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1
Revision of the oligosaccharide structures of yeast carboxypeptidase Y.酵母羧肽酶Y寡糖结构的修正
Proc Natl Acad Sci U S A. 1990 May;87(9):3368-72. doi: 10.1073/pnas.87.9.3368.
2
Localization of alpha 1----3-linked mannoses in the N-linked oligosaccharides of Saccharomyces cerevisiae mnn mutants.酿酒酵母mnn突变体N-连接寡糖中α1----3-连接甘露糖的定位
Biochemistry. 1990 Mar 13;29(10):2471-82. doi: 10.1021/bi00462a006.
3
Carbohydrate structure of Saccharomyces cerevisiae mnn9 mannoprotein.酿酒酵母mnn9甘露糖蛋白的碳水化合物结构
J Biol Chem. 1984 Mar 25;259(6):3805-11.
4
Structure of the phosphorylated N-linked oligosaccharides from the mnn9 and mnn10 mutants of Saccharomyces cerevisiae.酿酒酵母mnn9和mnn10突变体磷酸化N-连接寡糖的结构
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Structural heterogeneity in the Man8-13GlcNAc oligosaccharides from log-phase Saccharomyces yeast: a one- and two-dimensional 1H NMR spectroscopic study.对数期酿酒酵母中Man8-13GlcNAc寡糖的结构异质性：一维和二维¹H NMR光谱研究
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Early steps in processing of yeast glycoproteins.酵母糖蛋白加工的早期步骤。
J Biol Chem. 1984 Aug 25;259(16):10322-7.
7
Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast.Htm1p是一种甘露糖苷酶样蛋白，参与酵母中糖蛋白的降解。
EMBO Rep. 2001 May;2(5):423-30. doi: 10.1093/embo-reports/kve089.
8
Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae.酿酒酵母och1、och1 mnn1和och1 mnn1 alg3突变体中N-连接寡糖的结构，这些突变体显示α-1,6-多聚甘露糖外链完全缺失。
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Carbohydrate chains on yeast carboxypeptidase Y are phosphorylated.酵母羧肽酶Y上的碳水化合物链被磷酸化。
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10
Glycoprotein biosynthesis in the alg3 Saccharomyces cerevisiae mutant. II. Structure of novel Man6-10GlcNAc2 processing intermediates on secreted invertase.酿酒酵母alg3突变体中的糖蛋白生物合成。II. 分泌型转化酶上新型Man6-10GlcNAc2加工中间体的结构
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PLoS One. 2013 Dec 27;8(12):e84690. doi: 10.1371/journal.pone.0084690. eCollection 2013.
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Yeast Mnn9 is both a priming glycosyltransferase and an allosteric activator of mannan biosynthesis.酵母 Mnn9 既是一个启动糖基转移酶，也是甘露聚糖生物合成的别构激活剂。
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Free oligosaccharides to monitor glycoprotein endoplasmic reticulum-associated degradation in Saccharomyces cerevisiae.监测酿酒酵母糖蛋白内质网相关降解的游离寡糖。
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Filamentous fungi as production organisms for glycoproteins of bio-medical interest.丝状真菌作为具有生物医学意义的糖蛋白的生产生物体。
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Deletion of new covalently linked cell wall glycoproteins alters the electrophoretic mobility of phosphorylated wall components of Saccharomyces cerevisiae.新的共价连接细胞壁糖蛋白的缺失改变了酿酒酵母磷酸化细胞壁成分的电泳迁移率。
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A small protein (Ags1p) and the Pho80p-Pho85p kinase complex contribute to aminoglycoside antibiotic resistance of the yeast Saccharomyces cerevisiae.一种小蛋白（Ags1p）和Pho80p-Pho85p激酶复合物有助于酿酒酵母对氨基糖苷类抗生素产生抗性。
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本文引用的文献

1
Structural studies of phosphorylated high mannose-type oligosaccharides.磷酸化高甘露糖型寡糖的结构研究
J Biol Chem. 1980 Nov 25;255(22):10847-58.
2
Linkage and sequence analysis of mannose-rich glycoprotein core oligosaccharides by proton nuclear magnetic resonance spectroscopy.利用质子核磁共振波谱法对富含甘露糖的糖蛋白核心寡糖进行连锁和序列分析。
Biochemistry. 1980 Sep 2;19(18):4345-58. doi: 10.1021/bi00559a031.
3
Carbohydrate chains on yeast carboxypeptidase Y are phosphorylated.酵母羧肽酶Y上的碳水化合物链被磷酸化。
Proc Natl Acad Sci U S A. 1981 Apr;78(4):2244-8. doi: 10.1073/pnas.78.4.2244.
4
Early stages in the yeast secretory pathway are required for transport of carboxypeptidase Y to the vacuole.酵母分泌途径的早期阶段是羧肽酶Y转运至液泡所必需的。
Cell. 1982 Sep;30(2):439-48. doi: 10.1016/0092-8674(82)90241-0.
5
The vacuole as the lysosome of the yeast cell.作为酵母细胞溶酶体的液泡。
Arch Mikrobiol. 1967 Feb 20;56(2):148-55. doi: 10.1007/BF00408765.
6
Isolation and partial characterization of an acid carboxypeptidase from yeast.酵母酸性羧肽酶的分离及部分特性研究
Biochemistry. 1974 Sep 10;13(19):3871-7. doi: 10.1021/bi00716a008.
7
Polymorphism of the somatic antigen of yeast.酵母体细胞抗原的多态性
Science. 1974 Apr 12;184(4133):127-34. doi: 10.1126/science.184.4133.127.
8
Structure of yeast external invertase Man8-14GlcNAc processing intermediates by 500-megahertz 1H NMR spectroscopy.通过500兆赫1H核磁共振光谱法解析酵母外切转化酶Man8-14GlcNAc加工中间体的结构
J Biol Chem. 1986 Jul 25;261(21):9815-24.
9
Regulation of the protein glycosylation pathway in yeast: structural control of N-linked oligosaccharide elongation.酵母中蛋白质糖基化途径的调控：N-连接寡糖延伸的结构控制
Proc Natl Acad Sci U S A. 1987 Dec;84(24):8824-8. doi: 10.1073/pnas.84.24.8824.
10
Reconstitution of SEC gene product-dependent intercompartmental protein transport.SEC基因产物依赖性的隔室间蛋白质转运的重建。
Cell. 1988 Jul 29;54(3):335-44. doi: 10.1016/0092-8674(88)90196-1.

酵母羧肽酶Y寡糖结构的修正

Revision of the oligosaccharide structures of yeast carboxypeptidase Y.

作者信息

Ballou L, Hernandez L M, Alvarado E, Ballou C E

机构信息

Department of Biochemistry, University of California, Berkeley 94720.

出版信息

Proc Natl Acad Sci U S A. 1990 May;87(9):3368-72. doi: 10.1073/pnas.87.9.3368.

DOI:10.1073/pnas.87.9.3368
PMID:2185468
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC53901/
Abstract

The N-linked oligosaccharides from baker's yeast carboxypeptidase Y were analyzed by 1H NMR and specific mannosidase digestion and found to be identical to those from the Saccharomyces cerevisiae mnn9 mutant bulk mannoprotein. The results support the view that the mnn mutants make oligosaccharides that are a true reflection of the normal biosynthetic pathway and confirm that a recently revised yeast oligosaccharide structure is applicable to wild-type mannoproteins.

摘要

通过1H核磁共振和特定甘露糖苷酶消化对来自面包酵母羧肽酶Y的N-连接寡糖进行了分析，发现其与来自酿酒酵母mnn9突变体大量甘露糖蛋白的寡糖相同。这些结果支持了这样一种观点，即mnn突变体产生的寡糖是正常生物合成途径的真实反映，并证实了最近修订的酵母寡糖结构适用于野生型甘露糖蛋白。