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Tryptophanase

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Enzyme that converts tryptophan into indole
tryptophanase
Tryptophanase tetramer, E.Coli
Identifiers
EC no.4.1.99.1
CAS no.9024-00-4
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MetaCycmetabolic pathway
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The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

L-tryptophan + H2O {\displaystyle \rightleftharpoons } indole + pyruvate + NH3

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.

Structural studies

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

References

  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. 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. 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. 1AX4 Retrieved from Protein Data Bank (PDB)
  5. 2C44 Retrieved from Protein Data Bank (PDB)
  6. 2OQX Retrieved from Protein Data Bank (PDB)

External links

Carbon–carbon lyases (EC 4.1)
4.1.1: Carboxy-lyases
4.1.2: Aldehyde-lyases
4.1.3: Oxo-acid-lyases
4.1.99: Other
Enzymes
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