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Analysis of complex stability and allosteric interaction in the imidazole glycerol phosphate synthase complex

Holinski, Alexandra (2017) Analysis of complex stability and allosteric interaction in the imidazole glycerol phosphate synthase complex. PhD, Universität Regensburg.

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Date of publication of this fulltext: 04 Apr 2017 08:08

Abstract (German)

Imidazole glycerol phosphate synthase (ImGPS) is a bi-enzyme complex that consists of the glutaminase subunit HisH and the cyclase subunit HisF. HisH hydrolyzes glutamine to glutamate and ammonia, which is transported through a channel to the active site of HisF where it reacts with N´-[(5´-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) to imidazole glycerol ...

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Translation of the abstract (German)

Die Imidazolglycerolphosphat-Synthase (ImGPS) ist ein Bienzymkomplex, der aus der Glutaminase-Untereinheit HisH und der Zyklase-Untereinheit HisF besteht. HisH hydrolisiert Glutamin zu Glutamat und Ammoniak, das durch einen intermolekularen Kanal zum aktiven Zentrum von HisF diffundiert und dort mit [(5‘Phosphoribulosyl)formimino]-5-aminoimidazol-4-carboxamid-Ribonukleotid (PRFAR) zu ...

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Item type:Thesis of the University of Regensburg (PhD)
Date:4 April 2017
Referee:Prof. Dr. Reinhard Sterner
Date of exam:17 March 2017
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie
Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Reinhard Sterner
Keywords:Imidazole glycerol phosphate synthase, protein-protein interaction, allostery, ancestral sequence reconstruction
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:35507
Owner only: item control page

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