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Alan J. Barrett - One of the best experts on this subject based on the ideXlab platform.
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Families of cysteine peptidases.
Methods in Enzymology, 2004Co-Authors: Neil D. Rawlings, Alan J. BarrettAbstract:Publisher Summary This chapter presents families of cysteine peptidases. The activity of all cysteine peptidases depends on a catalytic dyad of cysteine and histidine. The order of the cysteine and histidine residues (Cys/His or His/Cys) in the linear sequence differs between families and this is among the lines of evidence suggesting that cysteine peptidases have had many separate evolutionary origins. The families C1, C2, and C10 can be described as “papainlike,” and form clan CA. The papain family contains peptidases with a wide variety of activities, including Endopeptidases with broad specificity, Endopeptidases with narrow specificity, aminopeptidases, and peptidases with both Endopeptidase and exopeptidase activities. Papain homologs are generally either lysosomal or secreted proteins. The calpain family includes the calcium-dependent cytosolic Endopeptidase calpain, which is known from birds and mammals, and the product of the sol gene in Drosophila. Calpain is a complex of two peptide chains. Picornains are a family of polyprotein-processing Endopeptidases from single-stranded RNA viruses. Each picornavirus has two picornains (2A and 3C).
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Identification of the active site of legumain links it to caspases, clostripain and gingipains in a new clan of cysteine Endopeptidases.
FEBS Letters, 1998Co-Authors: Jinq-may Chen, Neil D. Rawlings, Richard A. E. Stevens, Alan J. BarrettAbstract:We show by site-directed mutagenesis that the catalytic residues of mammalian legumain, a recently discovered lysosomal asparaginycysteine Endopeptidase, form a catalytic dyad in the motif His-Gly-spacer-Ala-Cys. We note that the same motif is present in the caspases, aspartate-specific Endopeptidases central to the process of apoptosis in animal cells, and also in the families of clostripain and gingipain which are arginyl/lysyl Endopeptidases of pathogenic bacteria. We propose that the four families have similar protein folds, are evolutionarily related in clan CD, and have common characteristics including substrate specificities dominated by the interactions of the S1 subsite.
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proteolytic enzymes serine and cysteine peptidases
1994Co-Authors: Alan J. BarrettAbstract: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.
Ken-ichi Kodaira - One of the best experts on this subject based on the ideXlab platform.
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genetic and biochemical characterization of glutamyl Endopeptidase of staphylococcus warneri m
Gene, 2001Co-Authors: Kenji Yokoi, Ayanori Yamakawa, Akira Taketo, Makiko Kakikawa, Hisashi Kimoto, Kouichi Watanabe, Hiroo Yasukawa, Ken-ichi KodairaAbstract:Abstract A Staphylococcus warneri strain M, newly isolated from processed seafood (smoked Watasenia scintillans), produced an extracellular protease. The protease, designated to as m-PROM (the mature form of PROM), selectively cleaved the carbonyl side of glutamic acid residues in β-casein. Sequence of N-terminal 27 amino acids of m-PROM, RANVILPNNDRHQINDTTLGHYAPVTF, was found to be similar to those of other glutamyl Endopeptidases, V8 protease (Staphylococcus aureus strain V8) and SPase (S. aureus ATCC 12600). To determine the complete primary structure and precursor of PROM, its gene (proM) was cloned and sequenced. The gene proM was found to encode for a protein of 316 amino acids. The amino acid residues from 64 to 90 completely coincided with the N-terminal 27 amino acids of the m-PROM, suggesting that the N-terminal 63 amino acids region of p-PROM (the precursor form of PROM) might be processed posttranslationally. Moreover, the whole amino acid sequence deduced from the primary structure of proM shows significant similarity to those of other glutamyl Endopeptidases, V8 protease and SPase. These results suggested that PROM belongs to the glutamyl Endopeptidase class. PROM, however, differs from V8 and SPase proteases in the processing site and the C-terminal region.
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Genetic and biochemical characterization of glutamyl Endopeptidase of Staphylococcus warneri M.
Gene, 2001Co-Authors: Kenji Yokoi, Ayanori Yamakawa, Akira Taketo, Makiko Kakikawa, Hisashi Kimoto, Kouichi Watanabe, Hiroo Yasukawa, Ken-ichi KodairaAbstract:A Staphylococcus warneri strain M, newly isolated from processed seafood (smoked Watasenia scintillans), produced an extracellular protease. The protease, designated to as m-PROM (the mature form of PROM), selectively cleaved the carbonyl side of glutamic acid residues in beta-casein. Sequence of N-terminal 27 amino acids of m-PROM, RANVILPNNDRHQINDTTLGHYAPVTF, was found to be similar to those of other glutamyl Endopeptidases, V8 protease (Staphylococcus aureus strain V8) and SPase (S. aureus ATCC 12600). To determine the complete primary structure and precursor of PROM, its gene (proM) was cloned and sequenced. The gene proM was found to encode for a protein of 316 amino acids. The amino acid residues from 64 to 90 completely coincided with the N-terminal 27 amino acids of the m-PROM, suggesting that the N-terminal 63 amino acids region of p-PROM (the precursor form of PROM) might be processed posttranslationally. Moreover, the whole amino acid sequence deduced from the primary structure of proM shows significant similarity to those of other glutamyl Endopeptidases, V8 protease and SPase. These results suggested that PROM belongs to the glutamyl Endopeptidase class. PROM, however, differs from V8 and SPase proteases in the processing site and the C-terminal region.
Igor S. Kulaev - One of the best experts on this subject based on the ideXlab platform.
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cloning and expression analysis of genes encoding lytic Endopeptidases l1 and l5 from lysobacter sp strain xl1
Applied and Environmental Microbiology, 2012Co-Authors: Yu S Lapteva, O. A. Stepnaya, I. M. Tsfasman, Igor S. Kulaev, O E Zolova, M G Shlyapnikov, T A Muranova, I E GranovskyAbstract:Lytic enzymes are the group of hydrolases that break down structural polymers of the cell walls of various microorganisms. In this work, we determined the nucleotide sequences of the Lysobacter sp. strain XL1 alpA and alpB genes, which code for, respectively, secreted lytic Endopeptidases L1 (AlpA) and L5 (AlpB). In silico analysis of their amino acid sequences showed these Endopeptidases to be homologous proteins synthesized as precursors similar in structural organization: the mature enzyme sequence is preceded by an N-terminal signal peptide and a pro region. On the basis of phylogenetic analysis, Endopeptidases AlpA and AlpB were assigned to the S1E family [clan PA(S)] of serine peptidases. Expression of the alpA and alpB open reading frames (ORFs) in Escherichia coli confirmed that they code for functionally active lytic enzymes. Each ORF was predicted to have the Shine-Dalgarno sequence located at a canonical distance from the start codon and a potential Rho-independent transcription terminator immediately after the stop codon. The alpA and alpB mRNAs were experimentally found to be monocistronic; transcription start points were determined for both mRNAs. The synthesis of the alpA and alpB mRNAs was shown to occur predominantly in the late logarithmic growth phase. The amount of alpA mRNA in cells of Lysobacter sp. strain XL1 was much higher, which correlates with greater production of Endopeptidase L1 than of L5.
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Secretion of bacteriolytic Endopeptidase L5 of Lysobacter sp. XL1 into the medium by means of outer membrane vesicles.
The FEBS journal, 2008Co-Authors: Natalia V. Vasilyeva, O. A. Stepnaya, Natalia E. Suzina, I. M. Tsfasman, Igor S. KulaevAbstract:The Gram-negative bacterium Lysobacter sp. XL1 secretes various proteins, including bacteriolytic enzymes (L1-L5), into the culture medium. These proteins are able to degrade Gram-positive bacteria. The mechanism of secretion of extracellular proteins by Lysobacter sp. XL1 has not been studied hitherto. Electron microscopic investigations revealed the phenomenon of the formation of extracellular vesicles by Lysobacter sp. XL1. These vesicles contained components of the Lysobacter sp. XL1 outer membrane, and demonstrated bacteriolytic activity against Gram-positive and Gram-negative bacteria: Staphylococcus aureus 209-P and Erwinia marcescens EC1, respectively. Western blotting analysis with antibodies to homologous bacteriolytic Endopeptidases L1 and L5 showed that Endopeptidase L5 was secreted into the culture medium by means of vesicles, unlike its homolog, Endopeptidase L1. When inside the vesicles, Endopeptidase L5 actively lysed the Gram-negative bacterium Erwinia marcescens; outside the vesicles, it lost this ability. The secretion of bacteriolytic Endopeptidase L5 through the outer membrane vesicles is of great biological significance: because of this ability, Lysobacter sp. XL1 can compete in nature with both Gram-positive and Gram-negative bacteria.
Kenji Yokoi - One of the best experts on this subject based on the ideXlab platform.
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genetic and biochemical characterization of glutamyl Endopeptidase of staphylococcus warneri m
Gene, 2001Co-Authors: Kenji Yokoi, Ayanori Yamakawa, Akira Taketo, Makiko Kakikawa, Hisashi Kimoto, Kouichi Watanabe, Hiroo Yasukawa, Ken-ichi KodairaAbstract:Abstract A Staphylococcus warneri strain M, newly isolated from processed seafood (smoked Watasenia scintillans), produced an extracellular protease. The protease, designated to as m-PROM (the mature form of PROM), selectively cleaved the carbonyl side of glutamic acid residues in β-casein. Sequence of N-terminal 27 amino acids of m-PROM, RANVILPNNDRHQINDTTLGHYAPVTF, was found to be similar to those of other glutamyl Endopeptidases, V8 protease (Staphylococcus aureus strain V8) and SPase (S. aureus ATCC 12600). To determine the complete primary structure and precursor of PROM, its gene (proM) was cloned and sequenced. The gene proM was found to encode for a protein of 316 amino acids. The amino acid residues from 64 to 90 completely coincided with the N-terminal 27 amino acids of the m-PROM, suggesting that the N-terminal 63 amino acids region of p-PROM (the precursor form of PROM) might be processed posttranslationally. Moreover, the whole amino acid sequence deduced from the primary structure of proM shows significant similarity to those of other glutamyl Endopeptidases, V8 protease and SPase. These results suggested that PROM belongs to the glutamyl Endopeptidase class. PROM, however, differs from V8 and SPase proteases in the processing site and the C-terminal region.
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Genetic and biochemical characterization of glutamyl Endopeptidase of Staphylococcus warneri M.
Gene, 2001Co-Authors: Kenji Yokoi, Ayanori Yamakawa, Akira Taketo, Makiko Kakikawa, Hisashi Kimoto, Kouichi Watanabe, Hiroo Yasukawa, Ken-ichi KodairaAbstract:A Staphylococcus warneri strain M, newly isolated from processed seafood (smoked Watasenia scintillans), produced an extracellular protease. The protease, designated to as m-PROM (the mature form of PROM), selectively cleaved the carbonyl side of glutamic acid residues in beta-casein. Sequence of N-terminal 27 amino acids of m-PROM, RANVILPNNDRHQINDTTLGHYAPVTF, was found to be similar to those of other glutamyl Endopeptidases, V8 protease (Staphylococcus aureus strain V8) and SPase (S. aureus ATCC 12600). To determine the complete primary structure and precursor of PROM, its gene (proM) was cloned and sequenced. The gene proM was found to encode for a protein of 316 amino acids. The amino acid residues from 64 to 90 completely coincided with the N-terminal 27 amino acids of the m-PROM, suggesting that the N-terminal 63 amino acids region of p-PROM (the precursor form of PROM) might be processed posttranslationally. Moreover, the whole amino acid sequence deduced from the primary structure of proM shows significant similarity to those of other glutamyl Endopeptidases, V8 protease and SPase. These results suggested that PROM belongs to the glutamyl Endopeptidase class. PROM, however, differs from V8 and SPase proteases in the processing site and the C-terminal region.
Jean-pierre Vincent - One of the best experts on this subject based on the ideXlab platform.
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Contribution of Endopeptidase 3.4.24.15 to central neurotensin inactivation
European journal of pharmacology, 1997Co-Authors: Bruno Vincent, Jiri Jiracek, Florence Noble, Mart Loog, Bernard P. Roques, Vincent Dive, Jean-pierre Vincent, Frédéric CheclerAbstract:Abstract The tridecapeptide, neurotensin elicits naloxone-insensitive analgesia after its intracebroventricular administration in mice. We used this central pharmacological effect to assess the putative contribution of the Endopeptidase 3.4.24.15 to central inactivation of the peptide. By means of combinatorial chemistry, we previously designed the first potent Endopeptidase 3.4.24.15 inhibitor. This agent, Z-( l , d )PheΨ(PO2CH2)( l , d )Ala–Lys–Met (phosphodiepryl 21), is shown here to behave as a fully specific Endopeptidase 3.4.24.15 inhibitor, as demonstrated by the absence of effect on a series of other exo- and Endopeptidases belonging to various classes of proteolytic activities present in murine brain membranes. Furthermore, central administration of phosphodiepryl 21 drastically prolongs the forepaw licking latency of mice tested on the hot plate and injected with sub-maximally active doses of neurotensin. Altogether, our results demonstrated that, in addition to Endopeptidase 3.4.24.16, Endopeptidase 3.4.24.15 likely contributes to the physiological termination of the neurotensinergic message in murine brain.
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A survey of the cerebral regionalization and ontogeny of eight exo- and Endopeptidases in murines
Peptides, 1993Co-Authors: Pascale Dauch, Jean-pierre Vincent, Yoshinori Masuo, Frédéric CheclerAbstract:Abstract We have established the cerebral regionalization and ontogeny of eight exo- and Endopeptidases in murines. Aminopeptidases A, B, and M, post-proline dipeptidylaminopeptidase (DAP IV), and proline Endopeptidase displayed a rather homogenous distribution within the brain regions with a three- to fourfold factor between the porrest and richest areas. Aminopeptidases M and B appeared maximal in the parietal cortex and nucleus accumbens, respectively, while proline Endopeptidase was abundant in the piriform cortex. By contrast with the peptidases exhibiting a rather homogenous distribution, Endopeptidase 24.11, angiotensin-converting enzyme, and, to a lesser extent, Endopeptidase 24.15 appeared located in much more discrete cerebral zones. Angiotensin-converting enzyme activity was mainly restricted to the nigro-striatal axis. Such feature also stands for Endopeptidase 24.11, which was also detected in additional zones corresponding to the globus pallidus and the nucleus accumbens. Endopeptidase 24.15 activity was maximal in the nucleus accumbens and particularly weak in the mamillary body. Neuropeptidases appeared differently regulated during development of mouse brain. Aminopeptidase M, DAP IV, and Endopeptidase 24.15 were detected in utero, and their specific activities did not significantly vary until adulthood. Proline Endopeptidase and Endopeptidase 24.11 were detected in high quantity at day 9 before birth, then activity decreased until birth. Then, proline Endopeptidase augmented and plateaued between day 3 and day 10, while Endopeptidase 24.11 remained constant at a relatively low level. Finally, angiotensin-converting enzyme was virtually undetectable at early stages before parturition, then slightly increased after birth. The possibility that distinct cerebral regionalization and ontogeny of peptides could directly influence peptide physiology and/or reflect additional functions of the peptidases besides peptide degradation is discussed.
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Hydrolysis of rat melanin-concentrating hormone by Endopeptidase 24.11 (neutral Endopeptidase).
Biochemical Journal, 1992Co-Authors: Frédéric Checler, Pascale Dauch, Hélène Barelli, Jean-louis Nahon, Jean-pierre VincentAbstract:Melanin-concentrating hormone (MCH) is a cyclic peptide which behaves as an antagonist of the pituitary melanotropic hormone alpha-melanocyte-stimulating hormone in fishes. Cloning of the rat MCH cDNA precursor recently revealed the presence of an additional putative peptide named NEI. The present work examined the susceptibility of these novel peptides to hydrolysis by various purified exo- and endo-peptidases including Endopeptidases 24.11 (NEP), 24.15, 24.16, angiotensin-converting enzyme, leucine aminopeptidase and carboxypeptidase A. NEP attacked MCH at three sites of the molecule with an apparent affinity of about 12 microM and a kcat. of 4 min-1. The first site of cleavage was at Cys-7-Met-8, i.e. within the peptide loop formed by the internal disulphide bridge. NEP could therefore be considered as an MCH-inactivating peptidase since the degradation products generated are probably devoid of biological activity. In contrast, NEI neither inhibited the degradation of the NEP chromogenic substrate glutaryl-Phe-Ala-Phe-p-aminobenzoate nor was susceptible to proteolysis by NEP. Unlike NEP, angiotensin-converting enzyme, Endopeptidase 24.15 and Endopeptidase 24.16 appeared totally unable to cleave MCH, whereas the peptide was readily degraded by aminopeptidase M and carboxypeptidase A.