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Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex.

Beismann-Driemeyer, Silke and Sterner, Reinhard (2001) Imidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex. The Journal of biological chemistry 276 (23), pp. 20387-96.

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Abstract

Imidazole glycerol phosphate synthase, which links histidine and de novo purine biosynthesis, is a member of the glutamine amidotransferase family. In bacteria, imidazole glycerol phosphate synthase constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Nascent ammonia produced by HisH reacts at the active site of HisF with ...

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Item Type:Article
Date:2001
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Identification Number:
ValueType
11264293PubMed ID
10.1074/jbc.M102012200DOI
Classification:
NotationType
Amino Acid SequenceMESH
Aminohydrolases/metabolismMESH
Base SequenceMESH
Binding SitesMESH
CatalysisMESH
DNA PrimersMESH
KineticsMESH
Molecular Sequence DataMESH
Protein Structure, QuaternaryMESH
Thermotoga maritima/enzymologyMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Owner: Universitätsbibliothek Regensburg
Deposited On:22 Mar 2010 08:48
Last Modified:22 Mar 2010 08:48
Item ID:13699
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