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Gene Review

AMS1  -  Ams1p

Saccharomyces cerevisiae S288c

Synonyms: Alpha-D-mannoside mannohydrolase, Alpha-mannosidase, G1861, YGL156W
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Disease relevance of AMS1


High impact information on AMS1


Biological context of AMS1


Anatomical context of AMS1

  • The cytoplasm to vacuole (Cvt) trafficking pathway in S. cerevisiae is a constitutive biosynthetic pathway required for the transport of two vacuolar enzymes, aminopeptidase I (Ape1p) and alpha-mannosidase (Ams1p), to the vacuole [12].
  • Ape1p and Ams1p bind to their receptor, Atg19p, in the cytosol to form a Cvt complex, which then associates with a membrane structure that envelops the complex before fusing with the vacuolar membrane [12].
  • Yeast alpha-mannosidase, a marker enzyme of vacuolar membranes, was solubilized and purified from commercial bakers' yeast [13].
  • The C-terminal domain lacking the putative transmembrane region was shown to have alpha-mannosidase activity when expressed in COS cells as a secreted Protein A fusion product [14].
  • Radiolabel pulse-chase experiments indicated that all of the cell lines processed and targeted lysosomal alpha-mannosidase normally, indicating the lack of a significant role for Rab7 in the targeting pathway; however, retention of mature lysosomal hydrolases was affected in Rab7 WT and Rab7 T22N cell lines [15].

Associations of AMS1 with chemical compounds

  • The heterogeneity resided in four families of oligosaccharides: (i) Glc3Man9GlcNAc----Man8 GlcNAc trimming intermediates; (ii) alpha-mannosidase degradation products of the principal isomers; (iii) mannan elongation intermediates; (iv) core structures with the alpha 1,2-linked mannose usually removed by the processing alpha-mannosidase [16].
  • High resolution 1H NMR analysis of the Man8GlcNAc formed from Man9GlcNAc in the presence of the alpha-mannosidase of Fraction II showed only a single isomer with the following structure: (see formula; see text) This specific enzyme is most probably involved in processing of oligosaccharide during biosynthesis of mannoproteins [17].
  • Nevertheless, disruption of the alpha-mannosidase encoding gene almost totally prevented degradation of a misfolded glycoprotein [18].
  • It was clearly separated from alpha-glucosidase, which acts onp-nitrophenyl-alpha-D-glucopyranoside, but still contained beta-glucosidase and alpha-mannosidase acting on p-nitrophenyl-beta-D-glucopyranoside and alpha-D-mannopyranoside, respectively [19].
  • The specific alpha-mannosidase does not require the addition of divalent cation for activity, but it is inhibited by Tris, EDTA, Mn2+, Co2+, Zn2+, and Mg2+ [20].

Other interactions of AMS1


Analytical, diagnostic and therapeutic context of AMS1

  • The rates of H+ exchange with Ca2+, Cd2+, and K+ were similar in both strains, as were alpha-mannosidase and H+-ATPase activities, and SDS/PAGE patterns of vacuolar proteins [25].
  • After 4,300-fold purification by conventional chromatography, the alpha-mannosidase gave a single band on nondenaturing polyacrylamide gel electrophoresis, but could be fractionated into active isoforms, which consisted of 107-, 73-, and 31-kDa polypeptides, with a Mono Q anion exchange fast protein liquid chromatography system [13].
  • 2. After high-speed zonal centrifugation most of the protein, acid and alkaline phosphatases, alkaline pyrophosphatase, adenosine monophosphatase, beta-fructofuranosidase, alpha-mannosidase, NADPH-cytochrome c oxidoreductase and an appreciable amount of phospholipid and sterol were non-sedimentable, i.e. were at densities below 1.09 (g/cm3) [26].
  • Parts of the yeast recombinant EG IIIs decreased their molecular masses to 25 kDa after treatment with endoglycosidase H and alpha-mannosidase, suggesting that they are N glycosylated at least partly [27].
  • The mannose-labeled oligosaccharide released from oligosaccharide-lipid of MI8-5 cells was analyzed by HPLC and alpha-mannosidase treatment, and the data were consistent with a structure of Man9GlcNAc2 [28].


  1. Production in yeast of alpha-galactosidase A, a lysosomal enzyme applicable to enzyme replacement therapy for Fabry disease. Chiba, Y., Sakuraba, H., Kotani, M., Kase, R., Kobayashi, K., Takeuchi, M., Ogasawara, S., Maruyama, Y., Nakajima, T., Takaoka, Y., Jigami, Y. Glycobiology (2002) [Pubmed]
  2. Cyclo(dehydroala-L-Leu), an alpha-glucosidase inhibitor from Penicillium sp. F70614. Kwon, O.S., Park, S.H., Yun, B.S., Pyun, Y.R., Kim, C.J. J. Antibiot. (2000) [Pubmed]
  3. Isolation and partial characterization of yeast mannan hydrolysing enzymes from bacterial isolates. Malek, M.A., Berry, D.R. Microbios (1995) [Pubmed]
  4. Hitchhikers guide to the vacuole-mechanisms of cargo sequestration in the Cvt and autophagic pathways. Thumm, M. Mol. Cell (2002) [Pubmed]
  5. Isolation, characterization, and expression of cDNAs encoding murine alpha-mannosidase II, a Golgi enzyme that controls conversion of high mannose to complex N-glycans. Moremen, K.W., Robbins, P.W. J. Cell Biol. (1991) [Pubmed]
  6. Cloning and heterologous expression of glycosidase genes from Saccharomyces cerevisiae. Kuranda, M.J., Robbins, P.W. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
  7. Nucleotide sequence of AMS1, the structure gene of vacuolar alpha-mannosidase of Saccharomyces cerevisiae. Yoshihisa, T., Anraku, Y. Biochem. Biophys. Res. Commun. (1989) [Pubmed]
  8. Vacuolar localization of oligomeric alpha-mannosidase requires the cytoplasm to vacuole targeting and autophagy pathway components in Saccharomyces cerevisiae. Hutchins, M.U., Klionsky, D.J. J. Biol. Chem. (2001) [Pubmed]
  9. Glycoprotein biosynthesis in Saccharomyces cerevisiae. Isolation and characterization of the gene encoding a specific processing alpha-mannosidase. Camirand, A., Heysen, A., Grondin, B., Herscovics, A. J. Biol. Chem. (1991) [Pubmed]
  10. Topology of ER processing alpha-mannosidase of Saccharomyces cerevisiae. Grondin, B., Herscovics, A. Glycobiology (1992) [Pubmed]
  11. Production, purification and characterization of recombinant yeast processing alpha 1,2-mannosidase. Lipari, F., Herscovics, A. Glycobiology (1994) [Pubmed]
  12. Atg19p ubiquitination and the cytoplasm to vacuole trafficking pathway in yeast. Baxter, B.K., Abeliovich, H., Zhang, X., Stirling, A.G., Burlingame, A.L., Goldfarb, D.S. J. Biol. Chem. (2005) [Pubmed]
  13. Solubilization and purification of alpha-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae. Yoshihisa, T., Ohsumi, Y., Anraku, Y. J. Biol. Chem. (1988) [Pubmed]
  14. Isolation of a mouse Golgi mannosidase cDNA, a member of a gene family conserved from yeast to mammals. Herscovics, A., Schneikert, J., Athanassiadis, A., Moremen, K.W. J. Biol. Chem. (1994) [Pubmed]
  15. Evidence for a recycling role for Rab7 in regulating a late step in endocytosis and in retention of lysosomal enzymes in Dictyostelium discoideum. Buczynski, G., Bush, J., Zhang, L., Rodriguez-Paris, J., Cardelli, J. Mol. Biol. Cell (1997) [Pubmed]
  16. Structural heterogeneity in the Man8-13GlcNAc oligosaccharides from log-phase Saccharomyces yeast: a one- and two-dimensional 1H NMR spectroscopic study. Trimble, R.B., Atkinson, P.H. Glycobiology (1992) [Pubmed]
  17. Characterization of a specific alpha-mannosidase involved in oligosaccharide processing in Saccharomyces cerevisiae. Jelinek-Kelly, S., Akiyama, T., Saunier, B., Tkacz, J.S., Herscovics, A. J. Biol. Chem. (1985) [Pubmed]
  18. Characterization of Schizosaccharomyces pombe ER alpha-mannosidase: a reevaluation of the role of the enzyme on ER-associated degradation. Movsichoff, F., Castro, O.A., Parodi, A.J. Mol. Biol. Cell (2005) [Pubmed]
  19. Partial purification from Saccharomyces cerevisiae of a soluble glucosidase which removes the terminal glucose from the oligosaccharide Glc3Man9GlcNAc2. Kilker, R.D., Saunier, B., Tkacz, J.S., Herscovics, A. J. Biol. Chem. (1981) [Pubmed]
  20. Glycoprotein biosynthesis in Saccharomyces cerevisiae. Purification of the alpha-mannosidase which removes one specific mannose residue from Man9GlcNAc. Jelinek-Kelly, S., Herscovics, A. J. Biol. Chem. (1988) [Pubmed]
  21. Free-oligosaccharide control in the yeast Saccharomyces cerevisiae: roles for peptide:N-glycanase (Png1p) and vacuolar mannosidase (Ams1p). Chantret, I., Frénoy, J.P., Moore, S.E. Biochem. J. (2003) [Pubmed]
  22. Mechanism of cargo selection in the cytoplasm to vacuole targeting pathway. Shintani, T., Huang, W.P., Stromhaug, P.E., Klionsky, D.J. Dev. Cell (2002) [Pubmed]
  23. Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins. Nakatsukasa, K., Nishikawa , S., Hosokawa, N., Nagata, K., Endo, T. J. Biol. Chem. (2001) [Pubmed]
  24. Biochemical and genetic analysis of an alpha-mannosidase mutant from Saccharomyces cerevisiae. Cueva, R., Bordallo, C., Suárez Rendueles, P. FEMS Microbiol. Lett. (1990) [Pubmed]
  25. The yeast mutant vps5Delta affected in the recycling of Golgi membrane proteins displays an enhanced vacuolar Mg2+/H+ exchange activity. Borrelly, G., Boyer, J.C., Touraine, B., Szponarski, W., Rambier, M., Gibrat, R. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  26. Distribution of membranes, especially of plasma-membrane fragments, during zonal centrifugations of homogenates from glucose-repressed Saccharomyces Cerevisiae. Nurminen, T., Taskinen, L., Suomalainen, H. Biochem. J. (1976) [Pubmed]
  27. Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414. Okada, H., Tada, K., Sekiya, T., Yokoyama, K., Takahashi, A., Tohda, H., Kumagai, H., Morikawa, Y. Appl. Environ. Microbiol. (1998) [Pubmed]
  28. Nonglucosylated oligosaccharides are transferred to protein in MI8-5 Chinese hamster ovary cells. Quellhorst, G.J., O'Rear, J.L., Cacan, R., Verbert, A., Krag, S.S. Glycobiology (1999) [Pubmed]
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