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Bioscience

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Displaying 1051 - 1075 of 1261

The Crystal Structure of Chorismate Lyase Shows a New Fold and a Tightly Retained Product

August 15, 2001
Author(s)
David T. Gallagher, M P. Mayhew, Marcia J. Holden, A J. Howard, K J. Kim, V L. Vilker
The enzyme chorismate lyase (CL) catalyzes the removal of pyruvate from chorismate to produce 4-hydroxy benzoate (4HB) for the ubiquinone pathway. In Escherichia coli, CL is monomeric with 164 residues; we have determined the structure of the CL product

Raman and FTIR Spectroscopies of Fluorescein in Solutions

August 1, 2001
Author(s)
Lili Wang, A. E. Roitberg, Curtis W. Meuse, Adolfas K. Gaigalas
Raman and FTIR transform-infra red (FT-IR) spectroscopies of fluorescein in aqueous solutions have been investigated in the pH range from 9.1 to 5.4. At pH 9.1 fluorescein is in the dianion form. At pH 5.4, fluorescein is a mixture of monoanion (

An MD/QM Study of the Chorismate Mutase-Catalyzed Claisen Rearrangement Reaction

July 1, 2001
Author(s)
S. E. Worthington, A. E. Roitberg, Morris Krauss
The reaction path for the rearrangement of chorismate to prephenate, catalyzed by chorismate mutase, has been calculated with ab initio quantum chemistry. The calculation of a reaction path is initiated from two catalytically competent conformations of the

The Claisen Rearrangement of an Unusual Substrate in Chorismate Mutase

July 1, 2001
Author(s)
S. E. Worthington, Morris Krauss
The calculated reaction path for an unusual substrate of chorismate mutase (Bacillus.subtilis) is found to be completely comparable to that of the native chorismate. In the unusual substrate, the cyclohexadienyl ring in chorismate is replaced by

Reference Materials for DNA Analysis

March 1, 2001
Author(s)
Barbara C. Levin, D J. Reeder
Mention has already been made, in Section 5.1. Of the use of DNA-based techniques for control of microbiological DNA. In parallel to the work of ATCC the USA National Institute of Standards and Technology (NIST) developed three Standard Reference Materials
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