Results 131 to 140 of about 4,684 (170)

The Allosteric Mechanism of Yeast Chorismate Mutase: A Dynamic Analysis

Journal of Molecular Biology, 2006
The effector-regulated allosteric mechanism of yeast chorismate mutase (YCM) was studied by normal mode analysis and targeted molecular dynamics. The normal mode analysis shows that the conformational change between YCM in the R state and in the T state can be represented by a relatively small number of low-frequency modes.
Yifei, Kong, Jianpeng, Ma, Martin, Karplus, William N, Lipscomb   +3 more
openaire   +2 more sources

Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure

Biochemistry, 1977
The enzymically catalyzed conversion of chorismate to prephenate may proceed through either a chair-like or a boat-like transition state. To distinguish between these alternatives, we have prepared a series of structural analogues of the two possible transition state structures and tested them as inhibitors of chorismate mutase-prephenate dehydrogenase
P R, Andrews, E N, Cain, E, Rizzardo, G D, Smith   +3 more
openaire   +2 more sources

The Claisen Rearrangement of an Unusual Substrate in Chorismate Mutase

The Journal of Physical Chemistry B, 2001
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.
Sharon E. Worthington, Morris Krauss
openaire   +1 more source

Preparative synthesis of prephenate from chorismate by chorismate mutase immobilized on decylamine agarose

Analytical Biochemistry, 1977
Abstract Chorismate mutase (EC 5.4.99.5) from Streptomyces aureofaciens is bound virtually irreversibly by n -decylamine-substituted agarose and remains active when immobilized by hydrophobic binding. The enzyme is not eluted by buffers containing 1 m NaCl or 50% ethylene glycol.
openaire   +2 more sources

Design, synthesis, and evaluation of aza inhibitors of chorismate mutase

Bioorganic & Medicinal Chemistry, 2004
A series of aza inhibitors (4-9) of chorismate mutase (E.C. 5.4.99.5) was designed, prepared, and evaluated against the enzyme by monitoring the direct inhibition of the chorismate, 1, to prephenate, 2, conversion. None of these aza inhibitors displayed tighter binding to the enzyme than the native substrate chorismate or greater inhibitory action than
openaire   +2 more sources

ChemInform Abstract: Chorismate Mutase in Microorganisms and Plants

ChemInform, 1996
AbstractChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.
R. M. ROMERO, M. F. ROBERTS, J. D. PHILLIPSON   +2 more
openaire   +1 more source

Stereochemistry of the rearrangement of chorismate to prephenate: chorismate mutase involves a chair transition state

Journal of the American Chemical Society, 1984
Unter Einsatz der markierten Substrate (III), (IV) bzw. (V), die zu diesem Zweck von den Autoren bereits (enzymatisch bzw. chemisch) synthetisiert worden sind, wird die enzymatische Claisen-Umlagerung von Chorismat (I) in Prephenat (II) untersucht; es wird gezeigt, das der enzymkatalysierte Prozes uber einen Ubergangszustand mit Sessel-ahnlicher ...
Steven G. Sogo, Theodore S. Widlanski, John H. Hoare, Charles E. Grimshaw, Glenn A. Berchtold, Jeremy R. Knowles   +5 more
openaire   +1 more source

The mechanism of the chorismate mutase reaction

Journal of the American Chemical Society, 1987
William J. Guilford, Shelley D. Copley, Jeremy R. Knowles   +2 more
openaire   +1 more source

Two components of chorismate mutase in Brevibacterium flavum.

Journal of biochemistry, 1979
Chorismate mutase of Brevibacterium flavum, a common enzyme in phenylalanine and tyrosine biosynthesis, was separted into two different component, A and B, with molecular weights of 250,000 and 25,000, respectively, by ammonium sulfate fractionation or gel-filtration. Both components were essential for the enzymatic activity.
I, Shiio, S, Sugimoto
openaire   +1 more source

Chorismate mutase of Chlamydomonas reinhardi

Biochimica et Biophysica Acta (BBA) - Enzymology, 1975
Gerard Zurawski, Keith D. Brown
openaire   +1 more source