Results 181 to 190 of about 43,584 (222)

Inactivation of yeast enolase with tetranitromethane

Biochemical and Biophysical Research Communications, 1982
Abstract Yeast enolase is inactivated by tetranitromethane with production of 1.2 moles of nitrotyrosine per subunit. Protection is afforded by “conformational” metal ion alone. Enzyme thus inactivated no longer appears to bind “conformational” metal ion.
S G, Spencer, J M, Brewer
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Lobster enolase crystallized by serendipity

Proteins: Structure, Function, and Bioinformatics, 1994
AbstractAn unknown protein crystallized from a lobster muscle preparation in which arginine kinase was the majority component. It was identified as enolase by peptide sequencing and activity testing, and a SIRAS electron density map showed its three‐dimensional structure to be very similar to that of yeast enolase. © 1994 John Wiley & Sons, Inc.
S, Duquerroy, G, Le Bras, J, Janin
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The Role of Enolases in Allergic Disease

The Journal of Allergy and Clinical Immunology: In Practice, 2021
Enolase is one of the most abundant cytosolic enzymes as well as an important glycolytic metalloenzyme highly conserved among organisms from different taxonomical groups. Participation of enolase in processes in which its enzymatic activity is not required has been widely reported.
Martha Beatriz, Morales-Amparano, José Ángel, Huerta-Ocampo, Guillermo, Pastor-Palacios, Luis M, Teran   +3 more
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Comparative enzymology of molluscan enolases

Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 1971
1. 1. Enolases from five molluscs have been isolated and partially characterized. 2. 2. Michaelis constants, metal ion activation constants and molecular weights of molluscan enolases are typical of those obtained for enolases from a wide variety of sources. 3. 3.
D P, Hanlon, L, De Vore, M C, Kincaid, A, Jones, L, Lane   +4 more
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Structural and mechanistic studies of enolase

Current Opinion in Structural Biology, 1996
The high-resolution structure of yeast enolase cocrystallized with its equilibrium mixture of substrate and product reveals the stereochemistry of substrate/product binding and therefore the groups responsible for acid/base catalysis and stabilization of the enolate intermediate.
G H, Reed, R R, Poyner, T M, Larsen, J E, Wedekind, I, Rayment   +4 more
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The Inhibition of Enolase by Fluoride in vitro

Caries Research, 2009
The activity of a commercial preparation of muscle enolase was determined photometrically. The sensitivity of the enzyme to fluoride and the kinetics of the inhibition was studied in the absence and in the presence of 5 mM phosphate. The effects of fluoride, magnesium, phosphate and fluorophosphate were investigated by introducing these ions alone or ...
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Two high-affinity enolase inhibitors. Reaction with enolases

Biochemistry, 1971
Thomas G. Spring, Finn Wold
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Enolase

2021
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Enolase isoenzymes

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1975
C.C. Rider, C.B. Taylor
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Enolase

1990
Dietmar Schomburg, Margit Salzmann
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