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Submission declined on 25 May 2023 by Dan arndt (talk). This draft's references do not show that the subject qualifies for a Wikipedia article. In summary, the draft needs multiple published sources that are: Declined by Dan arndt 15 months ago.
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Methionylglutaminylarginyltyrosylglutamylserylleucylphenylalanylalanylglutaminylleucyllysylglutanylarginyllysylglutamylglysylalanylphenylalanylvalylprolylphenylalanylyalylthreonylleucylglcycylaspartylprolylglicylisoleucyglutamylglutamimlserylleucyllysylisoleucylaspartylthreonylleucylisoleucylglutamylalanylglyclyalanylaspartylalanylleucyglutamylleucylgluycylisoleucylproluylphenylalanyserylaspartyprolylleucelalanylaspartylglycylprolylthreonylisolleucyglutaminylasparagimylalanythreonylleucylarginylalanylphenylalanylalanylalanylglycylvalylthreonylprolylalanylglutaminylcysteinylphenylalanylglglutamylmthionylleucalanylleucylisoleucylarginylglutaninyllysylhistidylpooyuthreonyoisoleucylprolylisoleuclglycylleucylleucylmethiolnyltyrosylalanylasbaraginylleucylvalylphenylalanylsparaginyyllysylglycylisoleucylaspartylglutamylphenylalanylyltyrosylalanylglutaminylcysteinylglutamyllysylvalylglycylvalylspartylserylvalylleucylvallalanylaspartylvalylprolylvalvlglutaminylglutamylserylalanylprolyiphenylalalrginylglutaminylalanylalanylleucylarginylhistidylasparaginylvalylalalprlylisoleucylphenylalanylisoleucylcysteinylprolyprolylaspartylalanylaspartyspartyleucylleucylarginylglutaminylisoleucylalanylseryltyroslglycylarginylglycyltyrosylthreonyltyrosylleucylleucylserylarginlalanylglycylvalylthreonylglycylalanylglutamylasparaginylarginylanylalanylleucylprolylleucylaspaaginylhitidylleucylvalylalanyllysylleucyllysylglutamyltyrosylasparagimylalanylalanyprolylprolylleucylglutaminylglycyphenlalanylglycylisoleyucylserylalanylprolylaspartymgmutaminylvalyllysylalanylalanylisoleucylalspartylalanylglycylalanylalanylglycylalanylasoleucylserylglycylserylalanylisoleucylbalyllysylisoleucylisoleucylglutamylglutaminylhistidylasparaginlisoleucylglutamylpronylgluotamyllysylmethionylluecylalanylalanyoeucyllysylvalylphenylalanlvalylglutamilylprolylmethionyllysylalanylalanylthreonylarginylserine. is the chemical name for the tryptophan synthase alpha subunit of Escherichia coli (E. coli). It is an essential enzyme involved in the biosynthesis of the amino acid tryptophan, a building block of proteins. TrpA is part of a heteromeric complex known as tryptophan synthase, which also includes the beta subunit encoded by the trpB gene.
English
editPronunciation: Methionylglutaminylarginyltyrosylglutamylserylleucylphenylalanylalanylglutaminylleucyllysylglutanylarginyllysylglutamylglysylalanylphenylalanylvalylprolylphenylalanylyalylthreonylleucylglcycylaspartylprolylglicylisoleucyglutamylglutamimlserylleucyllysylisoleucylaspartylthreonylleucylisoleucylglutamylalanylglyclyalanylaspartylalanylleucyglutamylleucylgluycylisoleucylproluylphenylalanyserylaspartyprolylleucelalanylaspartylglycylprolylthreonylisolleucyglutaminylasparagimylalanythreonylleucylarginylalanylphenylalanylalanylalanylglycylvalylthreonylprolylalanylglutaminylcysteinylphenylalanylglglutamylmthionylleucalanylleucylisoleucylarginylglutaninyllysylhistidylpooyuthreonyoisoleucylprolylisoleuclglycylleucylleucylmethiolnyltyrosylalanylasbaraginylleucylvalylphenylalanylsparaginyyllysylglycylisoleucylaspartylglutamylphenylalanylyltyrosylalanylglutaminylcysteinylglutamyllysylvalylglycylvalylspartylserylvalylleucylvallalanylaspartylvalylprolylvalvlglutaminylglutamylserylalanylprolyiphenylalalrginylglutaminylalanylalanylleucylarginylhistidylasparaginylvalylalalprlylisoleucylphenylalanylisoleucylcysteinylprolyprolylaspartylalanylaspartyspartyleucylleucylarginylglutaminylisoleucylalanylseryltyroslglycylarginylglycyltyrosylthreonyltyrosylleucylleucylserylarginlalanylglycylvalylthreonylglycylalanylglutamylasparaginylarginylanylalanylleucylprolylleucylaspaaginylhitidylleucylvalylalanyllysylleucyllysylglutamyltyrosylasparagimylalanylalanyprolylprolylleucylglutaminylglycyphenlalanylglycylisoleyucylserylalanylprolylaspartymgmutaminylvalyllysylalanylalanylisoleucylalspartylalanylglycylalanylalanylglycylalanylasoleucylserylglycylserylalanylisoleucylbalyllysylisoleucylisoleucylglutamylglutaminylhistidylasparaginlisoleucylglutamylpronylgluotamyllysylmethionylluecylalanylalanyoeucyllysylvalylphenylalanlvalylglutamilylprolylmethionyllysylalanylalanylthreonylarginylserine.
Structure and Function
editE. coli TrpA is a multifunctional protein with a molecular weight of approximately 27 kilodaltons. It is composed of 268 amino acids and is encoded by the trpA gene located on the bacterial chromosome. The protein consists of several distinct domains that contribute to its various functions.
The primary role of TrpA is to catalyze the conversion of indole-3-glycerol phosphate and L-serine to indole, glyceraldehyde 3-phosphate, and water. This reaction represents the first step in the tryptophan biosynthetic pathway. TrpA possesses both pyridoxal phosphate (PLP) binding and catalytic domains, which are essential for its enzymatic activity.
Regulation
editThe expression of the trpA gene and subsequent synthesis of TrpA is tightly regulated in E. coli. The availability of tryptophan in the cellular environment plays a critical role in this regulation. When tryptophan levels are high, it acts as a corepressor by binding to the trp repressor protein, resulting in the repression of trpA gene expression.
Under conditions of tryptophan limitation, the trp repressor is unable to bind to the trp operator region, allowing RNA polymerase to transcribe the trpA gene. This mechanism ensures that the E. coli cell produces tryptophan synthase only when tryptophan is scarce.
Importance in Biological Systems
editTryptophan synthase is a vital enzyme in both prokaryotic and eukaryotic organisms as it enables the de novo biosynthesis of tryptophan, an essential amino acid. Tryptophan serves as a precursor for various important molecules, including neurotransmitters, metabolites, and cofactors.
In E. coli, TrpA plays a crucial role in maintaining cellular homeostasis by regulating tryptophan levels. It contributes to the overall metabolic balance and ensures an adequate supply of tryptophan for protein synthesis and other cellular processes.
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