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In the experiment, an extract was prepared from bacterial cells that could make protein without the presence of intact living cells. An artificial form of RNA consisting entirely of uracil-containing nucleotides (polyuridylic acid or poly-U) was added to the extract, causing it to form a protein composed entirely of the amino acid phenylalanine.
Phenylalanine ball and stick model spinning. Phenylalanine (symbol Phe or F) [3] is an essential α-amino acid with the formula C 9 H 11 NO 2.It can be viewed as a benzyl group substituted for the methyl group of alanine, or a phenyl group in place of a terminal hydrogen of alanine.
The Erlenmeyer–Plöchl azlactone and amino acid synthesis, named after Friedrich Gustav Carl Emil Erlenmeyer who partly discovered the reaction, is a series of chemical reactions which transform an N-acyl glycine to various other amino acids via an oxazolone (also known as an azlactone).
Thus, the two substrates of this enzyme are L-phenylalanine and pyruvate, whereas its two products are phenylpyruvate and L-alanine. This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-phenylalanine:pyruvate aminotransferase.
The process is similar to that of bacterial termination, but unlike bacterial termination, there is a universal release factor, eRF1, that recognizes all three stop codons. Upon termination, the ribosome is disassembled and the completed polypeptide is released. eRF3 is a ribosome-dependent GTPase that helps eRF1 release the completed polypeptide.
Phenylalanine, tyrosine, and tryptophan, the aromatic amino acids, arise from chorismate. The first step, condensation of 3-deoxy-D-arabino-heptulosonic acid 7-phosphate (DAHP) from PEP/E4P, uses three isoenzymes AroF, AroG, and AroH. Each one of these has its synthesis regulated from tyrosine, phenylalanine, and tryptophan, respectively.
Phenylalanine-tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS (Aminoacyl-tRNA synthetase) family. Bacterial and mitochondrial PheRSs share a ferredoxin -fold anticodon binding (FDX-ACB) domain , which represents a canonical double split alpha+beta motif having no insertions.
Fumarylacetoacetate hydrolase (FAH) is a protein homodimer which cleaves fumarylacetoacetate at its carbon-carbon bond during a hydrolysis reaction. [8] As a critical enzyme in phenylalanine and tyrosine metabolism, 4-Fumarylacetoacetate hydrolase catalyzes the final step in the catabolism of 4-fumarylacetoacetate and water into acetoacetate, fumarate, and H + respectively. [9]