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Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1 -> 2)-mannosidase I

David Cantu, Wim Nerinckx (UGent) and Peter Reilly
(2008) CARBOHYDRATE RESEARCH. 343(13). p.2235-2242
Author
Organization
Abstract
It has been difficult to identify the proton donor and nucleophilic assistant/base of endoplasmic reticulum alpha-(1 -> 2)-mannosidase I, a member of glycoside hydrolase Family 47, which cleaves the glycosidic bond between two alpha-(1 -> 2)-linked mannosyl residues by the inverting mechanism, trimming Man(9)Glc-NAc2 to Man(8)GlcNAc(2) isomer B. Part of the difficulty is caused by the enzyme's use of a water molecule to transmit the proton that attacks the glycosidic oxygen atom. We earlier used automated docking to conclusively determine that Glu435 in the yeast enzyme (Glu599 in the corresponding human enzyme) is the nucleophilic assistant. The commonly accepted proton donor has been Glu330 in the human enzyme (Glu132 in the yeast enzyme). However, for theoretical reasons this conclusion is untenable. Theory, automated docking of alpha-D-S-3(1)-mannopyranosyl-(1 -> 2)-alpha-D-C-4(1)-mannopyranose and water molecules associated with candidate proton donors, and estimation of dissociation constants of the latter have shown that the true proton donor is Asp463 in the human enzyme (Asp275 in the yeast enzyme). (C) 2008 Elsevier Ltd. All rights reserved.
Keywords
MACROMOLECULES, SPECIFICITY, REVEALS, ALGORITHM, QUALITY-CONTROL, STRUCTURAL BASIS, TRANSITION-STATE, GLYCOSIDE HYDROLASES, SACCHAROMYCES-CEREVISIAE, CLASS-I ALPHA-1, 2-MANNOSIDASES

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MLA
Cantu, David, et al. “Theory and Computation Show That Asp463 Is the Catalytic Proton Donor in Human Endoplasmic Reticulum Alpha-(1 -> 2)-Mannosidase I.” CARBOHYDRATE RESEARCH, vol. 343, no. 13, ELSEVIER SCI LTD, 2008, pp. 2235–42, doi:10.1016/j.carres.2008.05.026.
APA
Cantu, D., Nerinckx, W., & Reilly, P. (2008). Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1 -> 2)-mannosidase I. CARBOHYDRATE RESEARCH, 343(13), 2235–2242. https://doi.org/10.1016/j.carres.2008.05.026
Chicago author-date
Cantu, David, Wim Nerinckx, and Peter Reilly. 2008. “Theory and Computation Show That Asp463 Is the Catalytic Proton Donor in Human Endoplasmic Reticulum Alpha-(1 -> 2)-Mannosidase I.” CARBOHYDRATE RESEARCH 343 (13): 2235–42. https://doi.org/10.1016/j.carres.2008.05.026.
Chicago author-date (all authors)
Cantu, David, Wim Nerinckx, and Peter Reilly. 2008. “Theory and Computation Show That Asp463 Is the Catalytic Proton Donor in Human Endoplasmic Reticulum Alpha-(1 -> 2)-Mannosidase I.” CARBOHYDRATE RESEARCH 343 (13): 2235–2242. doi:10.1016/j.carres.2008.05.026.
Vancouver
1.
Cantu D, Nerinckx W, Reilly P. Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1 -> 2)-mannosidase I. CARBOHYDRATE RESEARCH. 2008;343(13):2235–42.
IEEE
[1]
D. Cantu, W. Nerinckx, and P. Reilly, “Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1 -> 2)-mannosidase I,” CARBOHYDRATE RESEARCH, vol. 343, no. 13, pp. 2235–2242, 2008.
@article{685732,
  abstract     = {{It has been difficult to identify the proton donor and nucleophilic assistant/base of endoplasmic reticulum alpha-(1 -> 2)-mannosidase I, a member of glycoside hydrolase Family 47, which cleaves the glycosidic bond between two alpha-(1 -> 2)-linked mannosyl residues by the inverting mechanism, trimming Man(9)Glc-NAc2 to Man(8)GlcNAc(2) isomer B. Part of the difficulty is caused by the enzyme's use of a water molecule to transmit the proton that attacks the glycosidic oxygen atom. We earlier used automated docking to conclusively determine that Glu435 in the yeast enzyme (Glu599 in the corresponding human enzyme) is the nucleophilic assistant. The commonly accepted proton donor has been Glu330 in the human enzyme (Glu132 in the yeast enzyme). However, for theoretical reasons this conclusion is untenable. Theory, automated docking of alpha-D-S-3(1)-mannopyranosyl-(1 -> 2)-alpha-D-C-4(1)-mannopyranose and water molecules associated with candidate proton donors, and estimation of dissociation constants of the latter have shown that the true proton donor is Asp463 in the human enzyme (Asp275 in the yeast enzyme). (C) 2008 Elsevier Ltd. All rights reserved.}},
  author       = {{Cantu, David and Nerinckx, Wim and Reilly, Peter}},
  issn         = {{0008-6215}},
  journal      = {{CARBOHYDRATE RESEARCH}},
  keywords     = {{MACROMOLECULES,SPECIFICITY,REVEALS,ALGORITHM,QUALITY-CONTROL,STRUCTURAL BASIS,TRANSITION-STATE,GLYCOSIDE HYDROLASES,SACCHAROMYCES-CEREVISIAE,CLASS-I ALPHA-1,2-MANNOSIDASES}},
  language     = {{eng}},
  number       = {{13}},
  pages        = {{2235--2242}},
  publisher    = {{ELSEVIER SCI LTD}},
  title        = {{Theory and computation show that Asp463 is the catalytic proton donor in human endoplasmic reticulum alpha-(1 -> 2)-mannosidase I}},
  url          = {{http://doi.org/10.1016/j.carres.2008.05.026}},
  volume       = {{343}},
  year         = {{2008}},
}
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