... expected, the substituted Lys forms a hydrogen bond with the substrate, stabilizing the complex. The enzymaticactivity of S329K is 2% of that of the wild-typeenzyme. The catalytic site structure of ... those of Mn1 (14.6, 17.7, 22.2and 15.5 A˚2), supporting the high mobility of Mn2 in the enzyme. The displacement of Mn2 does not affectgreatly the overall structure of the subunit. The smallmovement ... O3 on the same side of the sugar ring, and the enzyme may strictly recog-nize the configuration of the 2- and 3-positions at thisstage. However, other anomers of furanoses, b-d-psi-cofuranose...