Publikationen - Molekulare Signalverarbeitung
Aktive Filter
Autor Nach Häufigkeit alphabetisch sortiert: Monostori, T
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C
Autor Nach Häufigkeit alphabetisch sortiert: Sharma, V.K
Autor Nach Häufigkeit alphabetisch sortiert: Maucher, H
Autor Nach Häufigkeit alphabetisch sortiert: Wasternack, C.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: New Biotechnology
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Trends in Plant Sci.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Plant Cell Rep
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Chembiochem.
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: New Biotechnol
Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert: Biochemistry
Alle Filter entfernen
Suchfilter
- Typ der Publikation
- Publikation (1)
- Erscheinungsjahr
- 2002 (1)
- Journal / Buchreihe / Preprint-Server Nach Häufigkeit alphabetisch sortiert
- 0 (15)
- Phytochemistry (14)
- Plant Physiol. (9)
- FEBS Lett. (8)
- Planta (8)
- J. Plant Physiol. (6)
- Plant Cell (6)
- Biol. Chem. (5)
- J. Biol. Chem. (5)
- J. Exp. Bot. (5)
- New Phytol. (5)
- Plant Cell Physiol. (5)
- Plant J. (5)
- Trends Plant Sci. (5)
- Ann. Bot. (3)
- Bot. Acta (3)
- Plant Mol. Biol. (3)
- Plant Signal Behav. (3)
- Annu. Rev. Plant Biol. (2)
- Biochem. Soc. Trans. (2)
- Biologie in unserer Zeit (2)
- Fett/Lipid (2)
- J. Plant Growth Regul. (2)
- Nat. Plants (2)
- New Biotechnol. (2)
- Plant Biol. (2)
- ACS Chem. Biol. (1)
- Acta Biol. Szeged. (1)
- Acta Physiol. Plant. (1)
- Anal. Biochem. (1)
- Annu. Plant Rev. (1)
- BBA-Mol. Cell Biol. Lipids (1)
- BIOspektrum (1)
- Biochemistry (1)
- Biochimie (1)
- Biotechnol. Adv. (1)
- Cereal Res. Commun. (1)
- ChemBioChem (1)
- ChemRxiv (1)
- Chromatographia (1)
- Curr. Opin. Plant Biol. (1)
- Eur. J. Biochem. (1)
- Eur. J. Plant Pathol. (1)
- Int. J. Mol. Sci. (1)
- J. Chromatogr. A (1)
- J. Integr. Plant Biol. (1)
- Jap. Soc. Chem. Regul Plants, Abstr. (1)
- Mol. Plant (1)
- Mol. Plant Microbe Interact. (1)
- Nat. Chem. Biol. (1)
- Nova Acta Leopoldina (1)
- PLOS ONE (1)
- Physiol. Plant. (1)
- Phytomedicine (1)
- Plant Cell Environ. (1)
- Plant Cell Rep. (1)
- Plant Growth Regul. (1)
- Plants (1)
- Proc. Natl. Acad. Sci. U.S.A. (1)
- Prog. Nucleic Acid Res. Mol. Biol. (1)
- Science (1)
- Tetrahedron (1)
- Z. Naturforsch. C (1)
- Autor Nach Häufigkeit alphabetisch sortiert
- Demuth, H.-U. (1)
- Hoffmann, T. (1)
- Manhart, S. (1)
- Rosche, F. (1)
- Schilling, S. (1)
- Wasternack, C. (1)
Zeige Ergebnisse 1 bis 1 von 1.
Schilling, S.; Hoffmann, T.; Rosche, F.; Manhart, S.; Wasternack, C.; Demuth, H.-U.; Heterologous Expression and Characterization of Human Glutaminyl Cyclase: Evidence for a Disulfide Bond with Importance for Catalytic Activity Biochemistry 41, 10849-10857, (2002) DOI: 10.1021/bi0260381
Glutaminyl cyclase (QC, EC 2.3.2.5) catalyzes the formation of pyroglutamate residues from glutamine at the N-terminus of peptides and proteins. In the current study, human QC was functionally expressed in the secretory pathway of Pichia pastoris, yielding milligram quantities after purification from the supernatant of a 5 L fermentation. Initial characterization studies of the recombinant QC using MALDI-TOF mass spectrometry revealed correct proteolytic processing and N-glycosylation at both potential sites with similar 2 kDa extensions. CD spectral analysis indicated a high α-helical content, which contrasts with plant QC from Carica papaya. The kinetic parameters for conversion of H-Gln-Tyr-Ala-OH by recombinant human QC were almost identical to those previously reported for purified bovine pituitary QC. However, the results obtained for conversion of H-Gln-Gln-OH, H-Gln-NH2, and H-Gln-AMC were found to be contradictory to previous studies on human QC expressed intracellularly in E. coli. Expression of QC in E. coli showed that approximately 50% of the protein did not contain a disulfide bond that is present in the entire QC expressed in P. pastoris. Further, the enzyme was consistently inactivated by treatment with 15 mM DTT, whereas deglycosylation had no effect on enzymatic activity. Analysis of the fluorescence spectra of the native, reduced, and unfolded human QC point to a conformational change of the protein upon treatment with DTT. In terms of the different enzymatic properties, the consequences of QC expression in different environments are discussed.