N-glycosylation influences the latency and catalytic properties of mammalian purple acid phosphatase.
N-glycosylation influences the latency and catalytic properties of mammalian purple acid phosphatase.
复制标题
N-糖基化影响哺乳动物紫色酸性磷酸酶的潜伏期和催化特性。
DOI:
10.1016/j.abb.2004.11.029
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发表时间:
2005
影响因子:
3.9
通讯作者:
G. Andersson
中科院分区:
文献类型:
--
作者:
Yunling Wang;M. Norgård;G. Andersson
Purple acid phosphatase (PAP), also known as tartrate-resistant acid phosphatase or uteroferrin, contains two potential consensus N-glycosylation sites at Asn97and Asn128. In this study, endogenous rat bone PAP was found to possess similar N-glycan structures as rat recombinant PAP heterologously expressed in baculovirus-infected Sf9 insect cells. PAP from Sf9 cells was shown to contain two N-linked oligosaccharides, whereas PAP expressed by mammalian CHO-K1 cells was less extensively glycosylated. The extent of N-glycosylation affected the catalytic properties of the enzyme, as N97Q and N128Q mutants, containing a single oligosaccharide chain, exhibited a lower substrate affinity and catalytic activity compared to those of the fully glycosylated PAP in the native, monomeric state. The differences in substrate affinity and catalytic activity were abolished and partially restored, respectively, by proteolytic cleavage in the loop domain, indicating that the extent of N-glycosylation influences the interaction of the repressive loop domain with catalytically important residues.
DOI:
--
发表时间:
1985
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Saunders,PT;Renegar,RH;Raub,TJ;Baumbach,GA;Atkinson,PH;Bazer,FW;Roberts,RM
通讯作者:
Roberts,RM
影响因子:
2.9
作者:
J. Orlando;T. Zirino;B. Quirk;B. Averill
通讯作者:
J. Orlando;T. Zirino;B. Quirk;B. Averill
DOI:
10.1073/pnas.81.10.2985
发表时间:
1984
影响因子:
11.1
作者:
Baumbach,GA;Saunders,PT;Bazer,FW;Roberts,RM
通讯作者:
Roberts,RM