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Topic: Peptidase

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	Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase -- ...
		Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase -- Tokunaga et al.
		Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase
		indicate that prolipoprotein signal peptidase is distinct from the M13
	www.jbc.org /cgi/content/abstract/257/17/9922 (306 words)

	Protease - Wikipedia, the free encyclopedia
		Proteases (proteinases, peptidases or proteolytic enzymes) are enzymes which break peptide bonds between amino acids of proteins.
		The threonine and glutamic peptidases was not described until 1995 and 2004, respectively.
		Peptidases can break either specific peptide bonds (limited proteolysis), depending on the amino acid sequence of a protein, or break down a complete peptide to amino acids (unlimited proteolysis).
	en.wikipedia.org /wiki/Peptidase (470 words)

	Peptidase -- Facts, Info, and Encyclopedia article (Site not responding. Last check: 2007-10-26)
		Peptidases occur naturally in all organisms and constitute 1-5% of the gene content.
		Peptidases can break either specific peptide bonds (limited proteolysis), depending on the (Organic compounds containing an amino group and a carboxylic acid group) amino acid sequence of a protein, or break down a complete peptide to amino acids (unlimited proteolysis).
		The function of peptidases is inhibited by (An antiviral drug used against HIV; interrupts HIV replication by binding and blocking HIV protease; often used in combination with other drugs) protease inhibitor enzymes.
	www.absoluteastronomy.com /encyclopedia/p/pe/peptidase.htm (518 words)

	Purification and characterization of an arginyl peptidase from the chloroplast stroma of pea seedlings. (Site not responding. Last check: 2007-10-26)
		Purification and characterization of an arginyl peptidase from the chloroplast stroma of pea seedlings.
		Fractionation of the peptidase on a sizing column suggested a size of 188 kDa for the native protein.
		This peptidase could not cleave stromal or thylakoid proteins, suggesting that its activity is limited to later stages of the protein degradation process in chloroplasts, in which short peptides are further cleaved to ultimately yield free amino acids.
	indycc1.agri.huji.ac.il /~zacha/purification.html (188 words)

	Biochemical Characterization of Signal Peptidase I from Gram-Positive Streptococcus pneumoniae -- Peng et al. 183 (2): ...
		Biochemical Characterization of Signal Peptidase I from Gram-Positive Streptococcus pneumoniae
		S-labeled prestreptokinase and its cleavage by wild-type and mutant signal peptidase I. SDS-PAGE and Coomassie brilliant blue staining of purified prestreptokinase and its cleavage by wild-type and mutant signal peptidase I. The assays were performed as described in the text.
		Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelope.
	jb.asm.org /cgi/content/full/183/2/621 (4680 words)

	World Intellectual Property Organization (Site not responding. Last check: 2007-10-26)
		These assays employ a second peptidase and a peptide, wherein the peptide comprises an N-terminal Met which is capable of being cleaved by MAP, and a C-terminal detection moiety which is capable of being released from the peptide by the second peptidase only if the N-terminal Met has been cleaved from the peptide.
		g., where a peptidase is adsorbed or covalently bound to a bead, tube, or well and the other components are in solution, or where the entire assay is performed on a solid phase such as a nitrocellulose membrane, and the detection moiety produces an insoluble detectable product upon release from the peptide.
		The reaction mixture of claim 14, wherein the second peptidase is dipeptidyl peptidase IV and the peptide comprises Met-Xaa-Pro, wherein Xaa is Ala, Cys, Gly, or Ser.
	www.wipo.int /ipdl/IPDL-CIMAGES/view/pct/getbykey5?KEY=01/27242.010419&ELEMENT_SET=DECL (4634 words)

	Kirkman's Peptidase Complete™
		Peptidase enzymes specifically function by breaking down what is known as protein peptides, which are shorter chains of amino acids.
		DPP-IV is a type of peptidase enzyme that is commonly located on the epithelial brush boarders of the small intestine where it is specifically imbedded in the mucosal membrane of the lining of the intestinal tract.
		has a balanced profile of peptidase activity meaning that it breaks the peptide bonds at the end as well as in the middle of the casein and gluten peptide molecule chain.
	www.kirkmanlabs.com /products/enzymes/peptidase/Peptidase_C_100_Spec248.html (870 words)

	Signal Peptidase Cleavage at the Flavivirus C-prM Junction: Dependence on the Viral NS2B-3 Protease for Efficient ...
		Signal peptidase cleavage at the C-prM junction in the flavivirus structural polyprotein is inefficient in the absence of
		peptidase cleavage in the lumen of the endoplasmic reticulum (ER)
		Sites of efficient cleavage by signal peptidase are indicated by arrowheads, the proteolytic cleavage catalyzed by the viral NS2B-3 complex is denoted by an arrow, and regions of the MVE C protein which were altered in the various pSTR.Cmut constructs are indicated by circles in parentheses.
	jvi.asm.org /cgi/content/full/72/3/2141 (7351 words)

	At3g05230 - signal peptidase subunit family protein (Site not responding. Last check: 2007-10-26)
		At3g05230 is a homologue of 6530401D17Rik (Microsomal signal peptidase 23 kDa subunit) from Mus musculus.
		At3g05230 is a homologue of FLJ22649 (Microsomal signal peptidase 23 kDa subunit) from Homo sapiens.
		At3g05230 is a homologue of SPC3 (Microsomal signal peptidase subunit 3) from Saccharomyces cerevisiae.
	www.ihop-net.org /UniPub/iHOP/gg/5051.html (119 words)

	Tripeptidyl Peptidase II & Cholecystokinin -- Neurotransmitter.net (Site not responding. Last check: 2007-10-26)
		Tripeptidyl peptidase II-like immunoreactivity was mostly detected in neurons, and also in ependymal cells and choroid plexuses, localizations consistent with a possible participation of the peptidase in the inactivation of cholecystokinin circulating in the cerebrospinal fluid.
		It was mainly associated with the cytoplasm of neuronal somata and dendrites, often in the vicinity of reticulum cisternae, Golgi apparatus or vesicles, and with the inner side of the dendritic plasma membrane.
		Characterization and inhibition of a cholecystokinin-inactivating serine peptidase.
	www.neurotransmitter.net /tpp2.html (10389 words)

	ARS \| Publication request: Isolation, Characterization and Mapping of the Bovine Signal Peptidase Subunit 18 Gene
		Bovine signal peptidase is very similar to other known signal peptidases from other species at both the DNA and protein level.
		Technical Abstract: Signal peptidases are responsible for the removal of amino-terminal signal peptides from secretory and integral membrane proteins and are ubiquitous in nature.
		Therefore, signal peptidase may be a candidate gene affecting economically important traits in dairy cattle such as milk production and, specifically protein yield due to its essential role in the secretory process.
	www.ars.usda.gov /research/publications/publications.htm?SEQ_NO_115=119224 (380 words)

	Cloning and Characterization of Archaeal Type I Signal Peptidase from Methanococcus voltae -- Ng and Jarrell 185 (20): ...
		The peptidase assay was performed at 0.4 M KCl with different incubation temperatures as indicated.
		The signal peptidase assay was performed as described in the legend to Fig.
		Eichler, J. Archaeal signal peptidases from the genus Thermoplasma: structural and mechanistic hybrids of the bacterial and eukaryal enzymes.
	jb.asm.org /cgi/content/full/185/20/5936 (4670 words)

	Characterization of the Prolyl Dipeptidyl Peptidase Gene (dppIV) from the Koji Mold Aspergillus oryzae -- Doumas et al. ...
		The dppIV gene encodes a prolyl dipeptidyl peptidase (DPPIV)
		Cloning, sequencing, and expression of the dipeptidyl peptidase IV gene from Flavobacterium meningosepticum in Escherichia coli.
		Primary structure of rat liver dipeptidyl peptidase IV deduced from its cDNA and identification of the NH -terminal signal sequence as the membrane-anchoring domain.
	aem.asm.org /cgi/content/full/64/12/4809 (4655 words)

	PEPB - peptidase B
		Acid phosphatase, NADP-isocitrate dehydrogenase, peptidase A, peptidase B and phosphohexose isomerase.
		This paper presents the results of an electrophoretic survey of approximately 4000 individuals from Hiroshima and Nagasaki for four erythrocyte enzymes: isocitrate dehydrogenase, peptidase A, peptidase B, and phosphohexose isomerase.
		Three private polymorphisms, at the 2,3-diphosphoglycerate mutase, peptidase B, and purine nucleoside phosphorylase loci, have been observed, which may be useful in future studies of genetic relationships between Eskimos and other circumpolar populations.
	www.ihop-net.org /UniPub/iHOP/gg/90931.html (1123 words)

	The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme -- Wolfe ...
		The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme -- Wolfe et al.
		The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzyme
		Biochemical Characterization of Signal Peptidase I from Gram-Positive Streptococcus pneumoniae
	www.jbc.org /cgi/content/abstract/257/13/7898 (448 words)

	Specific Localization of Membrane Dipeptidase and Dipeptidyl Peptidase IV in Secretion Granules of Two Different ...
		Dittié AS, Thomas L, Thomas G, Tooze SA (1997) Interaction of furin in immature secretory granules from neuroendocrine cells with the AP-1 adaptor complex is modulated by casein kinase II phosphorylation.
		Kieffer TJ, Mcintosh CHS, Pederson RA (1995) Degradation of glucose-dependent insulinotropic polypeptide and truncated glucagon-like peptide 1 in vitro and in vivo by dipeptidyl peptidase IV.
		Poulsen MD, Hansen GH, Dabelsteen E, Hoyer PE, Norén O, Sjöström H (1993) Dipeptidyl peptidase IV is sorted to the secretory granules in pancreatic islet A-cells.
	www.jhc.org /cgi/content/full/47/4/489 (3107 words)

	SPCS2 - Microsomal signal peptidase 25 kDa subunit
		SPCS2 is a homologue of 3N965 (Probable microsomal signal peptidase 25 kDa subunit) from Caenorhabditis elegans.
		SPCS2 is a homologue of At2g39960 (Probable microsomal signal peptidase 25 kDa subunit) from Arabidopsis thaliana.
		SPCS2 is a homologue of Spcs2 (Microsomal signal peptidase 25 kDa subunit) from Mus musculus.
	www.pdg.cnb.uam.es /UniPub/iHOP/gg/94961.html (493 words)

	Exogenous Peptides Delivered by Ricin Require Processing by Signal Peptidase for Transporter Associated with Antigen ...
		Signal peptidase is involved in Ag processing from ricin-mediated delivery.
		peptidase would be presented at the cell surface.
		A mutation affecting signal peptidase inhibits degradation of an abnormal membrane protein in Saccharomyces cerevisiae.
	www.jimmunol.org /cgi/content/full/169/1/99 (6602 words)

	Hydrolysis of Sequenced beta -Casein Peptides Provides New Insight into Peptidase Activity from Thermophilic Lactic ...
		The peptidases of thermophilic lactic acid bacteria have a key role in the proteolysis of Swiss cheeses during warm room ripening.
		Peptidases and amino acid catabolism in lactic acid bacteria.
		Peptidase activities in debittering and nondebittering strains of lactobacilli.
	aem.asm.org /cgi/content/full/66/12/5360 (3066 words)

	Pfam 18.0 : Peptidase_M16_C (Site not responding. Last check: 2007-10-26)
		They include proteins, which are classified as non-peptidase homologues either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity.
		In pitrilysin, it has been shown MEDLINE:7990931 that this H-x-x-E-H motif is involved in enzymatic activity; the two histidines bind zinc and the glutamate is necessary for catalytic activity.
		One is the active peptidase whereas the other, the C-terminal region, is inactive.
	pfam.wustl.edu /cgi-bin/getdesc?name=Peptidase_M16_C (244 words)

	SPC1 - Microsomal signal peptidase subunit 1 (Site not responding. Last check: 2007-10-26)
		Evidence is also presented that a double mutant lacking Spc1p and Spc2p grows well relative to wild type yeast cells, indicating that the signal peptidase complex missing at least two of its subunits is sufficient for signal peptidase activity in vivo.
		Among the three characterized subunits comprising the signal peptidase complex of the yeast Saccharomyces cerevisiae (Sec11p, Spc1p, and Spc2p), only Sec11p is essential for cell growth, signal peptide cleavage, and signal peptidase-dependent protein degradation.
		We show that both Spc1p and Spc2p are nonessential for signal peptidase activity and growth of yeast cells and that null mutations in the genes encoding Spc1p and Spc2p are synthetically lethal with a conditional mutation affecting Sec11p, an essential subunit of yeast signal peptidase.
	www.ihop-net.org /UniPub/iHOP/gg/33722.html (375 words)

	Immunization with C5a Peptidase or Peptidase-Type III Polysaccharide Conjugate Vaccines Enhances Clearance of Group B ...
		Antibody against surface-bound C5a peptidase is opsonic and initiates macrophage killing of group B streptococci.
		The group B streptococcal C5a peptidase is both a specific protease and an invasin.
		Conservation of the C5a peptidase genes in group A and B streptococci.
	iai.asm.org /cgi/content/full/70/11/6409 (4156 words)

	Evidence that “Vaginal Peptidase” Is a Bacterial Gene Product
		A peptidase has been described in vaginal samples, termed “vaginal peptidase.” This enzyme has been proposed as a tissue specific marker for vaginal debris.
		These studies reveal that “vaginal peptidase” is composed of a family of peptidase isozymes that originate from several bacterial species.
		The characterization of “vaginal peptidase” as a tissue specific marker for vaginal debris is premature.
	www.astm.org /JOURNALS/FORENSIC/PAGES/886.htm (145 words)

	The Arabidopsis Xylem Peptidase XCP1 Is a Tracheary Element Vacuolar Protein That May Be a Papain Ortholog -- Funk et ...
		The Arabidopsis Xylem Peptidase XCP1 Is a Tracheary Element Vacuolar Protein That May Be a Papain Ortholog -- Funk et al.
		XCP1 is a xylem-specific papain-like cysteine peptidase in Arabidopsis.
		In plants, increased peptidase gene expression is associated with remobilization of nitrogen from senescing source tissues
	www.plantphysiol.org /cgi/content/full/128/1/84 (6302 words)

	Cloning and functional expression of dipeptidyl peptidase IV from the ruminal bacterium Prevotella albensis M384T -- ...
		Cloning and functional expression of dipeptidyl peptidase IV from the ruminal bacterium Prevotella albensis M384T -- Walker et al.
		Anion-exchange chromatography of peptidase activities of crude cell extracts from a control clone (a) and cloned DPP-IV (b).
		Effect of inhibitors on peptidase activity of cloned DPP-IV Results are the mean of triplicate incubations.
	mic.sgmjournals.org /cgi/content/full/149/8/2227 (3665 words)

	Pfam 18.0 : Peptidase_S24 (Site not responding. Last check: 2007-10-26)
		This signature is associated with serine peptidases belong to MEROPS peptidase families: S24 (LexA family, clan SF); S26A (signal peptidase I) and S26B (signalase).
		Eukaryotic microsomal signal peptidase is involved in the removal of signal peptides from secretory proteins as they pass into the endoplasmic reticulumen MEDLINE:7845208.
		The peptidase is more complex than its mitochondrial and bacterial counterparts, containing a number of subunits, ranging from two in the chicken oviduct peptidase, to five in the dog pancreas protein MEDLINE:7845208.
	pfam.wustl.edu /cgi-bin/getdesc?name=Peptidase_S24 (698 words)

	N-linked glycosylation of dipeptidyl peptidase IV (CD26): Effects on enzyme activity, homodimer formation, and ...
		parameters of dipeptidyl peptidase cleavage of wild-type DPPIV
		Drucker, D.J. Therapeutic potential of dipeptidyl peptidase IV inhibitors for the treatment of type 2 diabetes.
		Qi, S.Y., Riviere, P.J., Trojnar, J., Junien, J.L., and Akinsanya, K.O. Cloning and characterization of dipeptidyl peptidase 10, a new member of an emerging subgroup of serine proteases.
	protsci.highwire.org /cgi/content/full/13/1/145 (5068 words)

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