Computational analyses of the conformational itinerary along the reaction pathway of GH94 cellobiose phosphorylase. Fushinobu, S., Mertz, B., Hill, A., Hidaka, M., Kitaoka, M., & Reilly, P. Carbohydrate Research, 2008. abstract bibtex GH94 cellobiose phosphorylase (CBP) catalyzes the phosphorolysis of cellobiose into α-d-glucose 1-phosphate (G1P) and d-glucose with inversion of anomeric configuration. The complex crystal structure of CBP from Cel lvibrio gilvus had previously been determined; glycerol, glucose, and phosphate are bound to subsites -1, +1, and the anion binding site, respectively. We performed computational analyses to elucidate the conformational itinerary along the reaction pathway of this enzyme. autodock was used to dock cellobiose with its glycon glucosyl residue in various conformations and with its aglycon glucosyl residue in the low-energy 4 C 1 conformer. An oxocarbenium ion-like glucose molecule mimicking the transition state was also docked. Based on the clustering analysis, docked energies, and comparison with the crystallographic ligands, we conclude that the reaction proceeds from 1 S 3 as the pre-transition state conformer (Michaelis complex) via E 3 as the transition state candidate to 4 C 1 as the G1P product conformer. The predicted reaction pathway of the inverting phosphorylase is similar to that proposed for the first-half glycosylation reaction of retaining cellulases, but is different from those for inverting cellulases. NAMD was used to simulate molecular dynamics of the enzyme. The 1 S 3 pre-transition state conformer is highly stable compared with other conformers, and a conformational change from 4 C 1 to 1,4 B was observed. © 2008 Elsevier Ltd. All rights reserved.
@article{
title = {Computational analyses of the conformational itinerary along the reaction pathway of GH94 cellobiose phosphorylase},
type = {article},
year = {2008},
identifiers = {[object Object]},
keywords = {Cellobiose phosphorylase,Docking,Molecular dynamics,Phosphorolysis,Substrate conformation,Transition state},
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abstract = {GH94 cellobiose phosphorylase (CBP) catalyzes the phosphorolysis of cellobiose into α-d-glucose 1-phosphate (G1P) and d-glucose with inversion of anomeric configuration. The complex crystal structure of CBP from Cel lvibrio gilvus had previously been determined; glycerol, glucose, and phosphate are bound to subsites -1, +1, and the anion binding site, respectively. We performed computational analyses to elucidate the conformational itinerary along the reaction pathway of this enzyme. autodock was used to dock cellobiose with its glycon glucosyl residue in various conformations and with its aglycon glucosyl residue in the low-energy 4 C 1 conformer. An oxocarbenium ion-like glucose molecule mimicking the transition state was also docked. Based on the clustering analysis, docked energies, and comparison with the crystallographic ligands, we conclude that the reaction proceeds from 1 S 3 as the pre-transition state conformer (Michaelis complex) via E 3 as the transition state candidate to 4 C 1 as the G1P product conformer. The predicted reaction pathway of the inverting phosphorylase is similar to that proposed for the first-half glycosylation reaction of retaining cellulases, but is different from those for inverting cellulases. NAMD was used to simulate molecular dynamics of the enzyme. The 1 S 3 pre-transition state conformer is highly stable compared with other conformers, and a conformational change from 4 C 1 to 1,4 B was observed. © 2008 Elsevier Ltd. All rights reserved.},
bibtype = {article},
author = {Fushinobu, S. and Mertz, B. and Hill, A.D. and Hidaka, M. and Kitaoka, M. and Reilly, P.J.},
journal = {Carbohydrate Research},
number = {6}
}
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The predicted reaction pathway of the inverting phosphorylase is similar to that proposed for the first-half glycosylation reaction of retaining cellulases, but is different from those for inverting cellulases. NAMD was used to simulate molecular dynamics of the enzyme. The 1 S 3 pre-transition state conformer is highly stable compared with other conformers, and a conformational change from 4 C 1 to 1,4 B was observed. © 2008 Elsevier Ltd. 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