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Literature summary for 4.1.99.2 extracted from

  • Milic, D.; Matkovic-Calogovic, D.; Demidkina, T.V.; Kulikova, V.V.; Sinitzina, N.I.; Antson, A.A.
    Structures of apo- and holo-tyrosine phenol-lyase reveal a catalytically critical closed conformation and suggest a mechanism for activation by K+ ions (2006), Biochemistry, 45, 7544-7552.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method with 50 mM potassium phosphate (pH 8.0), 2 mM DTT, 0.2 M KCl, and 32.5% (w/v) PEG2000 for the apo-enzyme, and 50 mM triethanolamine buffer (pH 8.0), containing 0.5 mM PLP, 2 mM DTT, 0.4-0.8 M KCl, and 35-38% (w/v) PEG5000 for the holo-enzyme Citrobacter freundii

Metals/Ions

Metals/Ions Comment Organism Structure
K+ catalytically important Citrobacter freundii
additional information divalent cations (Mg2+, Ca2+, Ba2+, and Sr2+) do not activate TPL Citrobacter freundii

Organism

Organism UniProt Comment Textmining
Citrobacter freundii P31013
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Citrobacter freundii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-tyrosine + H2O
-
 Citrobacter freundii phenol + pyruvate + NH3
-
 r

Subunits

Subunits Comment Organism
tetramer x-ray crystallography Citrobacter freundii

Synonyms

Synonyms Comment Organism
L-tyrosine phenol-lyase
-
 Citrobacter freundii
TPL
-
 Citrobacter freundii

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.2
-
-
 Citrobacter freundii

pH Stability

pH Stability pH Stability Maximum Comment Organism
6
-
 decrease of the enzymatic activity at pH 6.0 Citrobacter freundii

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
 Citrobacter freundii