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Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity.

Schneider, Birgit, Knöchel, Thorsten, Darimont, Beatrice, Hennig, Michael, Dietrich, Susanne, Babinger, Karin, Kirschner, Kasper and Sterner, Reinhard (2005) Role of the N-terminal extension of the (betaalpha)8-barrel enzyme indole-3-glycerol phosphate synthase for its fold, stability, and catalytic activity. Biochemistry 44 (50), pp. 16405-12.

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Abstract

Indole-3-glycerol phosphate synthase (IGPS) catalyzes the fifth step in the biosynthesis of tryptophan. It belongs to the large and versatile family of (betaalpha)(8)-barrel enzymes but has an unusual N-terminal extension of about 40 residues. Limited proteolysis with trypsin of IGPS from both Sulfolobus solfataricus (sIGPS) and Thermotoga maritima (tIGPS) removes about 25 N-terminal residues and ...

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Item type:Article
Date:2005
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
16342933PubMed ID
10.1021/bi051640nDOI
Classification:
NotationType
Amino Acid SequenceMESH
Base SequenceMESH
BiopolymersMESH
CatalysisMESH
DNA PrimersMESH
Enzyme StabilityMESH
HydrolysisMESH
Indole-3-Glycerol-Phosphate Synthase/metabolismMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Protein FoldingMESH
Sequence Homology, Amino AcidMESH
Sulfolobus solfataricus/enzymologyMESH
Thermotoga maritima/enzymologyMESH
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:13676
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