Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile
Identification of a novel human UDP-GalNAc transferase with unique catalytic activity and expression profile
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鉴定具有独特催化活性和表达谱的新型人 UDP-GalNAc 转移酶
DOI：
10.1016/j.bbrc.2010.10.084
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发表时间：
2010-11-26
影响因子：
3.1
通讯作者：
Zhang, Yan
中科院分区：
文献类型：
--
作者：
Peng, Can;Togayachi, Akira;Zhang, Yan
鉴定并表征了人ppGalNAc-T家族的新成员ppGalNAc-T20。氨基酸比对显示ppGalNAc-T20和-T10之间的高度序列同一性。在针对粘蛋白衍生的肽底物的GalNAc转移测定中，重组ppGalNAc-T20被证明是典型的糖肽GaINAc-转移酶，其表现出针对单-GalNAc-T10的活性。糖基化肽EA 2来源于大鼠下颌下腺，但对未修饰的EA 2没有活性将ppGalNAc-T20的体外催化性质与ppGalNAc-T10进行比较，以显示不同的受体底物特异性和动力学常数。T20转录本仅在睾丸和脑中发现原位杂交进一步揭示ppGalNAc-T20特异性地定位于两个减数分裂时期的初级和次级精母细胞，表明其可能参与小鼠精子发生过程中的O-糖基化（C）2010 Elsevier Inc版权所有
A novel member of the human ppGalNAc-T family ppGalNAc-T20 was identified and characterized Amino acid alignment revealed a high sequence identity between ppGalNAc-T20 and -T10 In the GalNAc transfer assay towards mucin-derived peptide substrates the recombinant ppGalNAc-T20 demonstrated to be a typical glycopeptide GaINAc-transferase that exhibits activity towards mono-GalNAc-glycosylated peptide EA2 derived from rat submandibular gland mum but no activity towards non-modified EA2 The in vitro catalytic property of ppGalNAc-T20 was compared with that of ppGalNAc-T10 to show different acceptor substrate specificities and kinetic constants The ppGalNAc-T20 transcript was found exclusively in testis and brain In situ hybridization further reveals that ppGalNAc-T20 was specifically localized in primary and secondary spermatocytes of the two meiotic periods suggesting that it may involve in O-glycosylation during mouse spermatogenesis (C) 2010 Elsevier Inc All rights reserved