Biology:Tryptophanase

From HandWiki
Short description: Enzyme that converts tryptophan into indole
tryptophanase
4w1y.jpg
Tryptophanase tetramer, E.Coli
Identifiers
EC number4.1.99.1
CAS number9024-00-4
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

The enzyme tryptophanase (EC 4.1.99.1) catalyzes the chemical reaction

L-tryptophan + H2O [math]\displaystyle{ \rightleftharpoons }[/math] indole + pyruvate + NH3
Indole.svg

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. "Properties of tryptophanase from Escherichia coli". Biochim. Biophys. Acta 65 (2): 233–44. 1962. doi:10.1016/0006-3002(62)91042-9. PMID 14017164. 
  2. "Tryptophanase from Aeromonas liquifaciens. Purification, molecular weight and some chemical, catalytic and immunological properties". Biochimica et Biophysica Acta 315: 449–463. 1973. doi:10.1016/0005-2744(73)90276-3. 
  3. "Properties of Crystalline Tryptophanase". J. Biol. Chem. 240 (3): 1211–8. 1965. 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