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Monofunctional chorismate mutase from Bacillus subtilis: purification of the protein, molecular cloning of the gene, and overexpression of the gene product in Escherichia coli
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This article has been cited by 6 ACS Journal articles (5 most recent appear below).
Investigation of Ligand Binding and Protein Dynamics in Bacillus subtilis Chorismate Mutase by Transverse Relaxation Optimized Spectroscopy−Nuclear Magnetic Resonance,
Alexander Eletsky, Alexander Kienhöfer, Donald Hilvert, and Konstantin PervushinBiochemistry2005 44 (18), 6788-6799Investigation of Ligand Binding and Protein Dynamics in Bacillus subtilis Chorismate Mutase by Transverse Relaxation Optimized Spectroscopy−Nuclear Magnetic Resonance,
Alexander Eletsky, Alexander Kienhöfer, Donald Hilvert, and Konstantin PervushinBiochemistry2005 44 (18), 6788-6799The structural and dynamical consequences of ligand binding to a monofunctional chorismate mutase from Bacillus subtilis have been investigated by solution NMR spectroscopy. TROSY methods were employed to assign 98% of the backbone 1HN, 1H, 15N, 13C, ...
Selective Stabilization of the Chorismate Mutase Transition State by a Positively Charged Hydrogen Bond Donor
Alexander Kienhöfer, Peter Kast, and Donald HilvertJournal of the American Chemical Society2003 125 (11), 3206-3207Selective Stabilization of the Chorismate Mutase Transition State by a Positively Charged Hydrogen Bond Donor
Alexander Kienhöfer, Peter Kast, and Donald HilvertJournal of the American Chemical Society2003 125 (11), 3206-3207Citrulline was incorporated via chemical semisynthesis at position 90 in the active site of the AroH chorismate mutase from Bacillus subtilis. The wild-type arginine at this position makes hydrogen-bonding interactions with the ether oxygen of chorismate. ...
Electrostatic Complementarity at Ligand Binding Sites: Application to Chorismate Mutase
Erik Kangas and Bruce TidorThe Journal of Physical Chemistry B2001 105 (4), 880-888Electrostatic Complementarity at Ligand Binding Sites: Application to Chorismate Mutase
Erik Kangas and Bruce TidorThe Journal of Physical Chemistry B2001 105 (4), 880-888Charge optimization methods facilitate examination and, potentially, improvement of electrostatic interactions between binding partners. Here charge optimization was applied to the chorismate mutase from Bacillus subtilis binding an endo-oxabicyclic ...
The Electronic Spectrum of the Prephenate Dianion. An Experimental and Theoretical (MD/QM) Comparison
Adrian E. Roitberg, Sharon E. Worthington, Marcia J. Holden, Martin P. Mayhew, and Morris KraussJournal of the American Chemical Society2000 122 (30), 7312-7316The Electronic Spectrum of the Prephenate Dianion. An Experimental and Theoretical (MD/QM) Comparison
Adrian E. Roitberg, Sharon E. Worthington, Marcia J. Holden, Martin P. Mayhew, and Morris KraussJournal of the American Chemical Society2000 122 (30), 7312-7316Prephenate is the product of a Claisen rearrangement of chorismate. The enzyme chorismate mutase (CM from B. subtilis) accelerates the reaction by a factor of 106. The standard method for quantifying prephenate measures the electronic absorption spectrum ...
Mutagenesis Study of Active Site Residues in Chorismate Mutase from Bacillus subtilis
Sharon T. Cload, David R. Liu, Richard M. Pastor, and Peter G. SchultzJournal of the American Chemical Society1996 118 (7), 1787-1788Mutagenesis Study of Active Site Residues in Chorismate Mutase from Bacillus subtilis
Sharon T. Cload, David R. Liu, Richard M. Pastor, and Peter G. SchultzJournal of the American Chemical Society1996 118 (7), 1787-1788
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- Published In Issue January, 1990
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