Imidazole Glycerol Phosphate Synthase fromThermotoga maritima
نویسندگان
چکیده
منابع مشابه
Allosteric pathways in imidazole glycerol phosphate synthase.
Protein allosteric pathways are investigated in the imidazole glycerol phosphate synthase heterodimer in an effort to elucidate how the effector (PRFAR, N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide) activates glutaminase catalysis at a distance of 25 Å from the glutamine-binding site. We apply solution NMR techniques and community analysis of dynamical netwo...
متن کاملCGTase cyclodextrin glycosyltransferase HisA ProFAR isomerase HisF imidazole glycerol phosphate synthase TIM triosephosphate isomerase TrpC indole glycerol phosphate synthase TrpF phosphoribosylanthranilate isomerase
The (βα)8-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (βα)8-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to interconvert catalytic activities or substrate specificities by rational design or directed evolution. Recently, the (βα)4-half-barrel was identified as a possible st...
متن کاملSubunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase.
A selection strategy has been developed to identify amino acid residues involved in subunit interactions that coordinate the two half-reactions catalyzed by glutamine amidotransferases. The protein structures known for this class of enzymes have revealed that ammonia is shuttled over long distances and that each amidotransferase evolved different molecular tunnels for this purpose. The heterodi...
متن کاملGlutamine Hydrolysis by Imidazole Glycerol Phosphate Synthase Displays Temperature Dependent Allosteric Activation
The enzyme imidazole glycerol phosphate synthase (IGPS) is a model for studies of long-range allosteric regulation in enzymes. Binding of the allosteric effector ligand N'-[5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide-ribonucleotide (PRFAR) stimulates millisecond (ms) timescale motions in IGPS that enhance its catalytic function. We studied the effect of temperature on these cr...
متن کاملTHE BIOSYNTHESIS OF HISTIDINE : n-erythro-IMIDAZOLE- GLYCEROL PHOSPHATE DEHYDRASE
Reaction 2 is catalyzed by the enzyme imidazoleacetol phosphate transaminase (1). Reaction 3 is catalyzed by the enzyme L-histidinol phosphate phosphatase (2). Reaction 4 is catalyzed by the enzyme L-histidinol dehydrogenase (3, 4). This report is concerned with the purification and description of the enzyme from N. crassa catalyzing Reaction 1, the dehydration of D-erythroimidazoleglycerol pho...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2001
ISSN: 0021-9258
DOI: 10.1074/jbc.m102012200