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Cathepsin C: an allosteric enzyme.
Biochimica et Biophysica Acta (BBA) - Enzymology, 1970Abstract 1. 1. Cathepsin C requires Cl− for activity. Activation is also found with bromide, iodide, thiocyanate, nitrate, and chlorate. 2. 2. At saturating activator concentrations, substrates are split according to Michaelis-Menten kinetics; at non-saturating concentrations cooperativity is observed.
J. Gorter, M. Gruber
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Creation of an allosteric enzyme by domain insertion.
Journal of Molecular Biology, 2004Two allosteric enzymes have been created by the covalent linkage of non-interacting, monomeric proteins with the prerequisite effector-binding and catalytic functionalities, respectively. This was achieved through a combinatorial process called random domain insertion.
Gurkan Guntas, M. Ostermeier
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Allosteric enzyme models and their analysis by the theory of graphs.
Biochimica et Biophysica Acta (BBA) - General Subjects, 1966Abstract Possible cooperative models, intended for the description of the properties of allosteric enzymes, have been studied for the simplest case of the dimeric protein. Both the “indirect” cooperativity used by Monod et al , 1 and the “direct” cooperativity determined by the direct interaction of active sites have been investigated.
M. Volkenstein, B. Goldstein
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CHARACTERIZATION AND CONTROL OF AN IMMOBILIZED ALLOSTERIC ENZYME SYSTEM
Annals of the New York Academy of Sciences, 1981Both immobilization techniques described in this work seem appropriate for this allosteric enzyme. However, the kinetic behavior of the dCMP deaminase trapped in a protein membrane is markedly different from that observed with the enzyme in solution and with the enzyme gelled on an artificial membrane.
G. Iorio +3 more
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Kinetics of Allosteric Enzymes
Annual Review of Biophysics and Bioengineering, 1974Within the cell, hundreds of different chemical reactions go on simultaneously, each requiring different substrates and producing different products. This array of rea,ctions must be carefully regulated in order to maintain the orderly function of a cell.
C W Wu, Gordon G. Hammes
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Biochemistry, 2016
Dihydrodipicolinate synthase is a tetrameric enzyme of the diaminopimelate pathway in bacteria and plants. The protein catalyzes the condensation of pyruvate (Pyr) and aspartate semialdehyde en route to the end product lysine (Lys).
Modupeola A. Sowole +4 more
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Dihydrodipicolinate synthase is a tetrameric enzyme of the diaminopimelate pathway in bacteria and plants. The protein catalyzes the condensation of pyruvate (Pyr) and aspartate semialdehyde en route to the end product lysine (Lys).
Modupeola A. Sowole +4 more
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Choline kinase as an allosteric enzyme
Biochemical and Biophysical Research Communications, 1970Abstract Choline kinase, enriched over 1,000-fold from the filaments of Cuscuta reflexa Roxb. exhibited sigmoidal response in assays with subsaturating levels of choline. The major part of the enzymic activity in the tissue resided in particulate fractions sedimenting at low centrifugal fields.
P. S. Krishnan, Pravina N. Setty
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Allosteric Regulation of Chromatin-Modifying Enzymes
Biochemistry, 2018Dynamic changes in chromatin structure are crucial for diverse biological processes. Given the complexity of the epigenetic landscape, understanding the specificity of chromatin modification has been a major interest in the epigenetics field. Recent progress in biochemical and structural analyses in the field of chromatin biology has revealed that ...
Jung-Ae Kim, Minjung Kwon, Jaehoon Kim
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Searching for new allosteric sites in enzymes
Current Opinion in Structural Biology, 2004The discovery of new allosteric sites generates opportunities for the identification of novel pharmaceuticals and increases our understanding of basic biological processes. Increasingly, allosteric sites are being discovered in various families of proteins by several methods, paving the way for the development of entirely new classes of drugs with a ...
Jeanne A. Hardy, James A. Wells
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Pseudilins: halogenated, allosteric inhibitors of the non-mevalonate pathway enzyme IspD.
Angewandte Chemie, 2014The enzymes of the non-mevalonate pathway for isoprenoid biosynthesis have been identified as attractive targets with novel modes of action for the development of herbicides for crop protection and agents against infectious diseases.
A. Kunfermann +12 more
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