Identification of the histidine residue in Escherichia coli isocitrate lyase that reacts with diethylpyrocarbonate
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
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1. The branch point effect. Ultrasensitivity and subsensitivity to metabolic control.
2. Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308
3. Use of chemical modification in the crystallization of isocitrate lyase from Escherichia coli
4. Comparative structure, function and regulation of isocitrate lyase, an important assimilatory enzyme
5. Isolation, hyperexpression, and sequencing of the aceA gene encoding isocitrate lyase in Escherichia coli
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1. Purification and Characterization of Isocitrate Lyase from the Wood-Destroying Basidiomycete Fomitopsis palustris Grown on Glucose;Archives of Biochemistry and Biophysics;2002-03
2. Identification of the active-site peptide of 2,3-dihydroxybenzoic acid decarboxylase from Aspergillus oryzae;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-04
3. Structure and function of manganese-containing biomolecules;Perspectives on Bioinorganic Chemistry;1996
4. The pH Dependence and Modification by Diethyl Pyrocarbonate of Isocitrate Lyase from Phycomyces blakesleeanus;European Journal of Biochemistry;1995-09
5. Isocitrate Lyase from Cephalosporium acremonium. Role of Mg2+ Ions, Kinetics, and Evidence for a Histidine Residue in the Active Site of the Enzyme;Biochemistry;1995-05-09
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