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Topic: Nonribosomal peptide

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	Nonribosomal peptide - Wikipedia, the free encyclopedia
		Nonribosomal peptide antibiotics, cytostatics, and immunosuppressants are in commercial use.
		Nonribosomal peptides are synthesized by one or more specialized nonribosomal peptide-synthetase (NRPS) enzymes.
		The NRPS genes for a certain peptide are usually organized in one operon in bacteria and in gene clusters in eukaryotes.
	en.wikipedia.org /wiki/Nonribosomal_peptide (676 words)

	Peptide - Wikipedia, the free encyclopedia
		Peptides differ from proteins, which are longer chains of amino acids, by virtue of their size.
		Nonribosomal peptides are synthesized using a modular enzyme complex (which functions much like a conveyor belt on a factory).
		Nonribosomal peptides and are confined primarily to unicellular organisms, plants, and fungi.
	en.wikipedia.org /wiki/Peptide (648 words)

	[No title] (Site not responding. Last check: 2007-11-03)
		195 : Q9Z4X6 0.46 0.57 517 639 5299 5420 122 1 1 7463 Q9Z4X6 CDA peptide synthetase I. 196 : Q93IL7 0.46 0.54 177 507 390 723 329 4 7 930 Q93IL7 Peptide synthetase (Fragment).
		654 : Q87WM7 0.41 0.50 177 509 637 972 329 5 11 3432 Q87WM7 Non-ribosomal peptide synthetase, termina 655 : Q87WM7 0.41 0.50 690 1022 637 972 329 5 11 3432 Q87WM7 Non-ribosomal peptide synthetase, termina 656 : Q83V14 0.41 0.48 177 466 17 308 285 5 12 310 Q83V14 Microcystin synthetase (Fragment).
		992 : Q88F79 0.38 0.45 177 508 1717 2065 330 6 21 3470 Q88F79 Non-ribosomal siderophore peptide synthet 993 : Q88F79 0.38 0.45 690 1021 1717 2065 330 6 21 3470 Q88F79 Non-ribosomal siderophore peptide synthet 994 : Q9F8V2 0.38 0.47 690 1022 187 519 330 4 6 599 Q9F8V2 Acyl-CoA synthetase.
	www.infobiogen.fr /db/hssp/1amu.hssp (17265 words)

	[No title] (Site not responding. Last check: 2007-11-03)
		For example, a nonribosomal peptide synthase may catalyze the covalent attachment of an amino acid or amino acid analog to an intermediate in the synthesis of a nonribosomally synthesized peptide.
		Preferred nonribosomal peptide synthases include tyrocidine synthases, bacterial and fungal nonribosomal peptide synthases, and proteins that have a region of consecutive amino acids that is substantially identical to the corresponding region of a bacterial nonribosomal peptide synthase.
		The ergotamine (D-lysergic acid-Ala-Phe-Pro) is a precursor for ergot peptide alkaloids.
	www.wipo.int /cgi-pct/guest/getbykey5?KEY=03/29409.030410&ELEMENT_SET=DECL (11329 words)

	Nonribosomal peptide: Encyclopedia topic (Site not responding. Last check: 2007-11-03)
		They are synthesized by nonribosomal (nonribosomal: a ribosome is an organelle composed of rrna (synthesized in the nucleolus) and...
		Nonribosomal peptide antibiotic (antibiotic: A chemical substance derivable from a mold or bacterium that kills microorganisms and cures infections) s, cytostatic (cytostatic: chemotherapy is the use of chemical substances to treat disease....
		Nonribosomal peptides are synthesized by one or more specialized nonribosomal peptide-synthetase (NRPS) enzyme (enzyme: Any of several complex proteins that are produced by cells and act as catalysts in specific biochemical reactions) s.
	www.absoluteastronomy.com /reference/nonribosomal_peptide (1569 words)

	The Multiple Carrier Model of Nonribosomal Peptide Biosynthesis at Modular Multienzymatic Templates -- Stein et al. 271 ... (Site not responding. Last check: 2007-11-03)
		Peptide mixtures were dissolved in 300-500 µl of 10-20% eluent B, loaded onto the columns which were equilibrated in 10-20% B, and eluted with linear gradients of acetonitrile.
		In a previous paper (11), we provided evidence from chemical and genetic studies that an active serine is involved in covalent binding of the substrate amino acids at each reaction center of gramicidin S synthetase 2, instead of a cysteine as proposed in the original version of the thiotemplate mechanism (2, 3, 4, 5).
		Peptide synthetases are composed of homologous building blocks comprising 1000-1500 amino acid residues, which are distinguished by a linear array of highly conserved sequence motifs representing the reactive structures of functional domains for substrate binding and catalysis of all intermediate steps in peptide biosynthesis as demonstrated for gramicidin S synthetase in Fig.
	www.jbc.org /cgi/content/full/271/26/15428 (6329 words)

	United States Patent Application: 0030175888
		[0037] A "nonribosomal peptide synthase" (NRPS) refers to an enzymatic complex of eukaryotic or prokaryotic origin, that is responsible for the synthesis of peptides by a nonribosomal mechanism, often known as thiotemplate synthesis (Kleinkauf and von Doehren (1987) Ann.
		Such peptides, which can be up to 20 or more amino acids in length, can have a linear, cyclic (cyclosporin, tyrocidine, mycobacilline, surfactin and others) or branched cyclic structure (polymyxin, bacitracin and others) and often contain amino acids not present in proteins or modified amino acids through methylation or epimerization.
		Leinamycin is a macrolactam of hybrid polyketide and nonribosomal peptide origin with an unprecedented 1,3-dioxo-1,2-dithiolane structure.
	appft1.uspto.gov /netacgi/nph-Parser?Sect1=PTO1&Sect2=HITOFF&d=PG01&p=1&u=/netahtml/PTO/srchnum.html&r=1&f=G&l=50&s1="20030175888".PGNR.&OS=DN/20030175888&RS=DN/20030175888 (14823 words)

	IRCE 2005: Abstract: MECHANISTIC STUDIES ON THE BIOSYNTHESIS OF CALCIUM DEPENDENT ANTIBIOTICS (CDA) (Site not responding. Last check: 2007-11-03)
		Nonribosomal peptide (NRP) biosynthesis is a powerful tool of nature for producing a wide variety of pharmacologically relevant peptide products.
		Nonribosomal peptides are a class of secondary metabolites which are widely found in nature, comprise of very diverse structures and exhibit a range of biologically important effects.
		Mechanistic studies on enzymes involved in the production of nonribosomal peptide antibiotics may well pave the way towards the engineered biosynthesis of new antibiotics that are otherwise too complicated obtain by total synthesis.
	www.irce.org /va_html_ai=262 (365 words)

	Functional Analysis of All Nonribosomal Peptide Synthetases in Cochliobolus heterostrophus Reveals a Factor, NPS6, ... (Site not responding. Last check: 2007-11-03)
		and from bacterial and fungal ACV-type nonribosomal peptide
		Analysis of a nonribosomal peptide synthetase gene from Alternaria brassicae and flanking genomic sequences.
		Characterization of the Ustilago maydis sid2 gene, encoding a multidomain peptide synthetase in the ferrichrome biosynthetic gene cluster.
	ec.asm.org /cgi/content/full/4/3/545 (6217 words)

	Molecular Ecology
		Biochemistry of peptide and polyketide biosynthesis in cyanobacteria
		The microcystin synthetase complex consists of peptide synthetases, polyketide synthases, and hybrid enzymes, and reveals a number of novel enzymatic features, signifying the potential of cyanobacterial biosynthetic systems for combinatorial biochemistry.
		We are interested in the functional role of metabolites of the nonribosomal peptide/polyketide class in planktonic cyanobacteria, in particular in the role of the cyclic hetapeptide toxin microcystin for Microcystis.
	www.biologie.hu-berlin.de /~moloeko/Research.html (291 words)

	The Marahiel Group
		A large number of therapeutically useful cyclic and linear peptides of bacterial or fungal origin are synthesized via a template-directed, nucleic acid-independend nonribosomal mechanism.
		The result is a peptide elongated by one residue fixed to the PCP and regeneration of the preceding module's PCP domain.
		The progress that has been made in the past decades towards understanding of the molecular principles of nonribosomal peptide synthesis has been extended in the last years to the structural level.
	www.chemie.uni-marburg.de /~ak66/science.html (1286 words)

	Jacques Ravel: Research (Site not responding. Last check: 2007-11-03)
		Nocardicin A is the most fully elaborated and most active of the nocardicins, a group of antibiotics belonging to the beta-lactams, which are of first-line importance in combating bacterial infections in humans.
		A terminal thioesterase is frequently present to release the peptide from the enzyme by cyclization or hydrolysis.
		One precursor of Nocardicin A is a tripeptide, nocardicin G which appears to be synthesized by a nonribosomal peptide synthetase (NRPS) encoded by two newly discovered genes ns1 and ns2.
	jhunix.hcf.jhu.edu /~ravel/research.html (706 words)

	Refs1700-1799
		D.E. Cane, C.T. Walsh, “The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases,”; Chem.
		L.E. Quadri, “Assembly of aryl-capped siderophores by modular peptide synthetases and polyketide synthases,”; Mol.
		Staunton, B. Wilkinson, “Combinatorial biosynthesis of polyketides and nonribosomal peptides,” Curr.
	www.molecularassembler.com /KSRM/Refs1700-1799.htm (1977 words)

	BCMP
		When bacteria are starved for iron, as occurs when they infect vertebrates, they turn on genes for biosynthesis of nonribosomal peptides, siderophores, that scavenge iron and then are taken back up by the bacteria.
		A variety of peptide antibiotics are cyclic peptides (gramicidin, tyrocidine, bacitracin) or cyclic lipopeptides (surfactin, daptomycin).
		These are made on nonribosomal peptide synthetase assembly lines and cyclized by the last domain, a Thioesterase (TE) domain of the multimodular enzymatic assembly line.
	bcmp.med.harvard.edu /index.php?option=com_akostaff&Itemid=51&func=fullview&staffid=33 (492 words)

	Peptide Antibiotics -- Hancock and Chapple 43 (6): 1317 -- Antimicrobial Agents and Chemotherapy (Site not responding. Last check: 2007-11-03)
		To permit full exploitation of peptides as new antimicrobial agents, it is important to determine their mode of action.
		Once the peptide has transited the outer membrane, it will bind to the negatively charged surface of the cytoplasmic membrane, created by the headgroups of phosphatidylglycerol and cardiolipin, and the amphipathic peptide will insert into the membrane interface (the region where the phospholipid headgroups meet the fatty acyl chains of the phospholipid membrane) (C).
		Bactenecin, a leukocyte antimicrobial peptide, is cytotoxic to neuronal and glial cells.
	aac.asm.org /cgi/content/full/43/6/1317 (6218 words)

	In Vivo Production of Artificial Nonribosomal Peptide Products in the Heterologous Host Escherichia coli -- Gruenewald ... (Site not responding. Last check: 2007-11-03)
		Control of directionality in nonribosomal peptide synthesis: role of the condensation domain in preventing misinitiation and timing of epimerization.
		Systematic and quantitative analysis of protein-protein recognition between nonribosomal peptide synthetases investigated in the tyrocidine biosynthetic template.
		-Lysergyl peptide synthetase from the ergot fungus Claviceps purpurea.
	aem.asm.org /cgi/content/full/70/6/3282 (6369 words)

	Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases -- Schwarzer et al. 99 (22): 14083 ... (Site not responding. Last check: 2007-11-03)
		Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases -- Schwarzer et al.
		or peptidyl PCPs, intermediates of nonribosomal peptide synthesis.
		PchC Thioesterase Optimizes Nonribosomal Biosynthesis of the Peptide Siderophore Pyochelin in Pseudomonas aeruginosa
	www.pnas.org /cgi/content/abstract/99/22/14083 (716 words)

	Support Content for: NR-2005-02-10
		Walsh is an outstanding and highly productive researcher who uses a broad integrated approach that includes genetics, protein and carbohydrate chemistry, mechanistic enzymology, molecular biology and X-ray crystallography to elucidate and exploit the pathways for natural antibiotic synthesis.
		A large variety of biologically active peptide natural products are biosynthesized by the nonribosomal peptide synthetases.
		Once released from these assembly lines, the peptides are often tailored by enzymes that glycosylate, oxygenate, and halogenate.
	www.asbmb.org /ASBMB/site.nsf/web/9F917B4F613E7D8285256FA5005D7CE5?OpenDocument (477 words)

	Generality of Peptide Cyclization Catalyzed by Isolated Thioesterase Domains of Nonribosomal Peptide Synthetases
		The C-terminal thioesterase (TE) domains from nonribosomal peptide synthetases (NRPSs) catalyze the final step in the biosynthesis of diverse biologically active molecules.
		Using synthetic peptide thioester substrates from 6 to 14 residues in length, we show that the excised TE domain from the tyrocidine NRPS can be used to generate an array of sizes of cyclic peptides with comparable kinetic efficiency.
		With an eye toward generating libraries of cyclic molecules by TE catalysis, we report the solid-phase synthesis and TE-mediated cyclization of a small pool of linear peptide thioesters.
	pubs.acs.org /cgi-bin/abstract.cgi/bichaw/2001/40/i24/abs/bi010036j.html (241 words)

	Chemical Reviews Volume 97
		Post-translational modification of polyketide and nonribosomal peptide synthases.
		Staunton J, Wilkinson B. Combinatorial biosynthesis of polyketides and nonribosomal peptides.
		Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines.
	www.npbiogene.com /review.htm (228 words)

	Suzanne J. Admiraal- Biological Chemistry
		The biosynthesis of many polyketides and peptides occurs on modular protein assembly lines known as polyketide synthases (PKS) and nonribosomal peptide synthetases (NRPS), respectively.
		For example, after each condensation reaction joining a new acetate-derived monomer to a growing polyketide chain, a PKS module causes the resulting ß-carbonyl to undergo all, part, or none of a reductive cycle of ß-ketoreduction, dehydration, and enoyl reduction.
		Admiraal, S.J., Khosla, C., Walsh, C.T. (2003) A switch for the transfer of substrate between nonribosomal peptide and polyketide modules of the rifamycin synthetase assembly line.
	www.biochem.med.umich.edu /biochem/research/profiles/admiraal.html (319 words)

	Characterization of the angR Gene of Vibrio anguillarum: Essential Role in Virulence -- Wertheimer et al. 67 (12): 6496 ...
		Squares indicate regions where the core motifs found in nonribosomal peptide synthetases are located.
		High-molecular-weight protein 2 of Yersinia enterocolitica is homologous to AngR of Vibrio anguillarum and belongs to a family of proteins involved in nonribosomal peptide synthesis.
		Modular structure of genes encoding multifunctional peptide synthetases required for nonribosomal peptide synthesis.
	iai.asm.org /cgi/content/full/67/12/6496 (9475 words)

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