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Conformational analysis of the mannosidase inhibitor kifunensine: a quantum mechanical and structural approach

STEM and males

Males A, Raich L, Rovira C, Williams SJ.
GSID: zuNzbGPtNwUJ
A Males, L Raich, SJ Williams, C Rovira… - …, 2017 - Wiley Online Library

… The major contemporary applications of kifunensine stem from its activity as a specific inhibitor of the class I GH47 α-mannosidases involved in glycoprotein biosynthesis within the …

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Males, A., Raich, L., Williams, S. J., Rovira, C., & Davies, G. J. (2017). Conformational analysis of the mannosidase inhibitor kifunensine: a quantum mechanical and structural approach. Chembiochem, 18(15), 1496-1501.
Males, Alexandra, et al. "Conformational analysis of the mannosidase inhibitor kifunensine: a quantum mechanical and structural approach." Chembiochem 18.15 (2017): 1496-1501.
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Screening for β-Mannosidases with Transmannosidation Capacity.

Bioscience, biotechnology, and biochemistry

Holazo A, Shinoyama H, Kamiyama Y, Yasui T.
PMID: 27286218
Biosci Biotechnol Biochem. 1992 Jan;56(5):822-4. doi: 10.1271/bbb.56.822.

No abstract available.

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Holazo A, Shinoyama H, Kamiyama Y, et al. Screening for β-Mannosidases with Transmannosidation Capacity. Biosci Biotechnol Biochem. 1992;56(5):822-4doi: 10.1271/bbb.56.822.
Holazo, A., Shinoyama, H., Kamiyama, Y., & Yasui, T. (1992). Screening for β-Mannosidases with Transmannosidation Capacity. Bioscience, biotechnology, and biochemistry, 56(5), 822-4. https://doi.org/10.1271/bbb.56.822
Holazo, A, et al. "Screening for β-Mannosidases with Transmannosidation Capacity." Bioscience, biotechnology, and biochemistry vol. 56,5 (1992): 822-4. doi: https://doi.org/10.1271/bbb.56.822
Holazo A, Shinoyama H, Kamiyama Y, Yasui T. Screening for β-Mannosidases with Transmannosidation Capacity. Biosci Biotechnol Biochem. 1992 Jan;56(5):822-4. doi: 10.1271/bbb.56.822. PMID: 27286218.
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Synthesis of 1,2- and 1,3-N-Linked Disaccharides of 5-Thio-alpha-D-mannopyranose as Potential Inhibitors of the Processing Mannosidase Class I and Mannosidase II Enzymes.

The Journal of organic chemistry

Johnston BD, Pinto BM.
PMID: 11672179
J Org Chem. 1998 Aug 21;63(17):5797-5800. doi: 10.1021/jo980168r.

The syntheses of S/N acetal heteroatom analogues of 1,2- and 1,3-linked mannopyranose disaccharides are described. The compounds are analogues of the Man-alpha-(1-->2)-Man and Man-alpha-(1-->3)-Man disaccharide components of oligosaccharides found in N-glycoproteins that are cleaved by trimming mannosidases during glycoprotein...

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Johnston BD, Pinto BM. Synthesis of 1,2- and 1,3-N-Linked Disaccharides of 5-Thio-alpha-D-mannopyranose as Potential Inhibitors of the Processing Mannosidase Class I and Mannosidase II Enzymes. J Org Chem. 1998;63(17):5797-5800doi: 10.1021/jo980168r.
Johnston, B. D., & Pinto, B. M. (1998). Synthesis of 1,2- and 1,3-N-Linked Disaccharides of 5-Thio-alpha-D-mannopyranose as Potential Inhibitors of the Processing Mannosidase Class I and Mannosidase II Enzymes. The Journal of organic chemistry, 63(17), 5797-5800. https://doi.org/10.1021/jo980168r
Johnston, Blair D., and Pinto, B. Mario. "Synthesis of 1,2- and 1,3-N-Linked Disaccharides of 5-Thio-alpha-D-mannopyranose as Potential Inhibitors of the Processing Mannosidase Class I and Mannosidase II Enzymes." The Journal of organic chemistry vol. 63,17 (1998): 5797-5800. doi: https://doi.org/10.1021/jo980168r
Johnston BD, Pinto BM. Synthesis of 1,2- and 1,3-N-Linked Disaccharides of 5-Thio-alpha-D-mannopyranose as Potential Inhibitors of the Processing Mannosidase Class I and Mannosidase II Enzymes. J Org Chem. 1998 Aug 21;63(17):5797-5800. doi: 10.1021/jo980168r. PMID: 11672179.
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Gene analysis and enzymatic properties of thermostable beta-glycosidase from Pyrococcus kodakaraensis KOD1.

Journal of bioscience and bioengineering

Ezaki S, Miyaoku K, Nishi K, Tanaka T, Fujiwara S, Takagi M, Atomi H, Imanaka T.
PMID: 16232586
J Biosci Bioeng. 1999;88(2):130-5. doi: 10.1016/s1389-1723(99)80190-x.

A beta-glycosidase with broad substrate specificity was identified from a hyperthermophilic archaeon, Pyrococcus kodakaraensis KOD1. The gene encoding beta-glycosidase (Pk-gly) consists of 1449 nucleotides corresponding to a polypeptide of 483 amino acids. The protein showed similarity with other beta-glycosidases...

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Ezaki S, Miyaoku K, Nishi K, et al. Gene analysis and enzymatic properties of thermostable beta-glycosidase from Pyrococcus kodakaraensis KOD1. J Biosci Bioeng. 1999;88(2):130-5doi: 10.1016/s1389-1723(99)80190-x.
Ezaki, S., Miyaoku, K., Nishi, K., Tanaka, T., Fujiwara, S., Takagi, M., Atomi, H., & Imanaka, T. (1999). Gene analysis and enzymatic properties of thermostable beta-glycosidase from Pyrococcus kodakaraensis KOD1. Journal of bioscience and bioengineering, 88(2), 130-5. https://doi.org/10.1016/s1389-1723(99)80190-x
Ezaki, S, et al. "Gene analysis and enzymatic properties of thermostable beta-glycosidase from Pyrococcus kodakaraensis KOD1." Journal of bioscience and bioengineering vol. 88,2 (1999): 130-5. doi: https://doi.org/10.1016/s1389-1723(99)80190-x
Ezaki S, Miyaoku K, Nishi K, Tanaka T, Fujiwara S, Takagi M, Atomi H, Imanaka T. Gene analysis and enzymatic properties of thermostable beta-glycosidase from Pyrococcus kodakaraensis KOD1. J Biosci Bioeng. 1999;88(2):130-5. doi: 10.1016/s1389-1723(99)80190-x. PMID: 16232586.
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One-pot synthesis of cyclic nitrones and their conversion to pyrrolizidines: 7a-epi-crotanecine inhibits alpha-mannosidases.

The Journal of organic chemistry

Cicchi S, Marradi M, Vogel P, Goti A.
PMID: 16468814
J Org Chem. 2006 Feb 17;71(4):1614-9. doi: 10.1021/jo0523518.

[reaction: see text] A new straightforward and inexpensive one-pot procedure is described for the preparation of enantiopure five-membered cyclic nitrones starting from the corresponding lactols. Its efficiency relies on the condensation of unprotected hydroxylamine with readily available lactols and...

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Cicchi S, Marradi M, Vogel P, et al. One-pot synthesis of cyclic nitrones and their conversion to pyrrolizidines: 7a-epi-crotanecine inhibits alpha-mannosidases. J Org Chem. 2006;71(4):1614-9doi: 10.1021/jo0523518.
Cicchi, S., Marradi, M., Vogel, P., & Goti, A. (2006). One-pot synthesis of cyclic nitrones and their conversion to pyrrolizidines: 7a-epi-crotanecine inhibits alpha-mannosidases. The Journal of organic chemistry, 71(4), 1614-9. https://doi.org/10.1021/jo0523518
Cicchi, S, et al. "One-pot synthesis of cyclic nitrones and their conversion to pyrrolizidines: 7a-epi-crotanecine inhibits alpha-mannosidases." The Journal of organic chemistry vol. 71,4 (2006): 1614-9. doi: https://doi.org/10.1021/jo0523518
Cicchi S, Marradi M, Vogel P, Goti A. One-pot synthesis of cyclic nitrones and their conversion to pyrrolizidines: 7a-epi-crotanecine inhibits alpha-mannosidases. J Org Chem. 2006 Feb 17;71(4):1614-9. doi: 10.1021/jo0523518. PMID: 16468814.
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Possible role of α-mannosidase and β-galactosidase in larynx cancer.

Contemporary oncology (Poznan, Poland)

Olszewska E, Borzym-Kluczyk M, Rzewnicki I, Wojtowicz J, Rogowski M, Pietruski JK, Czajkowska A, Sieskiewicz A.
PMID: 23788869
Contemp Oncol (Pozn). 2012;16(2):154-8. doi: 10.5114/wo.2012.28795. Epub 2012 May 29.

BACKGROUND: Lysosomal exoglycosidases, such as α-mannosidases (MAN) and β-galactosidases (GAL), are found in different glycoside hydrolase sequence-based families. Considerable research has proved plays the role of MAN, which play a key role in the modification and diversification of hybrid...

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Olszewska E, Borzym-Kluczyk M, Rzewnicki I, et al. Possible role of α-mannosidase and β-galactosidase in larynx cancer. Contemp Oncol (Pozn). 2012;16(2):154-8doi: 10.5114/wo.2012.28795.
Olszewska, E., Borzym-Kluczyk, M., Rzewnicki, I., Wojtowicz, J., Rogowski, M., Pietruski, J. K., Czajkowska, A., & Sieskiewicz, A. (2012). Possible role of α-mannosidase and β-galactosidase in larynx cancer. Contemporary oncology (Poznan, Poland), 16(2), 154-8. https://doi.org/10.5114/wo.2012.28795
Olszewska, Ewa, et al. "Possible role of α-mannosidase and β-galactosidase in larynx cancer." Contemporary oncology (Poznan, Poland) vol. 16,2 (2012): 154-8. doi: https://doi.org/10.5114/wo.2012.28795
Olszewska E, Borzym-Kluczyk M, Rzewnicki I, Wojtowicz J, Rogowski M, Pietruski JK, Czajkowska A, Sieskiewicz A. Possible role of α-mannosidase and β-galactosidase in larynx cancer. Contemp Oncol (Pozn). 2012;16(2):154-8. doi: 10.5114/wo.2012.28795. Epub 2012 May 29. PMID: 23788869; PMCID: PMC3687398.
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Synthesis of 1,4-imino-L-lyxitols modified at C-5 and their evaluation as inhibitors of GH38 α-mannosidases.

Beilstein journal of organic chemistry

Bella M, Šesták S, Moncoľ J, Koóš M, Poláková M.
PMID: 30202468
Beilstein J Org Chem. 2018 Aug 17;14:2156-2162. doi: 10.3762/bjoc.14.189. eCollection 2018.

A synthetic approach to 1,4-imino-L-lyxitols with various modifications at the C-5 position is reported. These imino-L-lyxitol cores were used for the preparation of a series of

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Bella M, Šesták S, Moncoľ J, et al. Synthesis of 1,4-imino-L-lyxitols modified at C-5 and their evaluation as inhibitors of GH38 α-mannosidases. Beilstein J Org Chem. 2018;14:2156-2162doi: 10.3762/bjoc.14.189.
Bella, M., Šesták, S., Moncoľ, J., Koóš, M., & Poláková, M. (2018). Synthesis of 1,4-imino-L-lyxitols modified at C-5 and their evaluation as inhibitors of GH38 α-mannosidases. Beilstein journal of organic chemistry, 142156-2162. https://doi.org/10.3762/bjoc.14.189
Bella, Maroš, et al. "Synthesis of 1,4-imino-L-lyxitols modified at C-5 and their evaluation as inhibitors of GH38 α-mannosidases." Beilstein journal of organic chemistry vol. 14 (2018): 2156-2162. doi: https://doi.org/10.3762/bjoc.14.189
Bella M, Šesták S, Moncoľ J, Koóš M, Poláková M. Synthesis of 1,4-imino-L-lyxitols modified at C-5 and their evaluation as inhibitors of GH38 α-mannosidases. Beilstein J Org Chem. 2018 Aug 17;14:2156-2162. doi: 10.3762/bjoc.14.189. eCollection 2018. PMID: 30202468; PMCID: PMC6122390.
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Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates.

Communications biology

Shenkman M, Ron E, Yehuda R, Benyair R, Khalaila I, Lederkremer GZ.
PMID: 30374462
Commun Biol. 2018 Oct 18;1:172. doi: 10.1038/s42003-018-0174-8. eCollection 2018.

Extensive mannose trimming of nascent glycoprotein N-glycans signals their targeting to endoplasmic reticulum-associated degradation (ERAD). ER mannosidase I (ERManI) and the EDEM protein family participate in this process. However, whether the EDEMs are truly mannosidases can be addressed only...

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Shenkman M, Ron E, Yehuda R, et al. Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Commun Biol. 2018;1:172doi: 10.1038/s42003-018-0174-8.
Shenkman, M., Ron, E., Yehuda, R., Benyair, R., Khalaila, I., & Lederkremer, G. Z. (2018). Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Communications biology, 1172. https://doi.org/10.1038/s42003-018-0174-8
Shenkman, Marina, et al. "Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates." Communications biology vol. 1 (2018): 172. doi: https://doi.org/10.1038/s42003-018-0174-8
Shenkman M, Ron E, Yehuda R, Benyair R, Khalaila I, Lederkremer GZ. Mannosidase activity of EDEM1 and EDEM2 depends on an unfolded state of their glycoprotein substrates. Commun Biol. 2018 Oct 18;1:172. doi: 10.1038/s42003-018-0174-8. eCollection 2018. PMID: 30374462; PMCID: PMC6194124.
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Synthetic trisaccharides reveal discrimination of .

Organic & biomolecular chemistry

Nitta K, Kuribara T, Totani K.
PMID: 33876795
Org Biomol Chem. 2021 May 12;19(18):4137-4145. doi: 10.1039/d1ob00428j.

A tri-antennary Man9GlcNAc2 glycan on the surface of endoplasmic reticulum (ER) glycoproteins functions as a glycoprotein secretion or degradation signal after regioselective cleavage of the terminal α-1,2-mannose residue of each branch. Four α-1,2-mannosidases-ER mannosidase I, ER degradation-enhancing α-mannosidase-like protein...

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Nitta K, Kuribara T, Totani K. Synthetic trisaccharides reveal discrimination of . Org Biomol Chem. 2021;19(18):4137-4145doi: 10.1039/d1ob00428j.
Nitta, K., Kuribara, T., & Totani, K. (2021). Synthetic trisaccharides reveal discrimination of . Organic & biomolecular chemistry, 19(18), 4137-4145. https://doi.org/10.1039/d1ob00428j
Nitta, Kyohei, et al. "Synthetic trisaccharides reveal discrimination of ." Organic & biomolecular chemistry vol. 19,18 (2021): 4137-4145. doi: https://doi.org/10.1039/d1ob00428j
Nitta K, Kuribara T, Totani K. Synthetic trisaccharides reveal discrimination of . Org Biomol Chem. 2021 May 12;19(18):4137-4145. doi: 10.1039/d1ob00428j. PMID: 33876795.
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Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?.

Carbohydrate research

Lee ZY, Loo JSE, Wibowo A, Mohammat MF, Foo JB.
PMID: 34280804
Carbohydr Res. 2021 Oct;508:108395. doi: 10.1016/j.carres.2021.108395. Epub 2021 Jul 05.

Dysregulation of glycosylation pathways has been well documented in several types of cancer, where it often participates in cancer development and progression, especially cancer metastasis. Hence, inhibition of glycosidases such as mannosidases can disrupt the biosynthesis of glycans on...

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Lee ZY, Loo JSE, Wibowo A, et al. Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?. Carbohydr Res. 2021;508:108395doi: 10.1016/j.carres.2021.108395.
Lee, Z. Y., Loo, J. S. E., Wibowo, A., Mohammat, M. F., & Foo, J. B. (2021). Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?. Carbohydrate research, 508108395. https://doi.org/10.1016/j.carres.2021.108395
Lee, Zheng Yang, et al. "Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?." Carbohydrate research vol. 508 (2021): 108395. doi: https://doi.org/10.1016/j.carres.2021.108395
Lee ZY, Loo JSE, Wibowo A, Mohammat MF, Foo JB. Targeting cancer via Golgi α-mannosidase II inhibition: How far have we come in developing effective inhibitors?. Carbohydr Res. 2021 Oct;508:108395. doi: 10.1016/j.carres.2021.108395. Epub 2021 Jul 05. PMID: 34280804.
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Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins.

The Plant cell

Hüttner S, Veit C, Vavra U, Schoberer J, Liebminger E, Maresch D, Grass J, Altmann F, Mach L, Strasser R, Dutt R, Hillaire G, Larke L, Rosé C.
PMID: 24737672
Plant Cell. 2014 Apr;26(4):1712-1728. doi: 10.1105/tpc.114.123216. Epub 2014 Apr 15.

To ensure that aberrantly folded proteins are cleared from the endoplasmic reticulum (ER), all eukaryotic cells possess a mechanism known as endoplasmic reticulum-associated degradation (ERAD). Many secretory proteins are N-glycosylated, and despite some recent progress, little is known about...

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Hüttner S, Veit C, Vavra U, et al. Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins. Plant Cell. 2014;26(4):1712-1728doi: 10.1105/tpc.114.123216.
Hüttner, S., Veit, C., Vavra, U., Schoberer, J., Liebminger, E., Maresch, D., Grass, J., Altmann, F., Mach, L., Strasser, R., Dutt, R., Hillaire, G., Larke, L., & Rosé, C. (2014). Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins. The Plant cell, 26(4), 1712-1728. https://doi.org/10.1105/tpc.114.123216
Hüttner, Silvia, et al. "Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins." The Plant cell vol. 26,4 (2014): 1712-1728. doi: https://doi.org/10.1105/tpc.114.123216
Hüttner S, Veit C, Vavra U, Schoberer J, Liebminger E, Maresch D, Grass J, Altmann F, Mach L, Strasser R, Dutt R, Hillaire G, Larke L, Rosé C. Arabidopsis Class I α-Mannosidases MNS4 and MNS5 Are Involved in Endoplasmic Reticulum-Associated Degradation of Misfolded Glycoproteins. Plant Cell. 2014 Apr;26(4):1712-1728. doi: 10.1105/tpc.114.123216. Epub 2014 Apr 15. PMID: 24737672; PMCID: PMC4036581.
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Up-regulation of golgi α-mannosidase IA and down-regulation of golgi α-mannosidase IC activates unfolded protein response during hepatocarcinogenesis.

Hepatology communications

Tu HC, Hsiao YC, Yang WY, Tsai SL, Lin HK, Liao CY, Lu JW, Chou YT, Wang HD, Yuh CH.
PMID: 29404456
Hepatol Commun. 2017 Apr 19;1(3):230-247. doi: 10.1002/hep4.1032. eCollection 2017 May.

α-1,2 mannosidases, key enzymes in N-glycosylation, are required for the formation of mature glycoproteins in eukaryotes. Aberrant regulation of α-1,2 mannosidases can result in cancer, although the underlying mechanisms are unclear. Here, we report the distinct roles of α-1,2...

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Tu HC, Hsiao YC, Yang WY, et al. Up-regulation of golgi α-mannosidase IA and down-regulation of golgi α-mannosidase IC activates unfolded protein response during hepatocarcinogenesis. Hepatol Commun. 2017;1(3):230-247doi: 10.1002/hep4.1032.
Tu, H. C., Hsiao, Y. C., Yang, W. Y., Tsai, S. L., Lin, H. K., Liao, C. Y., Lu, J. W., Chou, Y. T., Wang, H. D., & Yuh, C. H. (2017). Up-regulation of golgi α-mannosidase IA and down-regulation of golgi α-mannosidase IC activates unfolded protein response during hepatocarcinogenesis. Hepatology communications, 1(3), 230-247. https://doi.org/10.1002/hep4.1032
Tu, Hsiao-Chen, et al. "Up-regulation of golgi α-mannosidase IA and down-regulation of golgi α-mannosidase IC activates unfolded protein response during hepatocarcinogenesis." Hepatology communications vol. 1,3 (2017): 230-247. doi: https://doi.org/10.1002/hep4.1032
Tu HC, Hsiao YC, Yang WY, Tsai SL, Lin HK, Liao CY, Lu JW, Chou YT, Wang HD, Yuh CH. Up-regulation of golgi α-mannosidase IA and down-regulation of golgi α-mannosidase IC activates unfolded protein response during hepatocarcinogenesis. Hepatol Commun. 2017 Apr 19;1(3):230-247. doi: 10.1002/hep4.1032. eCollection 2017 May. PMID: 29404456; PMCID: PMC5721452.
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Showing 1 to 12 of 18 entries