RESEARCH PROGRESS IN MOLECULAR BIOLOGY OF PHENYLALANINE AMMONIA-LYASE(E.C.4.3.1.5)*
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L-phenylalanine is an important amino acid in commercial production of food industry and medicine nowaday. The biotransformations of trans-cinnamic acid to L-phenylalanine using phenylalanine ammonia- lyase(PAL) is in the front of research and development now.This article reviews the research progress in molecular biology of Phenylalanine ammonia-lyase (PAL) as an important enzyme for production of L-phenylalanine. Ref 43Keywords:
Phenylalanine ammonia-lyase
Cinnamic acid
Lyase
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Shikimic acid
Phosphofructokinase 2
Shikimate pathway
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MACROMOLECULESC-119 using the hanging drop technique.The precipitant conditions are 12% PEG8K 75mM MnS04, 100ml\II cacodylate pH 5.2.In order to obtain large single crystals, a temperature difference between the nucleation event and the growth event is essentiaL The space group of cholesterol oxidase is monoclinic P2 1 .The cell dimen~ons are a=77.6A,b=l25.7A,c=8L5A and f:\=109.1"with two molecules per asymmetric unit.X-ray data collection is carried out by flash-cooling the crystals to ll5K in a nitrogen stream.One heavy atom derivative has been obtained by soaking the crystals in 0.5mM K2Pt(CN)_,.Further screening for heavy atom derivatives is in progress.
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This chapter contains sections titled: Biosynthesis of phenylalanine, tyrosine and tryptophan Metabolism of phenylalanine and tyrosine Catabolism of phenylalanine and tyrosine Metabolism of tryptophan Quinone cofactors in amine oxidases Further reading
Phenylalanine hydroxylase
Catabolism
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Phenylalanine ammonia-lyase
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D-Amino acids are being increasingly used in the rational design of chiral drugs such as anti-cancer compounds and viral inhibitors. In common with the commercial manufacture of L-amino acids, both chemo-enzymatic resolution approaches and direct single isomer syntheses have been undertaken in the production of D-amino acids and their derivatives. We have developed a fermentation route to the synthesis of D-phenylalanine in Escherichia coli K12 using metabolic engineering. The key enzymes used in this system are a DAHP synthase and the chorismate mutase-prephenate dehydratase from E. coli in conjunction with an operon of D-amino acid aminotransferase (Bacillus sphaericus), L-amino acid deaminase (Proteus myxofaciens) and alanine racemase (Salmonella typhimurium). These enzymes form a pathway, which deregulates L-phenylalanine synthesis and subsequently converts the L-phenylalanine into its D-isomer. Due to the broad specificity of both the L-amino acid deaminase and the D-amino acid aminotransferase, this system, with slight modifications, can be used to synthesize a wide variety of D-amino acids.
Chorismate mutase
Metabolic Engineering
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Phenylalanine hydroxylase
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In addition to being a vital component of proteins, phenylalanine is also a precursor of numerous aromatic primary and secondary metabolites with broad physiological functions. In plants phenylalanine is synthesized predominantly via the arogenate pathway in plastids. Here, we describe the structure, molecular players and subcellular localization of a microbial-like phenylpyruvate pathway for phenylalanine biosynthesis in plants. Using a reverse genetic approach and metabolic flux analysis, we provide evidence that the cytosolic chorismate mutase is responsible for directing carbon flux towards cytosolic phenylalanine production via the phenylpyruvate pathway. We also show that an alternative transcription start site of a known plastidial enzyme produces a functional cytosolic prephenate dehydratase that catalyzes the conversion of prephenate to phenylpyruvate, the intermediate step between chorismate mutase and phenylpyruvate aminotransferase. Thus, our results complete elucidation of phenylalanine biosynthesis via phenylpyruvate in plants, showing that this pathway splits from the known plastidial arogenate pathway at chorismate, instead of prephenate as previously thought, and the complete pathway is localized in the cytosol.
Chorismate mutase
Metabolic pathway
Shikimate pathway
Phenylalanine hydroxylase
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Strain (injury)
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Hydroxylation
Metabolic Engineering
Shikimate pathway
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