SYNTHETIC REACTION OF CELLVIBRIO-GILVUS CELLOBIOSE PHOSPHORYLASE

被引:46
作者
KITAOKA, M [1 ]
SASAKI, T [1 ]
TANIGUCHI, H [1 ]
机构
[1] NATL FOOD RES INST,TSUKUBA,IBARAKI 305,JAPAN
关键词
D O I
10.1093/oxfordjournals.jbchem.a123862
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The synthetic reactions of the cellobiose phosphorylase from Cellvibrio gilvus were investigated in detail.It was found that, besides D-glucose, some sugars having substitution or deletion of the hydroxyl group at C2 or C6 of the D-glucose molecule could serve as a glucosyl acceptor, though less effectively than D-glucose. The enzyme showed higher activity with beta-D-glucose than with the alpha-anomer as an acceptor. This result indicates that it recognizes the anomeric hydroxyl group not involved directly in the reaction. beta-D-Cellobiose was also phosphorolyzed faster than the alpha-anomer. Substrate inhibition was observed with D-glucose, 6-deoxy-D-glucose, or D-glucosamine as an acceptor, with D-glucose being most inhibiting. This inhibition was studied in detail and it was found that D-glucose competes with alpha-D-glucose-1-phosphate for its binding site. A model of competitive substrate inhibition was proposed, and the experimental data fit well to the theoretical values that were calculated in accordance with this model.
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页码:40 / 44
页数:5
相关论文
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