Effect of alpha1,2-mannosidic linkage located in a alpha1,3-branch of Man6GlcNAc2 oligosaccharide on enzyme activity of recombinant human Man9-mannosidase produced in Escherichia coli.
We produced the human kidney Man9-mannosidase in Escherichia coli and studied the effect of the alpha-1,2-mannosidic linkage located in the alpha branch of Manalpha1-6(Manalpha1-2Manalpha1-3)Manalpha1-6(Manalpha1-3)Manbeta1-4GlcNAcbeta1-4-GlcNAc, an N-linked oligosaccharide, on the enzyme activity. The alpha1,2-mannose residue influenced the rate of hydrolysis of and substrate preference for other alpha-1,2-mannosidic linkages.
Fujiyama
K
K
The International Center for Biotechnology, Osaka University, 2-1 Yamada-oka, Suita, Osaka 565-0871, Japan. fujiyama@icb.osaka-u.ac.jp
Sakuradani
S
S
Moran
D G
DG
Yoshida
T
T
Seki
T
T