Results 121 to 130 of about 4,684 (170)

Properties of chorismate mutase ofStreptomyces venezuelae

Archiv für Mikrobiologie, 1972
1. Chorismate mutase, the first enzyme of the terminal biosynthetic pathway of phenylalanine and tyrosine has been purified 10 fold fromStreptomyces venezuelae. 2. The catalytic activity has a broad optimum between pH 6.6 and 7. The initial velocity data follow regular Michaelis-Menten kinetics with aKm of 3.8×10-4 M.
H, Görisch, F, Lingens
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Regulation of chorismate mutase in Saccharomyces cerevisiae

Molecular and General Genetics MGG, 1990
The Saccharomyces cerevisiae ARO7 gene was cloned by screening a wild-type gene bank for complementation of an aro7 auxotrophic mutant. In vitro mutagenesis of the isolated plasmid (pJFB1) gave several transformants resistant to levels of the phenylalanine analogue 2-thienylalanine inhibitory to the wild-type transformant.
J F, Brown, I W, Dawes
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The shikimate pathway. Part V. Chorismic acid and chorismate mutase

Journal of the Chemical Society, Perkin Transactions 1, 1976
The chemistry of the biochemical intermediate chorismic acid {trans-3-[(1-carboxyvinyl)oxy]-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid}(1) is discussed, including the formation of the fused pyrazoline (6) with diazomethane, the dihydro-derivatives (8) and (9) with di-imide, and the epoxide (10).
R J, Ife, L F, Ball, P, Lowe, E, Haslam
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The Monofunctional Chorismate Mutase from Bacillus subtilis

Journal of Molecular Biology, 1994
Yuh Min Chook, Joseph V. Gray, Hengming Ke, William N. Lipscomb   +3 more
exaly   +2 more sources

Chorismate mutase isozyme patterns in three fungi

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract As judged by results of gel electrophoresis and effector sensitivity, the number of chorismate mutase isozymes differs in extracts of the three fungi investigated. Neurospora crassa contains only one form of chorismate mutase designated CM 1 .
T S, Woodin, L, Nishioka
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Evidence for three isozymes of chorismate mutase in alfalfa

Biochimica et Biophysica Acta (BBA) - Enzymology, 1973
Abstract Three forms of chorismate mutase (CM1, CM2, CM3) have been found in alfalfa plants. The isozymes are separable by DEAE-cellulose fractionation and gel electrophoresis. They are distinguishable by different molecular weights (46 000, 58 000 and 69 000, respectively), different activation energies (11 300, 20 800 and 13 500 cal/mole ...
T S, Woodin, L, Nishioka
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A new test for chorismate mutase activity

Analytical Biochemistry, 1978
Abstract Chorismate mutase (EC 5.4.99.5) catalyzes the conversion of chorismic acid to prephenic acid. A continuous test of the enzymatic activity is based on the decrease of the absorption of the substrate chorismate at 274 nm (1). In a sensitive but discontinuous test, prephenic acid, the product of the enzymatic reaction is converted to ...
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Electrostatics, allostery, and activity of the yeast chorismate mutase

Proteins: Structure, Function, and Genetics, 1998
The predicted active site of chorismate mutase of baker's yeast Saccharomyces cerevisiae has been studied by continuum electrostatics, molecular surface/volume calculations, and molecular modeling. Our study shows that despite being subject to an allosteric transition, the enzyme's active-site pocket neither decreased in volume nor deformed ...
S L, Lin, D, Xu, A, Li, R, Nussinov
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An evolution-based model for designing chorismate mutase enzymes

Science, 2020
Learning from evolution Protein sequences contain information specifying their three-dimensional structure and function, and statistical analysis of families of sequences has been used to predict these properties. Building from sequence data, Russ et al.
William P. Russ, Matteo Figliuzzi, Christian Stocker, Pierre Barrat-Charlaix, Michael Socolich, Peter Kast, Donald Hilvert, Remi Monasson, Simona Cocco, Martin Weigt, Rama Ranganathan   +10 more
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Chorismate Mutase, Essentially a Template Enzyme

1997
It was a particular pleasure for the senior author to open the scientific sessions which celebrated Oleg Jardetzky’s 65th birthday anniversary. Oleg was a student in my Physical Chemistry course at the University of Minnesota in 1950, and received an M.D, from the Medical School in 1954. At that time he came to my office to ask for a Ph.D.
W.N. Lipscomb, Y.M. Chook
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