Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Milic, D.; Demidkina, T.V.; Faleev, N.G.; Matkovi?-Calogovi?, D.; Antson, A.A.
    Insights into the catalytic mechanism of tyrosine phenol-lyase from X-ray structures of quinonoid intermediates (2008), J. Biol. Chem., 283, 29206-29214.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.99.2 the plasmid pTZTPL is constructed for expression of the protein in Escherichia coli SVS370 cells Citrobacter freundii

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.1.99.2 the quinonoid intermediates of tyrosine phenol-lyase with L-alanine and L-methionine are trapped in the crystalline state and their structures are determined at 1.9 A and 1.95 A resolution, respectively Citrobacter freundii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.99.2 L-tyrosine + H2O Citrobacter freundii
-
 phenol + pyruvate + NH3
-
 r

Organism

EC Number Organism UniProt Comment Textmining
4.1.99.2 Citrobacter freundii P31013
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.99.2
-
 Citrobacter freundii

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
4.1.99.2 homotetramer composed of two catalytic dimers Citrobacter freundii

Synonyms

EC Number Synonyms Comment Organism
4.1.99.2 TPL
-
 Citrobacter freundii
4.1.99.2 tyrosine phenol-lyase
-
 Citrobacter freundii

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.99.2 pyridoxal 5'-phosphate
-
 Citrobacter freundii