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Items: 1 to 20 of 94

1.

Interaction of tyrosine phenol-lyase with phosphoroorganic analogues of substrate amino acids.

Faleev NG, Zhukov YN, Khurs EN, Gogoleva OI, Barbolina MV, Bazhulina NP, Belikov VM, Demidkina TV, Khomutov RM.

Eur J Biochem. 2000 Dec;267(23):6897-902.

2.

Tyrosine phenol-lyase from Citrobacter intermedius. Factors controlling substrate specificity.

Faleev NG, Ruvinov SB, Demidkina TV, Myagkikh IV, Gololobov MYu, Bakhmutov VI, Belikov VM.

Eur J Biochem. 1988 Nov 1;177(2):395-401.

3.

Syntheses of L-tyrosine-related amino acids by tyrosine phenol-lyase of Citrobacter intermedius.

Nagasawa T, Utagawa T, Goto J, Kim CJ, Tani Y, Kumagai H, Yamada H.

Eur J Biochem. 1981 Jun;117(1):33-40.

4.

Transamination catalysed by tyrosine phenol-lyase from Citrobacter intermedius.

Demidkina TV, Myagkikh IV, Azhayev AV.

Eur J Biochem. 1987 Dec 30;170(1-2):311-6.

5.

Elementary processes in the interaction of tyrosine phenol lyase with inhibitors and substrate.

Muro T, Nakatani H, Hiromi K, Kumagai H, Yamada H.

J Biochem. 1978 Sep;84(3):633-40. No abstract available.

6.

Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.

Mouratou B, Kasper P, Gehring H, Christen P.

J Biol Chem. 1999 Jan 15;274(3):1320-5.

7.

[Isolation and properties of tyrosine phenol-lyase from Citrobacter intermedius].

Demidkina TV, Miagkikh IV, Faleev NG, Belikov VM.

Biokhimiia. 1984 Jan;49(1):32-7. Russian.

PMID:
6704450
8.
10.

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

Demidkina TV, Barbolina MV, Faleev NG, Sundararaju B, Gollnick PD, Phillips RS.

Biochem J. 2002 May 1;363(Pt 3):745-52.

11.

Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions.

Milić D, Matković-Calogović D, Demidkina TV, Kulikova VV, Sinitzina NI, Antson AA.

Biochemistry. 2006 Jun 20;45(24):7544-52.

12.

[Interaction of tyrosine-phenol-lyase from Citrobacter intermedius with amino acids and their derivatives: factors determining the effectiveness of binding].

Faleev NG, Ruvinov SB, Demidkina TV, Miagkikh IV, Gololobov MIu.

Mol Biol (Mosk). 1988 Jan-Feb;22(1):249-56. Russian.

PMID:
3374486
13.

[Substrate specificity of tyrosine-phenol-lyase. Electron and steric control at the stage of aromatic moiety elimination].

Faleev NG, Ruvinov SB, Bakhmutov VI, Demidkina TV, Miagkikh IV.

Mol Biol (Mosk). 1987 Nov-Dec;21(6):1636-44. Russian.

PMID:
2833689
15.
16.

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

Barbolina MV, Phillips RS, Gollnick PD, Faleev NG, Demidkina TV.

Protein Eng. 2000 Mar;13(3):207-15.

PMID:
10775663
17.
19.

Aminoacrylate intermediates in the reaction of Citrobacter freundii tyrosine phenol-lyase.

Phillips RS, Chen HY, Faleev NG.

Biochemistry. 2006 Aug 8;45(31):9575-83.

PMID:
16878992
20.

The role of substrate strain in the mechanism of the carbon-carbon lyases.

Phillips RS, Demidkina TV, Faleev NG.

Bioorg Chem. 2014 Dec;57:198-205. doi: 10.1016/j.bioorg.2014.06.002. Review.

PMID:
25035301

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