Relevant bibliographies by topics / Tyrosine phenol-lyase

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters

Academic literature on the topic 'Tyrosine phenol-lyase'

Author: Grafiati
Published: 4 June 2021
Last updated: 5 February 2022

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Journal articles on the topic "Tyrosine phenol-lyase"

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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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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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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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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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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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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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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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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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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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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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Dissertations / Theses on the topic "Tyrosine phenol-lyase"

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Katayama, Takane. "Studies on Expression of Tyrosine Phenol-Lyase Gene in Erwinia herbicola." Kyoto University, 1999. http://hdl.handle.net/2433/78095.

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Kyoto University (京都大学)<br>0048<br>新制・課程博士<br>博士(農学)<br>甲第7905号<br>農博第1063号<br>新制||農||780(附属図書館)<br>学位論文||H11||N3268(農学部図書室)<br>UT51-99-G499<br>京都大学大学院農学研究科食品工学専攻<br>(主査)教授 熊谷 英彦, 教授 清水 昌, 教授 江崎 信芳<br>学位規則第4条第1項該当
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Lloyd-George, Ian. "The conversion of ammonia, phenol and pyruvate into tyrosine by the use of the tyrosine phenol-lyase activity of microencapsulated Erwinia Herbicola." Thesis, McGill University, 1993. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=41200.

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The tyrosine phenol-lyase (TPL)-E.C. 4.1.99.2-activity of free and alginate-polylysine-alginate microencapsulated whole cells of Erwinia herbicola, was used to convert ammonia, pyruvate and phenol or catechol into L-tyrosine of dihydroxyphenyl-L-alanine (L-dopa). This conversion could serve as the basis of a novel system for the removal of toxic ammonia and phenol from the blood during liver failure.<br>It was found that there were endogenous modifiers in the whole cell TPL system, hence the kinetic parameters vary with the amount of cells in the system. However typically the apparent $ rm K s
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Ibarra, Escutia Pedro. "Mise au point de biocapteurs enzymatiques pour la quantification du contenu phénolique d’extraits naturels." Perpignan, 2010. http://www.theses.fr/2010PERP1023.

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Le mémoire de thèse a pour objectif la mise au point de biocapteurs enzymatiques à détection ampérométrique pour l’évaluation du contenu phénolitique des infusions et de jus de raisins. Deux polyphénols oxydases ont été utilisées : une tyrosinase extraite de champignon et une laccase provenant de trametes versicolor. Les deux enzymes ont été immobilisées par encapsulation dans un gel de polyvinyle alcool photopolymérisable de PVA-AWP (le groupement azide sert à la polymérisation) et par co-réticulation en utilisant du glutaraldéhyde. Les paramètres expérimentaux, pH, température et potentiel a
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Chen, Tsai-Hsia, and 陳彩霞. "Application and establishment of cell surface display system of citinase and tyrosine phenol lyase on Escherichia coli." Thesis, 2006. http://ndltd.ncl.edu.tw/handle/43764266238567218234.

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碩士<br>國立屏東科技大學<br>食品科學系<br>94<br>Gram-negative bacteria have developed various surface display systems for targeting foreign proteins on the cell surface. The ice nucleation protein (INP), a membrane-associated protein from Pseudomonas syringae. The INP is able to accelerate ice crystal formation in supercooled water, which has a multidomain organization with nonrepetitive N- and C- terminal domains, and a highly repetitive central domain responsible for ice nucleation activity. In our study, it has been demonstrated that truncated INP derivatives containing the N-terminal domain (INPN), plus
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Book chapters on the topic "Tyrosine phenol-lyase"

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Schomburg, Dietmar, and Margit Salzmann. "Tyrosine phenol-lyase." In Enzyme Handbook 1. Springer Berlin Heidelberg, 1990. http://dx.doi.org/10.1007/978-3-642-86605-0_126.

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Antson, A. A., G. G. Dodson, K. S. Wilson, S. V. Pletnev, E. G. Harutyunyan, and T. V. Demidkina. "Crystallographic studies of tyrosine phenol-lyase." In Biochemistry of Vitamin B6 and PQQ. Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7393-2_30.

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VonTersch, R. L., F. Secundo, R. S. Phillips, and M. G. Newton. "Preparation of Fluorinated Amino Acids with Tyrosine Phenol Lyase." In ACS Symposium Series. American Chemical Society, 1996. http://dx.doi.org/10.1021/bk-1996-0639.ch007.

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Demidkina, T. V., and I. V. Myagkikh. "Structural and Catalytic Properties of Citrobacter Intermedius Tyrosine Phenol-Lyase." In Biochemistry of Vitamin B6. Birkhäuser Basel, 1987. http://dx.doi.org/10.1007/978-3-0348-9308-4_40.

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Phillips, Robert S., Haoyuan Chen, and Paul Gollnick. "Studies of the Mechanism of Tyrosine Phenol-lyase: Kinetics and Site-Directed Mutagenesis." In Biochemistry of Vitamin B6 and PQQ. Birkhäuser Basel, 1994. http://dx.doi.org/10.1007/978-3-0348-7393-2_31.

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Faleev, N. G., S. B. Ruvinov, T. V. Demidkina, et al. "The Substrate Specificity of Tyrosine Phenol-Lyase During the Different Stages of Enzymatic Process." In Biochemistry of Vitamin B6. Birkhäuser Basel, 1987. http://dx.doi.org/10.1007/978-3-0348-9308-4_39.

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"12. Tyrosine Phenol-Lyase." In Handbook on Metalloproteins. CRC Press, 2001. http://dx.doi.org/10.1201/9781482270822-6.

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ANTSON, ALFRED A., OLGA N. ZOGRAF, ELENA V. ORLOVA, EMIL H. HARUTYUNYAN, MICHAEL B. SHERMAN, and TATYANA V. DEMIDKINA. "Crystallization of Tyrosine Phenol-Lyase from Citrobacter Intermidius. Electron Microscopy of Tubes." In Enzymes Dependent on Pyridoxal Phosphate and Other Carbonyl Compounds As Cofactors. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-08-040820-0.50065-0.

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