-phosphate 3-epimerase, * D-ribulose phosphate-3-epimerase, * D-ribulose 5-phosphate wpimerase, * D-ribulose-5-P 3-epimerase, * D-xylulose-5-phosphate 3-epimerase, and * pentose-5-phosphate 3-epimerase. This enzyme participates in 3 metabolic pathways: pentose phosphate pathway, pentose and glucuronate interconversions, and carbon fixation. The human protein containing this domain is the RPE (gene). 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Phosphopentose epimerase」の詳細全文を読む スポンサード リンク
|