Spencer M, Blackburn P, Ferdinand W, Blackburn G M
Biochem J. 1973 Feb;131(2):421-3. doi: 10.1042/bj1310421.
UDP-6-deoxygalactose inhibits the UDP-galactose 4-epimerase (EC 5.1.3.2) from Escherichia coli in a competitive manner with respect to the substrate UDP-galactose, giving K(i) 1.3x10(-3)m. As a substrate for the enzyme, it is transformed into UDP-6-deoxyglucose, although the reaction stops before equilibrium is attained. Possible causes of this behaviour are discussed.
UDP-6-脱氧半乳糖以与底物UDP-半乳糖竞争的方式抑制来自大肠杆菌的UDP-半乳糖4-表异构酶(EC 5.1.3.2),抑制常数K(i)为1.3×10⁻³m。作为该酶的一种底物,它被转化为UDP-6-脱氧葡萄糖,尽管反应在达到平衡之前就停止了。文中讨论了这种行为可能的原因。