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A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role.

Hettwer, Stefan and Sterner, Reinhard (2002) A novel tryptophan synthase beta-subunit from the hyperthermophile Thermotoga maritima. Quaternary structure, steady-state kinetics, and putative physiological role. The Journal of biological chemistry 277 (10), pp. 8194-201.

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Abstract

Tryptophan synthase catalyzes the last two steps in the biosynthesis of the amino acid tryptophan. The enzyme is an alpha beta beta alpha complex in mesophilic microorganisms. The alpha-subunit (TrpA) catalyzes the cleavage of indoleglycerol phosphate to glyceraldehyde 3-phosphate and indole, which is channeled to the active site of the associated beta-subunit (TrpB1), where it reacts with serine ...

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Item type:Article
Date:2002
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
11756459PubMed ID
10.1074/jbc.M111541200DOI
Classification:
NotationType
Amino Acid SequenceMESH
CatalysisMESH
Chromatography, GelMESH
Cloning, MolecularMESH
Escherichia coli/metabolismMESH
Glyceraldehyde-3-Phosphate Dehydrogenases/metabolismMESH
Hot TemperatureMESH
KineticsMESH
Models, BiologicalMESH
Models, ChemicalMESH
Models, MolecularMESH
Molecular Sequence DataMESH
PhylogenyMESH
Plasmids/metabolismMESH
Protein BindingMESH
Protein Structure, QuaternaryMESH
Protein Structure, TertiaryMESH
Sequence Homology, Amino AcidMESH
TemperatureMESH
Thermotoga maritima/enzymologyMESH
Time FactorsMESH
Tryptophan/chemistryMESH
Tryptophan Synthase/physiologyMESH
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:13694
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