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首页> 外文期刊>FEBS Letters >A novel human UDP‐N‐acetyl‐D‐galactosamine:polypeptide N‐acetylgalactosaminyltransferase, GalNAc‐T7, with specificity for partial GalNAc‐glycosylated acceptor substrates
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A novel human UDP‐N‐acetyl‐D‐galactosamine:polypeptide N‐acetylgalactosaminyltransferase, GalNAc‐T7, with specificity for partial GalNAc‐glycosylated acceptor substrates

机译:一种新型人UDP-N-乙酰基-D-半乳糖胺:多肽N-乙酰半乳糖胺基转移酶GalNAc-T7,对部分GalNAc-糖基化受体底物具有特异性

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>A novel member of the human UDP-N-acetyl- class="smallCaps">D-galactosamine:polypeptide N-acetylgalactosaminyltransferase gene family, designated GalNAc-T7, was cloned and expressed. GalNAc-T7 exhibited different properties compared to other characterized members of this gene family, in showing apparent exclusive specificity for partially GalNAc-glycosylated acceptor substrates. GalNAc-T7 showed no activity with a large panel of non-glycosylated peptides, but was selectively activated by partial GalNAc glycosylation of peptide substrates derived from the tandem repeats of human MUC2 and rat submaxillary gland mucin. The function of GalNAc-T7 is suggested to be as a follow-up enzyme in the initiation step of O-glycosylation.
机译:>人类UDP- N -乙酰基- class =“ smallCaps”> D -半乳糖胺:多肽 N -乙酰半乳糖胺基转移酶基因的新成员克隆并表达了命名为GalNAc-T7的家族。与该基因家族的其他特征成员相比,GalNAc-T7具有不同的特性,对部分GalNAc-糖基化受体底物表现出明显的排他特异性。 GalNAc-T7对一大批未糖基化的肽均无活性,但被衍生自人MUC2和大鼠上颌下腺粘蛋白串联重复序列的肽底物的部分GalNAc糖基化选择性激活。 GalNAc-T7的功能被认为是 O -糖基化起始步骤中的后续酶。

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