Isolation of the tyrosine phenol lyase gene from Citrobacter freundii

Jacek Polak; Henry Brzeski

doi:10.1007/bf01022599

Isolation of the tyrosine phenol lyase gene from Citrobacter freundii

Biotechnology Letters ◽

10.1007/bf01022599 ◽

1990 ◽

Vol 12 (11) ◽

pp. 805-810 ◽

Cited By ~ 8

Author(s):

Jacek Polak ◽

Henry Brzeski

Keyword(s):

Citrobacter Freundii ◽

Tyrosine Phenol Lyase

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Binding of phenol and analogs to alanine complexes of tyrosine phenol-lyase from Citrobacter freundii: Implications for the mechanisms of .alpha.,.beta.-elimination and alanine racemization

Biochemistry ◽

10.1021/bi00094a016 ◽

1993 ◽

Vol 32 (43) ◽

pp. 11591-11599 ◽

Cited By ~ 26

Author(s):

Haoyuan Chen ◽

Robert S. Phillips

Keyword(s):

Citrobacter Freundii ◽

Tyrosine Phenol Lyase ◽

Beta Elimination ◽

Alpha Beta

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Aspartic acid 214 in Citrobacter freundii tyrosine phenol-lyase ensures sufficient C–H-acidity of the external aldimine intermediate and proper orientation of the cofactor at the active site

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics ◽

10.1016/j.bbapap.2006.05.001 ◽

2006 ◽

Vol 1764 (7) ◽

pp. 1268-1276 ◽

Cited By ~ 9

Author(s):

T.V. Demidkina ◽

N.G. Faleev ◽

A.I. Papisova ◽

N.P. Bazhulina ◽

V.V. Kulikova ◽

...

Keyword(s):

Aspartic Acid ◽

Active Site ◽

Citrobacter Freundii ◽

Tyrosine Phenol Lyase ◽

Proper Orientation

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Threonine-124 and phenylalanine-448 in Citrobacter freundii tyrosine phenol-lyase are necessary for activity with l-tyrosine

Biochemical Journal ◽

10.1042/0264-6021:3630745 ◽

2002 ◽

Vol 363 (3) ◽

pp. 745 ◽

Cited By ~ 15

Author(s):

Tatyana V. DEMIDKINA ◽

Maria V. BARBOLINA ◽

Nicolai G. FALEEV ◽

Bakthavatsalam SUNDARARAJU ◽

Paul D. GOLLNICK ◽

...

Keyword(s):

Citrobacter Freundii ◽

Tyrosine Phenol Lyase

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Structure of tyrosine phenol-lyase genes from Citrobacter freundii and structural comparison with tryptophanase from Escherichia coli

Journal of Fermentation and Bioengineering ◽

10.1016/0922-338x(91)90207-w ◽

1991 ◽

Vol 72 (3) ◽

pp. 147-151 ◽

Cited By ~ 13

Author(s):

Satoru Iwamori ◽

Sestuo Yoshino ◽

Ken-Ichi Ishiwata ◽

Nobuyoshi Makiguchi

Keyword(s):

Escherichia Coli ◽

Citrobacter Freundii ◽

Structural Comparison ◽

Tyrosine Phenol Lyase

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Optimization of process parameters for the production of tyrosine phenol lyase by Citrobacter freundii MTCC 2424

Bioresource Technology ◽

10.1016/j.biortech.2008.09.044 ◽

2009 ◽

Vol 100 (5) ◽

pp. 1840-1846 ◽

Cited By ~ 21

Author(s):

Meenakshi Chandel ◽

Wamik Azmi

Keyword(s):

Process Parameters ◽

Citrobacter Freundii ◽

Optimization Of Process Parameters ◽

Tyrosine Phenol Lyase

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Mechanistic deductions from kinetic isotope effects and pH studies of pyridoxal phosphate dependent carbon-carbon lyases: Erwinia herbicola and Citrobacter freundii tyrosine phenol-lyase

Biochemistry ◽

10.1021/bi00419a023 ◽

1988 ◽

Vol 27 (19) ◽

pp. 7333-7338 ◽

Cited By ~ 33

Author(s):

Dennis M. Kiick ◽

Robert S. Phillips

Keyword(s):

Pyridoxal Phosphate ◽

Isotope Effects ◽

Kinetic Isotope Effects ◽

Citrobacter Freundii ◽

Erwinia Herbicola ◽

Kinetic Isotope ◽

Tyrosine Phenol Lyase

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Serine 51 residue of Citrobacter freundii tyrosine phenol-lyase assists in C-α-proton abstraction and transfer in the reaction with substrate

Biochimie ◽

10.1016/j.biochi.2017.11.016 ◽

2018 ◽

Vol 147 ◽

pp. 63-69 ◽

Cited By ~ 4

Author(s):

Maria V. Barbolina ◽

Vitalia V. Kulikova ◽

Marina A. Tsvetikova ◽

Natalia V. Anufrieva ◽

Svetlana V. Revtovich ◽

...

Keyword(s):

Citrobacter Freundii ◽

Proton Abstraction ◽

Tyrosine Phenol Lyase

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Site-Directed Mutagenesis of Tyrosine-71 to Phenylalanine in Citrobacter freundii Tyrosine Phenol-Lyase: Evidence for Dual Roles of Tyrosine-71 as a General Acid Catalyst in the Reaction Mechanism and in Cofactor Binding

Biochemistry ◽

10.1021/bi00038a023 ◽

1995 ◽

Vol 34 (38) ◽

pp. 12276-12283 ◽

Cited By ~ 42

Author(s):

Hao Yuan Chen ◽

Tatyana V. Demidkina ◽

Robert S. Phillips

Keyword(s):

Reaction Mechanism ◽

Acid Catalyst ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Citrobacter Freundii ◽

Dual Roles ◽

Cofactor Binding ◽

General Acid ◽

Tyrosine Phenol Lyase

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Crystal Structures of Wild-Type and F448A Mutant Citrobacter freundii Tyrosine Phenol-Lyase Complexed with a Substrate and Inhibitors: Implications for the Reaction Mechanism

Biochemistry ◽

10.1021/acs.biochem.8b00724 ◽

2018 ◽

Vol 57 (43) ◽

pp. 6166-6179 ◽

Cited By ~ 1

Author(s):

Robert S. Phillips ◽

Steven Craig

Keyword(s):

Reaction Mechanism ◽

Crystal Structures ◽

Citrobacter Freundii ◽

Wild Type ◽

Tyrosine Phenol Lyase

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Site-Directed Mutagenesis of His343Ala in Citrobacter freundii Tyrosine Phenol-Lyase. Effects on the Kinetic Mechanism and Rate-Determining Step

European Journal of Biochemistry ◽

10.1111/j.1432-1033.1995.tb20496.x ◽

1995 ◽

Vol 229 (2) ◽

pp. 540-549 ◽

Cited By ~ 30

Author(s):

Haoyuan Chen ◽

Paul Gollnick ◽

Robert S. Phillips

Keyword(s):

Kinetic Mechanism ◽

Site Directed Mutagenesis ◽

Directed Mutagenesis ◽

Citrobacter Freundii ◽

Rate Determining Step ◽

Tyrosine Phenol Lyase

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