Biology:Tryptophan N-monooxygenase

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Short description: Class of enzymes
Tryptophan N-monooxygenase
Identifiers
EC number1.14.13.125
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Tryptophan N-monooxygenase (EC 1.14.13.125, tryptophan N-hydroxylase, CYP79B1, CYP79B2, CYP79B3) is an enzyme with systematic name L-tryptophan,NADPH:oxygen oxidoreductase (N-hydroxylating).[1][2][3][4] This enzyme catalyses the following chemical reaction

L-tryptophan + 2 O2 + 2 NADPH + 2 H+ [math]\displaystyle{ \rightleftharpoons }[/math] (E)-indol-3-ylacetaldoxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-tryptophan + O2 + NADPH + H+ [math]\displaystyle{ \rightleftharpoons }[/math] N-hydroxy-L-tryptophan + NADP+ + H2O
(1b) N-hydroxy-L-tryptophan + O2 + NADPH + H+ [math]\displaystyle{ \rightleftharpoons }[/math] N,N-dihydroxy-L-tryptophan + NADP+ + H2O
(1c) N,N-dihydroxy-L-tryptophan [math]\displaystyle{ \rightleftharpoons }[/math] (E)-indol-3-ylacetaldoxime + CO2 + H2O

Tryptophan N-monooxygenase is a heme-thiolate protein (P-450).

References

  1. "Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid". The Journal of Biological Chemistry 275 (43): 33712–7. October 2000. doi:10.1074/jbc.M001667200. PMID 10922360. 
  2. "Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis". Proceedings of the National Academy of Sciences of the United States of America 97 (5): 2379–84. February 2000. doi:10.1073/pnas.040569997. PMID 10681464. Bibcode2000PNAS...97.2379H. 
  3. "Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3". Genes & Development 16 (23): 3100–12. December 2002. doi:10.1101/gad.1035402. PMID 12464638. 
  4. "CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime". Archives of Biochemistry and Biophysics 409 (1): 235–41. January 2003. doi:10.1016/s0003-9861(02)00567-2. PMID 12464264. 

External links