Category:Complex:TYRB-DIMER
About
Description (originally from EcoCyc[1]) tyrosine aminotransferase
Comments (originally from EcoCyc[2]) This enzyme catalyzes the final reaction in the biosynthesis of both phenylalanine and tyrosine. Under normal physiological conditions phenylalanine and tyrosine synthesis are primarily carried out by the aromatic aminotransferase, the product of the tyrB gene. Only when the pool sizes of phenylpyruvate and 4-hydroxyphenylpyruvate become very high will the aspartate aminotransferase start to contribute to the synthesis of these two amino acids. [3][4][5][6][7][8][4][7][9][9][10][11][12][13][14][15].
References
- ↑ EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ Gelfand, DH & Steinberg, RA (1977) Escherichia coli mutants deficient in the aspartate and aromatic amino acid aminotransferases. J. Bacteriol. 130 429-40 PubMed
- ↑ 4.0 4.1 Collier, RH & Kohlhaw, G (1972) Nonidentity of the aspartate and the aromatic aminotransferase components of transaminase A in Escherichia coli. J. Bacteriol. 112 365-71 PubMed
- ↑ Houben, EN et al. (2005) Early encounters of a nascent membrane protein: specificity and timing of contacts inside and outside the ribosome. J. Cell Biol. 170 27-35 PubMed
- ↑ Mavrides, C & Orr, W (1975) Multispecific aspartate and aromatic amino acid aminotransferases in Escherichia coli. J. Biol. Chem. 250 4128-33 PubMed
- ↑ 7.0 7.1 Powell, JT & Morrison, JF (1978) Role of the Escherichia coli aromatic amino acid aminotransferase in leucine biosynthesis. J. Bacteriol. 136 1-4 PubMed
- ↑ Hayashi, H et al. (1993) Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase. Biochemistry 32 12229-39 PubMed
- ↑ 9.0 9.1 Vartak, NB et al. (1991) A functional leuABCD operon is required for leucine synthesis by the tyrosine-repressible transaminase in Escherichia coli K-12. J. Bacteriol. 173 3864-71 PubMed
- ↑ Islam, MM et al. (2000) The substrate activation process in the catalytic reaction of Escherichia coli aromatic amino acid aminotransferase. Biochemistry 39 15418-28 PubMed
- ↑ Iwasaki, M et al. (1994) Protonation state of the active-site Schiff base of aromatic amino acid aminotransferase: modulation by binding of ligands and implications for its role in catalysis. J. Biochem. 115 156-61 PubMed
- ↑ Onuffer, JJ et al. (1995) The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases. Protein Sci. 4 1743-9 PubMed
- ↑ Hayashi, H et al. (1996) Analysis of the substrate-recognition mode of aromatic amino acid aminotransferase by combined use of quasisubstrates and site-directed mutagenesis: systematic hydroxy-group addition/deletion studies to probe the enzyme-substrate interactions. Biochemistry 35 6754-61 PubMed
- ↑ Powell, JT & Morrison, JF (1978) The purification and properties of the aspartate aminotransferase and aromatic-amino-acid aminotransferase from Escherichia coli. Eur. J. Biochem. 87 391-400 PubMed
- ↑ Ko, TP et al. (1999) Crystallization and preliminary crystallographic analysis of the Escherichia coli tyrosine aminotransferase. Acta Crystallogr. D Biol. Crystallogr. 55 1474-7 PubMed
This category currently contains no pages or media.
