Tryptophanase

Tryptophanase

Tryptophanase

Enzyme that converts tryptophan into indole

The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

L-tryptophan + H2O indole + pyruvate + NH3
Quick Facts Identifiers, EC no. ...

This enzyme belongs to the family of lyases, specifically in the "catch-all" class of carbon-carbon lyases. The systematic name of this enzyme class is L-tryptophan indole-lyase (deaminating; pyruvate-forming). Other names in common use include L-tryptophanase, and L-tryptophan indole-lyase (deaminating). This enzyme participates in tryptophan metabolism and nitrogen metabolism. It has 2 cofactors: pyridoxal phosphate, and potassium.[1][2][3]

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1AX4,[4] 2C44,[5] and 2OQX.[6]

References

  1. [1]
    BURNS RO, DEMOSS RD (1962). "Properties of tryptophanase from Escherichia coli". Biochim. Biophys. Acta. 65 (2): 233–44. doi:10.1016/0006-3002(62)91042-9. PMID 14017164.
  2. [2]
    Cowell JL, Maser K, DeMoss, RD (1973). "Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties". Biochimica et Biophysica Acta. 315: 449–463. doi:10.1016/0005-2744(73)90276-3.
  3. [3]
    NEWTON WA, MORINO Y, SNELL EE (1965). "Properties of Crystalline Tryptophanase". J. Biol. Chem. 240 (3): 1211–8. doi:10.1016/S0021-9258(18)97562-9. PMID 14284727.
  4. [4]
    1AX4 Retrieved from Protein Data Bank (PDB)
  5. [5]
    2C44 Retrieved from Protein Data Bank (PDB)
  6. [6]
    2OQX Retrieved from Protein Data Bank (PDB)


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