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Plasma methionine depletion and pharmacokinetic properties in mice of methionine γ-lyase from Citrobacter freundii , Clostridium tetani and Clostridium sporogenes

Biomedicine & pharmacotherapy, 2017-04, Vol.88, p.978-984

2017

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Pathological Metabolism of Methionine in Malignant Cells Is a Potential Target for the Antitumor Therapy

Kliničeskaâ onkogematologiâ, 2017, Vol.10 (3), p.324-332

2017

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Kinetic and spectral parameters of interaction of Citrobacter freundii methionine γ-lyase with amino acids

Biochemistry (Moscow), 2010-10, Vol.75 (10), p.1272-1280

2010

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Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine γ-lyase with substrates

Biochemistry (Moscow), 2011-05, Vol.76 (5), p.564-570

2011

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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, 2006-07, Vol.1764 (7), p.1268-1276

2006

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Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate

Protein engineering, 2000-03, Vol.13 (3), p.207-215

2000

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Selective modification of tyrosine and cysteine residues in aspartate aminotransferase from pig heart cytosol

Biochemical and biophysical research communications, 1973-01, Vol.50 (2), p.377-383

1973

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The position of an essential tyrosine residue in the polypeptide chain of aspartate transaminase

FEBS letters, 1972-06, Vol.23 (2), p.262-264

1972

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Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola

Biochemistry and molecular biology international, 1996-02, Vol.38 (1), p.37-42

1996

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Plasma methionine depletion and pharmacokinetic properties in mice of methionine γ-lyase from Citrobacter freundii , Clostridium tetani and Clostridium sporogenes

Pathological Metabolism of Methionine in Malignant Cells Is a Potential Target for the Antitumor Therapy

Kinetic and spectral parameters of interaction of Citrobacter freundii methionine γ-lyase with amino acids

Three-dimensional structures of noncovalent complexes of Citrobacter freundii methionine γ-lyase with substrates

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

Citrobacter freundii tyrosine phenol-lyase: the role of asparagine 185 in modulating enzyme function through stabilization of a quinonoid intermediate

Selective modification of tyrosine and cysteine residues in aspartate aminotransferase from pig heart cytosol

The position of an essential tyrosine residue in the polypeptide chain of aspartate transaminase

Purification and crystals of tyrosine phenol-lyase from Erwinia herbicola

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