CGTase cyclodextrin glycosyltransferase HisA ProFAR isomerase HisF imidazole glycerol phosphate synthase TIM triosephosphate isomerase TrpC indole glycerol phosphate synthase TrpF phosphoribosylanthranilate isomerase
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چکیده
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 structural subdomain.
منابع مشابه
Cloning and sequencing analysis of Trp1 gene of Flammulina velutipes.
The genomic TRP1 gene from basidiomycete Flammulina velutipes was cloned by complementation of yeast Saccharomyces cerevisiae trp1 mutation. Sequencing analysis revealed that the TRP1 gene encoded a single protein consisting of three catalytic functional domains; glutamine amidotransferase, indole-3-glycerol phosphate synthase ) and N-(5'-phosphoribosyl) anthranilate isomerase, in order of NH2-...
متن کاملAn evolutionary comparison of Acinetobacter calcoaceticus trpF with trpF genes of several organisms.
The deduced amino acid sequence of Acinetobacter calcoaceticus N-(5'-phosphoribosyl) anthranilate isomerase (PRAI), which is coded by trpF, was compared with TrpF of Caulobacter crescentus, Escherichia coli, Bacillus subtilis, Saccharomyces cerevisiae, Neurospora crassa, and Aspergillus nidulans. Sixty percent of identical or similar amino acids were located in alpha/beta TIM (triose-phosphate ...
متن کاملDirected evolution of a (ba)8-barrel enzyme to catalyze related reactions in two different metabolic pathways
Enzymes participating in different metabolic pathways often have similar catalytic mechanisms and structures, suggesting their evolution from a common ancestral precursor enzyme. We sought to create a precursor-like enzyme for N*-[(5*-phosphoribosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (ProFAR) isomerase (HisA; EC 5.3.1.16) and phosphoribosylanthranilate (PRA) isomerase (Trp...
متن کاملMimicking enzyme evolution by generating new ( )8-barrels from ( )4-half-barrels
Gene duplication and fusion events that multiply and link functional protein domains are crucial mechanisms of enzyme evolution. The analysis of amino acid sequences and three-dimensional structures suggested that the ( )8-barrel, which is the most frequent fold among enzymes, has evolved by the duplication, fusion, and mixing of ( )4-half-barrel domains. Here, we mimicked this evolutionary str...
متن کاملRoles of triosephosphate isomerase and aerobic metabolism in Trypanosoma brucei.
Kinetoplastid protozoa compartmentalize the first seven enzymes of glycolysis and two enzymes of glycerol metabolism in a microbody, the glycosome. While in its mammalian host, Trypanosoma brucei depends entirely on glucose for ATP generation. Under aerobic conditions, most of the glucose is metabolized to pyruvate. Aerobic metabolism depends on the activities of glycosomal triosephosphate isom...
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