Fan D F, Feingold D S
Plant Physiol. 1970 Oct;46(4):592-5. doi: 10.1104/pp.46.4.592.
Uridine diphosphate (UDP)-arabinose 4-epimerase (EC 5.1.3.5) has been purified at least 20-fold from wheat germ by MnCl(2) treatment, (NH(4))(2)SO(4) fractionation, dialysis, and Sephadex and diethylaminoethyl cellulose column chromatography. The enzyme has no action on UDP-d-glucose, UDP-d-glucuronic acid, or TDP-d-glucose. The pH optimum is 8.0. Km values are 1.5 mM for UDP-d-xylose and 0.5 mm for UDP-l-arabinose. The equilibrium constant, K, for the reaction UDP-l-arabinose left arrow over right arrow UDP-d-xylose is 1.25. The enzyme is neither activated by nicotinamide adenine dinucleotide nor inhibited by reduced nicotinamide adenine dinucleotide. It is completely inhibited by p-chloromercuri-phenylsulfonate; the inhibition is reversed by cysteine.
尿苷二磷酸(UDP)-阿拉伯糖4-表异构酶(EC 5.1.3.5)已通过氯化锰处理、硫酸铵分级分离、透析以及葡聚糖凝胶和二乙氨基乙基纤维素柱色谱法从小麦胚芽中纯化了至少20倍。该酶对UDP-D-葡萄糖、UDP-D-葡萄糖醛酸或TDP-D-葡萄糖无作用。最适pH为8.0。UDP-D-木糖的Km值为1.5 mM,UDP-L-阿拉伯糖的Km值为0.5 mM。反应UDP-L-阿拉伯糖⇌UDP-D-木糖的平衡常数K为1.25。该酶既不被烟酰胺腺嘌呤二核苷酸激活,也不被还原型烟酰胺腺嘌呤二核苷酸抑制。它被对氯汞苯磺酸盐完全抑制;半胱氨酸可逆转这种抑制作用。