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海洋细菌唾液酸转移酶。

Marine bacterial sialyltransferases.

机构信息

Glycotechnology Business Unit, Japan Tobacco Inc., 700 Higashibara, Iwata, Shizuoka 438-0802, Japan.

出版信息

Mar Drugs. 2010 Nov 5;8(11):2781-94. doi: 10.3390/md8112781.

DOI:10.3390/md8112781
PMID:21139844
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2996176/
Abstract

Sialyltransferases transfer N-acetylneuraminic acid (Neu5Ac) from the common donor substrate of these enzymes, cytidine 5'-monophospho-N-acetylneuraminic acid (CMP-Neu5Ac), to acceptor substrates. The enzymatic reaction products including sialyl-glycoproteins, sialyl-glycolipids and sialyl-oligosaccharides are important molecules in various biological and physiological processes, such as cell-cell recognition, cancer metastasis, and virus infection. Thus, sialyltransferases are thought to be important enzymes in the field of glycobiology. To date, many sialyltransferases and the genes encoding them have been obtained from various sources including mammalian, bacterial and viral sources. During the course of our research, we have detected over 20 bacteria that produce sialyltransferases. Many of the bacteria we isolated from marine environments are classified in the genus Photobacterium or the closely related genus Vibrio. The paper reviews the sialyltransferases obtained mainly from marine bacteria.

摘要

唾液酸转移酶将 N-乙酰神经氨酸(Neu5Ac)从这些酶的共同供体底物胞苷 5'-单磷酸 N-乙酰神经氨酸(CMP-Neu5Ac)转移到受体底物上。酶促反应产物包括唾液酸化糖蛋白、唾液酸化糖脂和唾液酸化寡糖,是各种生物和生理过程中的重要分子,如细胞-细胞识别、癌症转移和病毒感染。因此,唾液酸转移酶被认为是糖生物学领域的重要酶。迄今为止,已经从哺乳动物、细菌和病毒等各种来源获得了许多唾液酸转移酶及其编码基因。在我们的研究过程中,我们已经检测到超过 20 种产生唾液酸转移酶的细菌。我们从海洋环境中分离出的许多细菌属于发光杆菌属或密切相关的弧菌属。本文综述了主要从海洋细菌中获得的唾液酸转移酶。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/4856382eaba7/marinedrugs-08-02781f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/6c964c529ac7/marinedrugs-08-02781f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/79ff0d1695f0/marinedrugs-08-02781f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/a8af8ae0f684/marinedrugs-08-02781f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/7d774148ab16/marinedrugs-08-02781f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/ef4551ed43b4/marinedrugs-08-02781f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/4856382eaba7/marinedrugs-08-02781f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/6c964c529ac7/marinedrugs-08-02781f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/79ff0d1695f0/marinedrugs-08-02781f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/a8af8ae0f684/marinedrugs-08-02781f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/7d774148ab16/marinedrugs-08-02781f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/ef4551ed43b4/marinedrugs-08-02781f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0078/2996176/4856382eaba7/marinedrugs-08-02781f6.jpg

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本文引用的文献

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Microbes Environ. 2010;25(3):152-5. doi: 10.1264/jsme2.me10118.
2
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Carbohydr Res. 2010 Nov 22;345(17):2485-90. doi: 10.1016/j.carres.2010.09.022. Epub 2010 Sep 25.
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Enzymatic synthesis of unique sialyloligosaccharides using marine bacterial alpha-(2-->3)- and alpha-(2-->6)-sialyltransferases.
荧光假单胞菌来源的具有广泛底物特异性的α2,3-唾液酸转移酶:通过定向进化控制水解活性。
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Reconstruction of the sialylation pathway in the ancestor of eukaryotes.真核生物祖先中唾液酸化途径的重建。
Sci Rep. 2018 Feb 13;8(1):2946. doi: 10.1038/s41598-018-20920-1.
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A Photobacterium sp. α2-6-sialyltransferase (Psp2,6ST) mutant with an increased expression level and improved activities in sialylating Tn antigens.一种表达水平提高且在唾液酸化Tn抗原方面活性增强的嗜光菌属α2-6-唾液酸转移酶(Psp2,6ST)突变体。
Carbohydr Res. 2015 May 18;408:127-33. doi: 10.1016/j.carres.2014.12.007. Epub 2014 Dec 23.
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