The Experts below are selected from a list of 9 Experts worldwide ranked by ideXlab platform

Seungho Kim - One of the best experts on this subject based on the ideXlab platform.

  • Endopeptidase Clp atp dependent Clp protease from escherichia coli
    Methods in Enzymology, 1994
    Co-Authors: Michael R Maurizi, Mark W Thompson, Satyendra K Singh, Seungho Kim
    Abstract:

    Publisher Summary Escherichia coli Clp protease is a multicomponent protease that has an adenosine triphosphate (ATP)-activated proteolytic activity and an ATPase activity that is activated by proteins and peptides. This chapter describes purification and properties of two components of Clp protease—namely, ClpP and ClpA. These two components by themselves form an active complex, referred as “ClpAP protease,” responsible for degradation of specific classes of proteins. The regulatory subunit of Clp protease, ClpA, can be overexpressed in mostly soluble form in E. coli cells, both under its own promoter and under strong promoters such as p L and p tac on multicopy plasmids. Repeated freezing and thawing of purified ClpA and relatively short exposures to temperatures above 10° lead to losses of activity. ATP and nonhydrolyzable analogs of ATP stabilize ClpA. ClpA and ClpP form a tight complex in the presence of MgCl 2 and ATP or the nonhydrolyzable analog, ATP γ S. The ClpAP complex is composed of a dodecamer of ClpP and a hexamer of ClpA.

Michael R Maurizi - One of the best experts on this subject based on the ideXlab platform.

  • Endopeptidase Clp atp dependent Clp protease from escherichia coli
    Methods in Enzymology, 1994
    Co-Authors: Michael R Maurizi, Mark W Thompson, Satyendra K Singh, Seungho Kim
    Abstract:

    Publisher Summary Escherichia coli Clp protease is a multicomponent protease that has an adenosine triphosphate (ATP)-activated proteolytic activity and an ATPase activity that is activated by proteins and peptides. This chapter describes purification and properties of two components of Clp protease—namely, ClpP and ClpA. These two components by themselves form an active complex, referred as “ClpAP protease,” responsible for degradation of specific classes of proteins. The regulatory subunit of Clp protease, ClpA, can be overexpressed in mostly soluble form in E. coli cells, both under its own promoter and under strong promoters such as p L and p tac on multicopy plasmids. Repeated freezing and thawing of purified ClpA and relatively short exposures to temperatures above 10° lead to losses of activity. ATP and nonhydrolyzable analogs of ATP stabilize ClpA. ClpA and ClpP form a tight complex in the presence of MgCl 2 and ATP or the nonhydrolyzable analog, ATP γ S. The ClpAP complex is composed of a dodecamer of ClpP and a hexamer of ClpA.

Mark W Thompson - One of the best experts on this subject based on the ideXlab platform.

  • Endopeptidase Clp atp dependent Clp protease from escherichia coli
    Methods in Enzymology, 1994
    Co-Authors: Michael R Maurizi, Mark W Thompson, Satyendra K Singh, Seungho Kim
    Abstract:

    Publisher Summary Escherichia coli Clp protease is a multicomponent protease that has an adenosine triphosphate (ATP)-activated proteolytic activity and an ATPase activity that is activated by proteins and peptides. This chapter describes purification and properties of two components of Clp protease—namely, ClpP and ClpA. These two components by themselves form an active complex, referred as “ClpAP protease,” responsible for degradation of specific classes of proteins. The regulatory subunit of Clp protease, ClpA, can be overexpressed in mostly soluble form in E. coli cells, both under its own promoter and under strong promoters such as p L and p tac on multicopy plasmids. Repeated freezing and thawing of purified ClpA and relatively short exposures to temperatures above 10° lead to losses of activity. ATP and nonhydrolyzable analogs of ATP stabilize ClpA. ClpA and ClpP form a tight complex in the presence of MgCl 2 and ATP or the nonhydrolyzable analog, ATP γ S. The ClpAP complex is composed of a dodecamer of ClpP and a hexamer of ClpA.

Satyendra K Singh - One of the best experts on this subject based on the ideXlab platform.

  • Endopeptidase Clp atp dependent Clp protease from escherichia coli
    Methods in Enzymology, 1994
    Co-Authors: Michael R Maurizi, Mark W Thompson, Satyendra K Singh, Seungho Kim
    Abstract:

    Publisher Summary Escherichia coli Clp protease is a multicomponent protease that has an adenosine triphosphate (ATP)-activated proteolytic activity and an ATPase activity that is activated by proteins and peptides. This chapter describes purification and properties of two components of Clp protease—namely, ClpP and ClpA. These two components by themselves form an active complex, referred as “ClpAP protease,” responsible for degradation of specific classes of proteins. The regulatory subunit of Clp protease, ClpA, can be overexpressed in mostly soluble form in E. coli cells, both under its own promoter and under strong promoters such as p L and p tac on multicopy plasmids. Repeated freezing and thawing of purified ClpA and relatively short exposures to temperatures above 10° lead to losses of activity. ATP and nonhydrolyzable analogs of ATP stabilize ClpA. ClpA and ClpP form a tight complex in the presence of MgCl 2 and ATP or the nonhydrolyzable analog, ATP γ S. The ClpAP complex is composed of a dodecamer of ClpP and a hexamer of ClpA.

Alan J. Barrett - One of the best experts on this subject based on the ideXlab platform.

  • proteolytic enzymes serine and cysteine peptidases
    1994
    Co-Authors: Alan J. Barrett
    Abstract:

    A.J. Barrett, Classification of Peptidases. Serine Peptidases: N.D. Rawlings and A.J. Barrett, Families of Serine Peptidases. J.R. Hoidal, N.V. Rao, and B. Gray, Myeloblastin: Leukocyte Proteinase 3. M.M. Simon and M.D. Kramer, Granzyme A. M.C. Peitsch and J. Tschopp, Granzyme B. L.B. Schwartz, Tryptase: A Mast Cell Serine Protease. K. Kurachi, A. Torres-Rosado, and A. Tsuji, Hepsin. J.J. Birktoft and K. Breddam, Glutamyl Endopeptidases. F. Sakiyama and T. Masaki, Lysyl Endopeptidase of Achromobacter lyticus. A.G. Plaut and W.W. Bachovchin, IgA-Specific Prolyl Endopeptidases: Serine Type. C. Brenner, A. Bevan, and R.S. Fuller, Biochemical and Genetic Methods for Analyzing Specificity and Activity of Precursor-Processing Enzyme: Yeast Kex2 Protease, Kexin. K. Nakayama, Purification of Recombinant Soluble Forms of Furin Produced in Chinese Hamster Ovary Cells. N.G. Seidah and M. Chretien, Pro-Protein Convertases of Subtilisin/Kexin Family. L. Polgar, Prolyl Oligopeptidases. D. Tsuru and T. Yoshimoto, Oligopeptidase B: Protease II from Escherichia coli. Y. Ikehara, S. Ogata, and Y. Misumi, Dipeptidyl-peptidase IV from Rat Liver. W.M. Jones, A. Scaloni, and J.M. Manning, Acylaminoacyl-peptidase. S.J. Remington and K. Breddam, Carboxypeptidases C and D. B. Granier, M. Jamin, M. Adam, M. Galleni, B. Lakaye, W. Zorzi, J. Grandchamps, J.-M. Wilkin, C. Fraipont, B. Joris, C. Duez, M. Nguyen-Distoche, J. Coyette, M. Leyh-Bouille, J. Dusart, L. Christiaens, J.-M. Frore, and J.-M. Ghuysen, Serine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins. J.W. Little, B. Kim, K.L. Roland, M.H. Smith, L.-L. Lin, and S.N. Slilaty, Cleavage of LexA Repressor. W.R. Tschantz and R.E. Dalbey, Bacterial Leader Peptidase 1. M.O. Lively, A.L. Newsome, and M. Nusier, Eukaryote Microsomal Signal Peptidases. M.R. Maurizi, M.W. Thompson, S.K. Singh, and S.-H. Kim, Endopeptidase Clp: ATP-Dependent Clp Protease from Escherichia coli. A.J. Rivett, P.J. Savory, and H. Djaballah, Multicatalytic Endopeptidase Complex: Proteasome. A.L. Goldberg, R.P. Moerschell, C.H. Chung, and M.R. Maurizi, ATP-Dependent Protease La (Lon) from Escherichia coli. S. Kuzela and A.L. Goldberg, Mitochondrial ATP-Dependent Protease from Rat Liver and Yeast. W.F. Mangel, D.L. Toledo, M.T. Brown, K. Worzalla, M. Lee, and J.J. Dunn, Omptin: An Escherichia coli Outer Membrane Proteinase That Activates Plasminogen. W. Gibson, A.R. Welch, and J. Ludford, Transient Transfection Assay of the Herpesvirus Maturational Proteinase, Assemblin. M.C. Smith, J. Giordano, J.A. Cook, M. Wakulchik, E.C. Villarreal, G.W. Becker, K. Bemis, J. Labus, and J.S. Manetta, Purification and Kinetic Characterization of Human Cytomegalovirus Assemblin. J. Oleksyszyn and J.C. Powers, Amino Acid and Peptide Phosphonate Derivatives as Specific Inhibitors of Serine Peptidases. J.C. Powers and C.-M. Kam, Isocoumarin Inhibitors of Serine Peptidases. Cysteine Peptidases: N.D. Rawlings and A.J. Barrett, Families of Cysteine Peptidases. A.C. Storer and R. Menard, Catalytic Mechanism in Papain Family of Cysteine Peptidases. H. Kirschke and B. Wiederanders, Cathepsin S and Related Lysosomal Endopeptidases. H. Scholze and E. Tannich, Cysteine Endopeptidases of Entamoeba histolytica. M.J. North, Cysteine Endopeptidases of Parasitic Protozoa. D.J. Buttle, Glycyl Endopeptidase. A.D. Rowan and D.J. Buttle, Pineapple Cysteine Endopeptidases. S.G. Gordon, Cancer Procoagulant. T. Skern and H.-D. Liebig, Picornains 2A and 3C. J.M. Weber and K. Tihanyi, Adenovirus Endopeptidases. S-I. Ishii, Legumain: Asparaginyl Endopeptidase. N.A. Thornberry, Interleukin-1( Converting Enzyme. R.R. Rando and Y.-T. Ma, Isoprenylated Protein Endopeptidase. D.J. Buttle, Affinity Chromatography of Cysteine Peptidases. E. Shaw, Peptidyl Diazomethanes as Inhibitors of Cysteine and Serine Proteinases. A. Krantz, Peptidyl (Acyloxy)methanes as Quiescent Affinity Labels for Cysteine Proteinases. D. Brimme and H.-U. Demuth, N,O-Diacyl Hydroxamates as Selective and Irreversible Inhibitors of Cysteine Proteinases. M. Abrahamson, Cystatins. Author Index. Subject Index.