The Experts below are selected from a list of 15 Experts worldwide ranked by ideXlab platform
Peter J. Reilly - One of the best experts on this subject based on the ideXlab platform.
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The fate of β-d-mannopyranose after its formation by endoplasmic reticulum α-(1→2)-mannosidase I catalysis
Carbohydrate research, 2006Co-Authors: Chandrika Mulakala, Wim Nerinckx, Peter J. ReillyAbstract:Abstract The automated docking program AutoDock was used to dock all 38 characteristic β- d -mannopyranose ring conformers into the active site of the yeast endoplasmic reticulum α-(1→2)-mannosidase I, a Family 47 glycoside hydrolase that converts Man9GlcNAc2 to Man8GlcNAc2. The subject of this work is to establish the conformational pathway that allows the cleaved glycon product to leave the enzyme active site and eventually reach the ground-state conformation. Twelve of the 38 conformers optimally dock in the active site where the inhibitors 1-Deoxymannonojirimycin and kifunensine are found in enzyme crystal structures. A further 23 optimally dock in a second site on the side of the active-site well, while three dock outside the active-site cavity. It appears, through analysis of the internal energies of different ring conformations, of intermolecular energies between the ligands and enzyme, and of forces exerted on the ligands by the enzyme, that β- d -mannopyranose follows the path 3E→1C4→1H2→B2,5 before being expelled by the enzyme. The highly conserved second site that strongly binds β- d -mannopyranose-4C1 may exist to prevent competitive inhibition by the product, and is worthy of further investigation.
Chandrika Mulakala - One of the best experts on this subject based on the ideXlab platform.
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The fate of β-d-mannopyranose after its formation by endoplasmic reticulum α-(1→2)-mannosidase I catalysis
Carbohydrate research, 2006Co-Authors: Chandrika Mulakala, Wim Nerinckx, Peter J. ReillyAbstract:Abstract The automated docking program AutoDock was used to dock all 38 characteristic β- d -mannopyranose ring conformers into the active site of the yeast endoplasmic reticulum α-(1→2)-mannosidase I, a Family 47 glycoside hydrolase that converts Man9GlcNAc2 to Man8GlcNAc2. The subject of this work is to establish the conformational pathway that allows the cleaved glycon product to leave the enzyme active site and eventually reach the ground-state conformation. Twelve of the 38 conformers optimally dock in the active site where the inhibitors 1-Deoxymannonojirimycin and kifunensine are found in enzyme crystal structures. A further 23 optimally dock in a second site on the side of the active-site well, while three dock outside the active-site cavity. It appears, through analysis of the internal energies of different ring conformations, of intermolecular energies between the ligands and enzyme, and of forces exerted on the ligands by the enzyme, that β- d -mannopyranose follows the path 3E→1C4→1H2→B2,5 before being expelled by the enzyme. The highly conserved second site that strongly binds β- d -mannopyranose-4C1 may exist to prevent competitive inhibition by the product, and is worthy of further investigation.
Wim Nerinckx - One of the best experts on this subject based on the ideXlab platform.
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The fate of β-d-mannopyranose after its formation by endoplasmic reticulum α-(1→2)-mannosidase I catalysis
Carbohydrate research, 2006Co-Authors: Chandrika Mulakala, Wim Nerinckx, Peter J. ReillyAbstract:Abstract The automated docking program AutoDock was used to dock all 38 characteristic β- d -mannopyranose ring conformers into the active site of the yeast endoplasmic reticulum α-(1→2)-mannosidase I, a Family 47 glycoside hydrolase that converts Man9GlcNAc2 to Man8GlcNAc2. The subject of this work is to establish the conformational pathway that allows the cleaved glycon product to leave the enzyme active site and eventually reach the ground-state conformation. Twelve of the 38 conformers optimally dock in the active site where the inhibitors 1-Deoxymannonojirimycin and kifunensine are found in enzyme crystal structures. A further 23 optimally dock in a second site on the side of the active-site well, while three dock outside the active-site cavity. It appears, through analysis of the internal energies of different ring conformations, of intermolecular energies between the ligands and enzyme, and of forces exerted on the ligands by the enzyme, that β- d -mannopyranose follows the path 3E→1C4→1H2→B2,5 before being expelled by the enzyme. The highly conserved second site that strongly binds β- d -mannopyranose-4C1 may exist to prevent competitive inhibition by the product, and is worthy of further investigation.
Reilly Peter - One of the best experts on this subject based on the ideXlab platform.
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The fate of beta-D-mannopyranose after its formation by endoplasmic reticulum alpha-(1 -> 2)-mannosidase I catalysis
'Elsevier BV', 2007Co-Authors: Mulakala Chandrika, Nerinckx Wim, Reilly PeterAbstract:The automated docking program AutoDock was used to dock all 38 characteristic P-D-mannopyranose ring conformers into the active site of the yeast endoplasmic reticulum alpha-(1 2)-mannosidase 1, a Family 47 glycoside hydrolase that converts lMan(9)GlcNAc(2) to Man8GlcNAc(2). The subject of this work is to establish the conformational pathway that allows the cleaved glycon product to leave the enzyme active site and eventually reach the ground-state conformation. Twelve of the 38 conformers optimally dock in the active site where the inhibitors 1-Deoxymannonojirimycin and kifunensine are found in enzyme crystal structures. A further 23 optimally dock in a second site on the side of the active-site well, while three dock outside the active-site cavity. It appears, through analysis of the internal energies of different ring conformations, of intermolecular energies between the ligands and enzyme, and of forces exerted on the ligands by the enzyme, that beta-D-mannopyranose follows the path E-3 -> C-1(4) ->(H2 -> B2,5)-H-1 before being expelled by the enzyme. The highly conserved second site that strongly binds beta-D-mannopyranose-C-4(1) may exist to prevent competitive inhibition by the product, and is worthy of further investigation
Antonio C. B. Burtoloso - One of the best experts on this subject based on the ideXlab platform.
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Six-Step Syntheses of (−)-1-Deoxyaltronojirimycin and (+)-1-Deoxymannonojirimycin from N‑Z‑O‑TBDPS‑l‑serinal
2016Co-Authors: Meire Y. Kawamura, Alexánder G. Talero, João Victor Santiago, Edson Garambel-vilca, Isac G. Rosset, Antonio C. B. BurtolosoAbstract:Highly stereoselective six-step syntheses of (−)-1-deoxyaltronojirimycin (altro-DNJ) and (+)-1-deoxymannojirimycin (manno-DNJ) from N-Cbz-O-TBDPS-l-serinal are described. Key transformations involve a two-step preparation of a functionalized dihydropyridin-3-one as a common intermediate followed by Luche reduction and dihydroxylation (for altro-DNJ). The same sequence employing an epoxidation/epoxide opening in place of dihydroxylation furnishes manno-DNJ
