Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: BMC Evolutionary Biology
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Annu Rev Plant Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Curr. Opin. Plant Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: J Gen Virol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: BMC Plant Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Kluwer Academic Publishers
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Comprehensive Natural Products II
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Methods Mol Biol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Biol. Chem.
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (2)
- Erscheinungsjahr
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- Phytochemistry (12)
- 0 (11)
- Plant Physiol. (11)
- Plant J. (8)
- PLOS ONE (7)
- FEBS Lett. (5)
- Front. Plant Sci. (4)
- Methods Mol. Biol. (4)
- New Phytol. (4)
- Trends Plant Sci. (4)
- Curr. Opin. Plant Biol. (3)
- EMBO J. (3)
- Plant Cell (3)
- Plant Cell Physiol. (3)
- Plant Signal Behav. (3)
- Proc. Natl. Acad. Sci. U.S.A. (3)
- bioRxiv (3)
- Annu. Rev. Plant Biol. (2)
- Biol. Chem. (2)
- J. Biol. Chem. (2)
- Mol. Plant (2)
- Nat. Plants (2)
- Nucleic Acids Res. (2)
- Physiol. Plant. (2)
- Planta (2)
- RNA Biol. (2)
- eLife (2)
- Annu. Plant Rev. (1)
- Annu. Rev. Microbiol. (1)
- Annu. Rev. Phytopathol. (1)
- BIOspektrum (1)
- BMC Genomics (1)
- BMC Plant Biol. (1)
- Biocell (1)
- Biologie in unserer Zeit (1)
- Biology of Plant-Microbe Interactions (1)
- Bot. Acta (1)
- Braz. J. Plant Physiol. (1)
- Cell (1)
- Cell Rep. (1)
- Cereal Res. Commun. (1)
- ChemRxiv (1)
- Cold Spring Harb. Perspect. Biol. (1)
- Electron. J. Biotechnol. (1)
- Environ. Sci. Pollut. Res. (1)
- Equine Vet. Educ. (1)
- Eur. J. Plant Pathol. (1)
- Front Cell Dev Biol (1)
- Gene (1)
- Int. J. Mol. Sci. (1)
- J. Agr. Food Chem. (1)
- J. Chromatogr. A (1)
- J. Exp. Bot. (1)
- J. Mol. Biol. (1)
- J. Plant Growth Regul. (1)
- J. Plant Physiol. (1)
- Methods Cell Biol. (1)
- Methods Enzymol. (1)
- Mol. Biol. Evol. (1)
- Nat. Chem. Biol. (1)
- Nat. Commun. (1)
- Pharmazie (1)
- Plant Cell Rep. (1)
- Plant Growth Regul. (1)
- Plant Mol. Biol. Rep. (1)
- Redox Biol. (1)
- Sci. Rep. (1)
- Skin Pharmacol. Physiol. (1)
- The Plant Cytoskeleton (1)
- Theor. Appl. Genet. (1)
- Trop. Plant Biol. (1)
- Virus Genes (1)
- Virus Res. (1)
- Viruses (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Wasternack, C. (2)
- Demuth, H.-U. (1)
- Hoffmann, T. (1)
- Ludwig, H.-H. (1)
- Manhart, S. (1)
- Miersch, O. (1)
- Schilling, S. (1)
Zeige Ergebnisse 1 bis 2 von 2.
Schilling, S.; Manhart, S.; Hoffmann, T.; Ludwig, H.-H.; Wasternack, C.; Demuth, H.-U.; Substrate Specificity of Glutaminyl Cyclases from Plants and Animals Biol. Chem. 384, 1583-1592, (2003) DOI: 10.1515/BC.2003.175
Glutaminyl cyclases (QC) catalyze the intramolecular cyclization of N-terminal glutamine residues of peptides and proteins. For a comparison of the substrate specificity of human and papaya QC enzymes, a novel continuous assay was established by adapting an existing discontinuous method. Specificity constants (kcat/Km) of dipeptides and dipeptide surrogates were higher for plant QC, whereas the selectivity for oligopeptides was similar for both enzymes. However, only the specificity constants of mammalian QC were dependent on size and composition of the substrates. Specificity constants of both enzymes were equally pH-dependent in the acidic pH-region, revealing a pKa value identical to the pKa of the substrate, suggesting similarities in the substrate conversion mode. Accordingly, both QCs converted the L-?homoglutaminyl residue in the peptide H-?homoGln-Phe-Lys-Arg-Leu-Ala-NH2 and the glutaminyl residues of the branched peptide H-Gln-Lys(Gln)-Arg-Leu-Ala-NH2 as well as the partially cyclized peptide H-Gln-cyclo( N?-Lys-Arg-Pro-Ala-Gly-Phe). In contrast, only QC from C. papaya was able to cyclize a methylated glutamine residue, while this compound did not even inhibit human QC-catalysis, suggesting distinct substrate recognition pattern. The conversion of the potential physiological substrates gastrin, neurotensin and [GlN1]-fertilization promoting peptide indicates that human QC may play a key role in posttranslational modification of most if not all pGlu-containing hormones.
Miersch, O.; Wasternack, C.; Octadecanoid and Jasmonate Signaling in Tomato (Lycopersicon esculentum Mill.) Leaves: Endogenous Jasmonates Do Not Induce Jasmonate Biosynthesis Biol. Chem. 381, 715-722, (2000) DOI: 10.1515/BC.2000.092
Jasmonates and their precursors, the octadecanoids, are signals in stress-induced alteration of gene expression. Several mRNAs coding for enzymes of jasmonic acid (JA) biosynthesis are up-regulated upon JA treatment or endogenous increase of the JA level. Here we investigated the positive feedback of endogenous JA on JA formation, as well as its β-oxidation steps. JA-responsive gene expression was recorded in terms of proteinase inhibitor2 (pin2) mRNA accumulation. JA formed upon treatment of tomato (Lycopersicon esculentum cv. Moneymaker) leaves with JA derivatives carrying different lengths of the carboxylic acid side chain was quantified by gas chromatography-mass spectrometry (GC-MS). The data revealed that β-oxidation of the side chain occurs up to a butyric acid moiety. The amount of JA formed from side-chain modified JA derivatives correlated with pin2-mRNA accumulation. JA derivatives with a carboxylic side chain of 3, 5 or 7 carbon atoms were unable to form JA and to express on pin2, whereas evennumbered derivatives were active.After treatment of tomato leaves with (10-2H)-(–)-12-oxophytoenoic acid, (4-2H)-(–)-JA and its methyl ester were formed and could be quantified separately from the endogenously nonlabeled JA pool by GC-MS analysis via isotopic discrimination. The level of 8 nmol per g fresh weight JA and its methyl ester originated exclusively from labeled 12-oxophytoenic acid. This and further data indicate that endogenous synthesis of the JA precursor 12-oxophytodienoic acid, as well as of JA and its methyl ester, are not induced in tomato leaves, suggesting that positive feedback in JA biosynthesis does not function in vivo.