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Journal articles on the topic 'Tyrosine phenol-lyase'

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Published: 4 June 2021

Last updated: 5 February 2022

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1

Do, Quang, Giang T. Nguyen, and Robert S. Phillips. "Inhibition of tyrosine phenol-lyase by tyrosine homologues." Amino Acids 48, no. 9 (2016): 2243–51. http://dx.doi.org/10.1007/s00726-016-2263-7.

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2

Phillips, Robert S., Krishamurthy Ravichandran, and Robert L. Von Tersch. "Synthesis of l-tyrosine from phenol and catalysed by tyrosine phenol-lyase." Enzyme and Microbial Technology 11, no. 2 (1989): 80–83. http://dx.doi.org/10.1016/0141-0229(89)90064-1.

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3

Antson, Alfred A., Tatyana V. Demidkina, Paul Gollnick, et al. "Three-dimensional structure of tyrosine phenol-lyase." Biochemistry 32, no. 16 (1993): 4195–206. http://dx.doi.org/10.1021/bi00067a006.

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4

Antson, A., G. Dodson, K. Wilson, and T. Demidkina. "Elucidating the mechanism of tyrosine phenol-lyase." Acta Crystallographica Section A Foundations of Crystallography 52, a1 (1996): C119. http://dx.doi.org/10.1107/s0108767396094391.

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5

Wierckx, Nick J. P., Hendrik Ballerstedt, Jan A. M. de Bont, Johannes H. de Winde, Harald J. Ruijssenaars, and Jan Wery. "Transcriptome Analysis of a Phenol-Producing Pseudomonas putida S12 Construct: Genetic and Physiological Basis for Improved Production." Journal of Bacteriology 190, no. 8 (2007): 2822–30. http://dx.doi.org/10.1128/jb.01379-07.

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ABSTRACT The unknown genetic basis for improved phenol production by a recombinant Pseudomonas putida S12 derivative bearing the tpl (tyrosine-phenol lyase) gene was investigated via comparative transcriptomics, nucleotide sequence analysis, and targeted gene disruption. We show upregulation of tyrosine biosynthetic genes and possibly decreased biosynthesis of tryptophan caused by a mutation in the trpE gene as the genetic basis for the enhanced phenol production. In addition, several genes in degradation routes connected to the tyrosine biosynthetic pathway were upregulated. This either may b

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6

Phillips, Robert S., Tatyana V. Demidkina, and Nicolai G. Faleev. "Structure and mechanism of tryptophan indole-lyase and tyrosine phenol-lyase." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1647, no. 1-2 (2003): 167–72. http://dx.doi.org/10.1016/s1570-9639(03)00089-x.

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7

Demidkina, T. Y., I. V. Myagkikh, A. A. Antson, and E. H. Harutyunyan. "Crystallization and crystal data on tyrosine phenol-lyase." FEBS Letters 232, no. 2 (1988): 381–82. http://dx.doi.org/10.1016/0014-5793(88)80774-9.

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8

Palcic, M. M., S. J. Shen, E. Schleicher, et al. "Stereochemistry and Mechanism of Reactions Catalyzed by Tyrosine Phenol-Lyase from Escherichia intermedia." Zeitschrift für Naturforschung C 42, no. 4 (1987): 307–18. http://dx.doi.org/10.1515/znc-1987-0401.

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Stereochemical studies on tyrosine phenol-lyase from Escherichia intermedia have shown that the α,β-elimination reactions of ʟ-serine and ᴅ- and ʟ-tyrosine proceed with retention of configuration at C-β. Stereospecifically (β-tritiated ʟ-serine is slowly racemized at C-β Deuterium from the α-position of ʟ-tyrosine is partially transferred to C-4 of the phenol formed when the α,β- elimination reaction is carried out in H2O, although no transfer of α-1H in 2H2O was seen. The result favors tautomerization of the p-hydroxyphenyl to a cyclohexadienonyl moiety prior to carbon-carbon bond cleavage.

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9

DEMIDKINA, Tatyana V., Igor V. MYAGKIKH, and Alexei V. AZHAYEV. "Transamination catalysed by tyrosine phenol-lyase from Citrobacter intermedius." European Journal of Biochemistry 170, no. 1-2 (1987): 311–16. http://dx.doi.org/10.1111/j.1432-1033.1987.tb13701.x.

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10

Suzuki, Hideyuki, Takane Katayama, Kenji Yamamoto, and Hidehiko Kumagai. "Transcriptional Regulation of Tyrosine Phenol-Lyase Gene ofErwinia herbicolaAJ2985." Bioscience, Biotechnology, and Biochemistry 59, no. 12 (1995): 2339–41. http://dx.doi.org/10.1271/bbb.59.2339.

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11

Kim, Sanggil, Bong Hyun Sung, Sun Chang Kim, and Hyun Soo Lee. "Genetic incorporation ofl-dihydroxyphenylalanine (DOPA) biosynthesized by a tyrosine phenol-lyase." Chemical Communications 54, no. 24 (2018): 3002–5. http://dx.doi.org/10.1039/c8cc00281a.

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l-Dihydroxyphenylalanine (DOPA) was biosynthesized by a tyrosine-phenol lyase from catechol, pyruvate, and ammonia inEscherichia coli, and the biosynthesized amino acid was directly incorporated into proteins.

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12

Phillips, Robert S., Tatyana V. Demidkina, Lyudmila N. Zakomirdina, Stefano Bruno, Luca Ronda, and Andrea Mozzarelli. "Crystals of Tryptophan Indole-Lyase and Tyrosine Phenol-Lyase Form Stable Quinonoid Complexes." Journal of Biological Chemistry 277, no. 24 (2002): 21592–97. http://dx.doi.org/10.1074/jbc.m200216200.

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13

Demidkina, T. V., A. A. Antson, N. G. Faleev, R. S. Phillips, and L. N. Zakomirdina. "Spatial structure and the mechanism of tyrosine phenol-lyase and tryptophan indole-lyase." Molecular Biology 43, no. 2 (2009): 269–83. http://dx.doi.org/10.1134/s0026893309020101.

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14

Xu, Sha, Yu Zhang, Youran Li, Xiaole Xia, Jingwen Zhou, and Guiyang Shi. "Production of L-tyrosine using tyrosine phenol-lyase by whole cell biotransformation approach." Enzyme and Microbial Technology 131 (December 2019): 109430. http://dx.doi.org/10.1016/j.enzmictec.2019.109430.

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15

Wierckx, Nick J. P., Hendrik Ballerstedt, Jan A. M. de Bont, and Jan Wery. "Engineering of Solvent-Tolerant Pseudomonas putida S12 for Bioproduction of Phenol from Glucose." Applied and Environmental Microbiology 71, no. 12 (2005): 8221–27. http://dx.doi.org/10.1128/aem.71.12.8221-8227.2005.

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ABSTRACT Efficient bioconversion of glucose to phenol via the central metabolite tyrosine was achieved in the solvent-tolerant strain Pseudomonas putida S12. The tpl gene from Pantoea agglomerans, encoding tyrosine phenol lyase, was introduced into P. putida S12 to enable phenol production. Tyrosine availability was a bottleneck for efficient production. The production host was optimized by overexpressing the aroF-1 gene, which codes for the first enzyme in the tyrosine biosynthetic pathway, and by random mutagenesis procedures involving selection with the toxic antimetabolites m-fluoro-dl-phe

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16

FALEEV, Nikolai G., Sergei B. RUVINOV, Tatyana V. DEMIDKINA, et al. "Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity." European Journal of Biochemistry 177, no. 2 (1988): 395–401. http://dx.doi.org/10.1111/j.1432-1033.1988.tb14388.x.

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17

Nagasawa, Toru, Takafumi Ishii, and Hideaki Yamada. "Location of tyrosine phenol-lyase in some Gram-negative bacteria." FEMS Microbiology Letters 30, no. 3 (1985): 269–72. http://dx.doi.org/10.1111/j.1574-6968.1985.tb01094.x.

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18

Chandel, Meenakshi, and Wamik Azmi. "Purification and Characterization of Tyrosine Phenol Lyase from Citrobacter freundii." Applied Biochemistry and Biotechnology 171, no. 8 (2013): 2040–52. http://dx.doi.org/10.1007/s12010-013-0491-9.

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19

Polak, Jacek, and Henry Brzeski. "Isolation of the tyrosine phenol lyase gene from Citrobacter freundii." Biotechnology Letters 12, no. 11 (1990): 805–10. http://dx.doi.org/10.1007/bf01022599.

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20

NAGASAWA, Toru, Takashi UTAGAWA, Joji GOTO, et al. "Syntheses of l-Tyrosine-Related Amino Acids by Tyrosine Phenol-lyase of Citrobacter intermedius." European Journal of Biochemistry 117, no. 1 (2005): 33–40. http://dx.doi.org/10.1111/j.1432-1033.1981.tb06299.x.

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21

Kim, Kyonghee, та Philip A. Cole. "Synthesis of (2S,3R)-β-methyltyrosine catalyzed by tyrosine phenol-lyase". Bioorganic & Medicinal Chemistry Letters 9, № 8 (1999): 1205–8. http://dx.doi.org/10.1016/s0960-894x(99)00162-6.

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22

Milić, D., D. Matković-Čalogović, T. T. Demidkina та A. A. Antson. "Structural details in the β-elimination mechanism of tyrosine phenol-lyase". Acta Crystallographica Section A Foundations of Crystallography 63, a1 (2007): s122. http://dx.doi.org/10.1107/s0108767307097346.

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23

Han, Hongmei, Weizhu Zeng, Guocheng Du, Jian Chen, and Jingwen Zhou. "Site-directed mutagenesis to improve the thermostability of tyrosine phenol-lyase." Journal of Biotechnology 310 (February 2020): 6–12. http://dx.doi.org/10.1016/j.jbiotec.2020.01.005.

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24

Faleev, Nicolai G., Olga V. Axenova, Tatyana V. Demidkina, and Robert S. Phillips. "The role of acidic dissociation of substrate's phenol group in the mechanism of tyrosine phenol-lyase." Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1647, no. 1-2 (2003): 260–65. http://dx.doi.org/10.1016/s1570-9639(03)00063-3.

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25

Watkins, E. Blake, and Robert S. Phillips. "Inhibition of Tyrosine Phenol-lyase fromCitrobacter freundiiby 2-Azatyrosine and 3-Azatyrosine†." Biochemistry 40, no. 49 (2001): 14862–68. http://dx.doi.org/10.1021/bi015707s.

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26

Azmi, Wamik, Ajay Kumar, and Varun Dev. "Paraffin as oxygen vector modulates tyrosine phenol lyase production byCitrobacter freundiiMTCC 2424." Acta Microbiologica et Immunologica Hungarica 60, no. 2 (2013): 145–54. http://dx.doi.org/10.1556/amicr.60.2013.2.5.

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27

Faleev, Nikolai G., Yurii N. Zhukov, Elena N. Khurs, et al. "Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids." European Journal of Biochemistry 267, no. 23 (2000): 6897–902. http://dx.doi.org/10.1046/j.1432-1033.2000.01794.x.

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28

Koralewska, Anna, Wojciech Augustyniak, Andrzej Temeriusz, and Marianna Kańska. "Effects of Cyclodextrin Derivatives on the Catalytic Activity of Tyrosine Phenol-Lyase." Journal of Inclusion Phenomena 49, no. 1/2 (2004): 193–97. http://dx.doi.org/10.1023/b:jiph.0000031135.42890.92.

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29

Kurusu, Yasurou, Makiko Fukushima, Keiko Kohama, et al. "Cloning and nucleotide sequencing of the tyrosine phenol lyase gene fromEscherichia intermedia." Biotechnology Letters 13, no. 11 (1991): 769–72. http://dx.doi.org/10.1007/bf01026756.

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30

Suzuki, Hideyuki, Kazuyo Nishihara, Naoki Usui, Hiroshi Matsui, and Hidehiko Kumagai. "Cloning and nucleotide sequence of Erwinia herbicola AJ2982 tyrosine phenol-lyase gene." Journal of Fermentation and Bioengineering 75, no. 2 (1993): 145–48. http://dx.doi.org/10.1016/0922-338x(93)90226-x.

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31

Zhu, Hang-Qin, Xiao-Ling Tang, Ren-Chao Zheng, and Yu-Guo Zheng. "Purification and Biochemical Characterization of a Tyrosine Phenol-lyase from Morganella morganii." Applied Biochemistry and Biotechnology 192, no. 1 (2020): 71–84. http://dx.doi.org/10.1007/s12010-020-03301-1.

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32

Mouratou, Barbara, Patrik Kasper, Heinz Gehring та Philipp Christen. "Conversion of Tyrosine Phenol-lyase to Dicarboxylic Amino Acid β-Lyase, an Enzyme Not Found in Nature". Journal of Biological Chemistry 274, № 3 (1999): 1320–25. http://dx.doi.org/10.1074/jbc.274.3.1320.

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33

DEMIDKINA, Tatyana V., Maria V. BARBOLINA, Nicolai G. FALEEV, Bakthavatsalam SUNDARARAJU, Paul D. GOLLNICK, and Robert S. PHILLIPS. "Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with l-tyrosine." Biochemical Journal 363, no. 3 (2002): 745–52. http://dx.doi.org/10.1042/bj3630745.

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Thr-124 and Phe-448 are located in the active site of Citrobacter freundii tyrosine phenol-lyase (TPL) near the phenol ring of a bound substrate analogue, 3-(4′-hydroxyphenyl)propionic acid [Sundararaju, Antson, Phillips, Demidkina, Barbolina, Gollnick, Dodson and Wilson (1997) Biochemistry 36, 6502–6510]. Thr-124 is replaced by Asp and Phe-448 is replaced by His in the crystal structure of a structurally similar enzyme, Proteus vulgaris tryptophan indole-lyase, which has 50% identical residues. Hence, Thr-124 and Phe-448 in TPL were mutated to Ala or Asp, and His, respectively, in order to pr

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34

Seisser, Birgit, René Zinkl, Karl Gruber, Franz Kaufmann, Andreas Hafner, and Wolfgang Kroutil. "Cutting Long Syntheses Short: Access to Non-Natural Tyrosine Derivatives Employing an Engineered Tyrosine Phenol Lyase." Advanced Synthesis & Catalysis 352, no. 4 (2010): 731–36. http://dx.doi.org/10.1002/adsc.200900826.

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35

Pioselli, Barbara, Stefano Bettati, Tatyana V. Demidkina, Lyudmila N. Zakomirdina, Robert S. Phillips, and Andrea Mozzarelli. "Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformations." Protein Science 13, no. 6 (2004): 1706–7. http://dx.doi.org/10.1002/pro.131707.

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36

Pioselli, B. "Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformations." Protein Science 13, no. 4 (2004): 913–24. http://dx.doi.org/10.1110/ps.03492904.

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37

Kim, Kyonghee, та Philip A. Cole. "ChemInform Abstract: Synthesis of (2S,3R)-β-Methyltyrosine Catalyzed by Tyrosine Phenol-Lyase." ChemInform 30, № 32 (2010): no. http://dx.doi.org/10.1002/chin.199932204.

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38

Demidkina, Tatyana V., and Igor V. Myagkikh. "The activity and reaction specificity of tyrosine phenol-lyase regulated by monovalent cations." Biochimie 71, no. 4 (1989): 565–71. http://dx.doi.org/10.1016/0300-9084(89)90188-0.

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39

Li, Guosi, Jiazhang Lian, Hailong Xue, et al. "Biocascade Synthesis of L-Tyrosine Derivatives by Coupling a Thermophilic Tyrosine Phenol-Lyase and L-Lactate Oxidase." European Journal of Organic Chemistry 2020, no. 8 (2020): 1050–54. http://dx.doi.org/10.1002/ejoc.202000061.

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40

Para, G., and J. Baratti. "The effect of phenol on growth and induction of tyrosine phenol lyase of escherichia intermedia and Erwinia herbicola." Biotechnology Letters 9, no. 6 (1987): 399–404. http://dx.doi.org/10.1007/bf01089004.

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41

DEMIDKINA, Tatyana V., Maria V. BARBOLINA, Nicolai G. FALEEV, Bakthavatsalam SUNDARARAJU, Paul D. GOLLNICK, and Robert S. PHILLIPS. "Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with l-tyrosine." Biochemical Journal 363, no. 3 (2002): 745. http://dx.doi.org/10.1042/0264-6021:3630745.

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42

Katayama, Takane, Hideyuki Suzuki, and Hidehiko Kumagai. "Control mechanism of expression of tyrosine phenol-lyase, vitamin B6dependent L-DOPA producing enzyme." BioFactors 11, no. 1-2 (2000): 103–4. http://dx.doi.org/10.1002/biof.5520110130.

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43

KATAYAMA, Takane, Hideyuki SUZUKI, Kenji YAMAMOTO, and Hidehiko KUMAGAI. "Transcriptional Regulation of Tyrosine Phenol-lyase Gene Mediated through TyrR and cAMP Receptor Protein." Bioscience, Biotechnology, and Biochemistry 63, no. 10 (1999): 1823–27. http://dx.doi.org/10.1271/bbb.63.1823.

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44

Phillips, Robert S. "Reactions of O-acyl-l-serines with tryptophanase, tyrosine phenol-lyase, and tryptophan synthase." Archives of Biochemistry and Biophysics 256, no. 1 (1987): 302–10. http://dx.doi.org/10.1016/0003-9861(87)90450-4.

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45

Han, Hongmei, Weizhu Zeng, Guoqiang Zhang, and Jingwen Zhou. "Active tyrosine phenol-lyase aggregates induced by terminally attached functional peptides in Escherichia coli." Journal of Industrial Microbiology & Biotechnology 47, no. 8 (2020): 563–71. http://dx.doi.org/10.1007/s10295-020-02294-4.

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Abstract The formation of inclusion bodies (IBs) without enzyme activity in bacterial research is generally undesirable. Researchers have attempted to recovery the enzyme activities of IBs, which are commonly known as active IBs. Tyrosine phenol-lyase (TPL) is an important enzyme that can convert pyruvate and phenol into 3,4-dihydroxyphenyl-l-alanine (L-DOPA) and IBs of TPL can commonly occur. To induce the correct folding and recover the enzyme activity of the IBs, peptides, such as ELK16, DKL6, L6KD, ELP10, ELP20, L6K2, EAK16, 18A, and GFIL16, were fused to the carboxyl terminus of TPL. The

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46

Antson, Alfred A., Boris V. Strokopytov, Garib N. Murshudov, et al. "The polypeptide chain fold in tyrosine phenol-lyase, a pyridoxal-5′-phosphate-dependent enzyme." FEBS Letters 302, no. 3 (1992): 256–60. http://dx.doi.org/10.1016/0014-5793(92)80454-o.

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47

Tang, Xiao-Ling, Hui Suo, Ren-Chao Zheng, and Yu-Guo Zheng. "An efficient colorimetric high-throughput screening method for synthetic activity of tyrosine phenol-lyase." Analytical Biochemistry 560 (November 2018): 7–11. http://dx.doi.org/10.1016/j.ab.2018.08.026.

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48

Katayama, Takane, Hideyuki Suzuki, Takashi Koyanagi, and Hidehiko Kumagai. "Cloning and Random Mutagenesis of the Erwinia herbicola tyrR Gene for High-Level Expression of Tyrosine Phenol-Lyase." Applied and Environmental Microbiology 66, no. 11 (2000): 4764–71. http://dx.doi.org/10.1128/aem.66.11.4764-4771.2000.

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ABSTRACT Tyrosine phenol-lyase (Tpl), which can synthesize 3,4-dihydroxyphenylalanine from pyruvate, ammonia, and catechol, is a tyrosine-inducible enzyme. Previous studies demonstrated that thetpl promoter of Erwinia herbicola is activated by the TyrR protein of Escherichia coli. In an attempt to create a high-Tpl-expressing strain, we cloned the tyrRgene of E. herbicola and then randomly mutagenized it. Mutant TyrR proteins with enhanced ability to activate tplwere screened for by use of the lac reporter system inE. coli. The most increased transcription oftpl was observed for the strain wit

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49

Phillips, Robert S., Andrew Vita, J. Blaine Spivey, Alexander P. Rudloff, Max D. Driscoll, and Sam Hay. "Ground-State Destabilization by Phe-448 and Phe-449 Contributes to Tyrosine Phenol-Lyase Catalysis." ACS Catalysis 6, no. 10 (2016): 6770–79. http://dx.doi.org/10.1021/acscatal.6b01495.

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50

Rha, Eugene, Sujin Kim, Su-Lim Choi, et al. "Simultaneous improvement of catalytic activity and thermal stability of tyrosine phenol-lyase by directed evolution." FEBS Journal 276, no. 21 (2009): 6187–94. http://dx.doi.org/10.1111/j.1742-4658.2009.07322.x.

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