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Die Imidazolglycerinphosphat-Synthase aus Thermotoga maritima: Struktur, Regulation und Evolution einer Glutaminamidotransferase

URN to cite this document: urn:nbn:de:bvb:355-epub-127746

List, Felix (2011) Die Imidazolglycerinphosphat-Synthase aus Thermotoga maritima: Struktur, Regulation und Evolution einer Glutaminamidotransferase. PhD, Universität Regensburg

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Abstract (German)

Die vorliegende Arbeit beschäftigte sich mit der Struktur, Funktion und Evolution von Glutaminamidotransferasen (GATasen). Vertreter dieser Enzymfamilie sind für den Einbau von Stickstoff innerhalb der Biosynthesewege von Nukleotiden, Aminosäuren, Coenzymen und Antibiotika verantwortlich. Bei allen GATasen wird am aktiven Zentrum einer Glutaminase durch die Hydrolyse von Glutamin Ammoniak ...

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Translation of the abstract (English)

The bi-enzyme complex imidazole glycerol phosphate synthase (ImGP-S) belongs to the family of glutamine amidotransferases (GATases). GATases exert a key role in nitrogen incorporation into numerous metabolic intermediates. ImGP-S consists of a synthase and a glutaminase subunit. The ImGP glutaminase HisH generates ammonia by hydrolyzing glutamine, which reacts at the active site of the synthase ...

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Item Type:Thesis of the University of Regensburg (PhD)
Date:16 February 2011
Referee:Prof. Dr. Reinhard Sterner
Date of exam:4 February 2010
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
Interdisciplinary Subject Network:Not selected
Keywords:allosterische Kontrolle, Ammoniakkanal, Histidin Biosynthese, Tryptophan Biosynthese, allosteric mechanism, ammonia chanel, histidine biosynthesis, tryptophan biosynthesis
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Deposited On:16 Feb 2011 10:21
Last Modified:13 Mar 2014 16:52
Item ID:12774
Owner Only: item control page

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