Recognition Properties of Processing α‐Glucosidase I and α‐Glucosidase II
Recognition Properties of Processing α‐Glucosidase I and α‐Glucosidase II
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α-葡萄糖苷酶 I 和 α-葡萄糖苷酶 II 加工的识别特性
DOI:
10.1081/car-120030022
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发表时间:
2004
影响因子:
1
通讯作者:
A. Takatsuki
中科院分区:
文献类型:
--
作者:
W. Hakamata;M. Muroi;T. Nishio;T. Oku;A. Takatsuki
Abstract All four possible monodeoxy derivatives of p‐nitrophenyl α‐D‐glucopyranoside (PNP Glc) and 1‐amino‐2,6‐anhydro‐1‐deoxy‐D‐glycero‐D‐ido‐heptitol derivatives were prepared and used as substrates and inhibitors of rat liver processing α‐glucosidases. α‐Glucosidase II hydrolyzed the 2‐deoxy derivative of PNP Glc (1); the hydrolysis of 1 was more rapid than that of PNP Glc. These results indicate that the presence of a C‐2 hydroxyl group is not essential for the action of α‐glucosidase II. In contrast, PNP Glc and all of the deoxy derivatives of PNP Glc 1–4 inhibited α‐glucosidase I. These results indicate that α‐glucosidase I does not necessarily need all of the hydroxyl groups of the glycon moiety for binding to the enzyme. 2,6‐Anhydro‐1‐benzamide‐D‐glycero‐D‐ido‐heptitol (11), with a terminal phenyl group, inhibited α‐glucosidase I and α‐glucosidase II. Both α‐glucosidase I and II showed the same aglycon specificities. When probes 5–12 were assayed for their ability to inhibit processing by α‐glucosidases at the cellular level, no effects on glycoprotein processing were observed.
DOI:
10.1016/s0021-9258(18)33975-9
发表时间:
1982-09
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Douglas;Burns;O. Touster
通讯作者:
Douglas;Burns;O. Touster
DOI:
10.1042/bj2470555
发表时间:
1987
期刊:
The Biochemical journal
影响因子:
--
作者:
Shailubhai,K;Pratta,MA;Vijay,IK
通讯作者:
Vijay,IK