Tryptophan N-monooxygenase

Tryptophan N-monooxygenase
Identifiers
EC number 1.14.13.125
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB 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+ (E)-indol-3-ylacetaldoxime + 2 NADP+ + CO2 + 3 H2O (overall reaction)
(1a) L-tryptophan + O2 + NADPH + H+ N-hydroxy-L-tryptophan + NADP+ + H2O
(1b) N-hydroxy-L-tryptophan + O2 + NADPH + H+ N,N-dihydroxy-L-tryptophan + NADP+ + H2O
(1c) N,N-dihydroxy-L-tryptophan (E)-indol-3-ylacetaldoxime + CO2 + H2O

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

References

  1. Mikkelsen, M.D.; Hansen, C.H.; Wittstock, U.; Halkier, B.A. (2000). "Cytochrome P450 CYP79B2 from Arabidopsis catalyzes the conversion of tryptophan to indole-3-acetaldoxime, a precursor of indole glucosinolates and indole-3-acetic acid". J. Biol. Chem. 275 (43): 33712–33717. doi:10.1074/jbc.M001667200. PMID 10922360.
  2. Hull, A.K.; Vij, R.; Celenza, J.L. (2000). "Arabidopsis cytochrome P450s that catalyze the first step of tryptophan-dependent indole-3-acetic acid biosynthesis". Proc. Natl. Acad. Sci. USA. 97 (5): 2379–2384. doi:10.1073/pnas.040569997. PMC 15809Freely accessible. PMID 10681464.
  3. Zhao, Y.; Hull, A.K.; Gupta, N.R.; Goss, K.A.; Alonso, J.; Ecker, J.R.; Normanly, J.; Chory, J.; Celenza, J.L. (2002). "Trp-dependent auxin biosynthesis in Arabidopsis: involvement of cytochrome P450s CYP79B2 and CYP79B3". Genes Dev. 16 (23): 3100–3112. doi:10.1101/gad.1035402. PMC 187496Freely accessible. PMID 12464638.
  4. Naur, P.; Hansen, C.H.; Bak, S.; Hansen, B.G.; Jensen, N.B.; Nielsen, H.L.; Halkier, B.A. (2003). "CYP79B1 from Sinapis alba converts tryptophan to indole-3-acetaldoxime". Arch. Biochem. Biophys. 409 (1): 235–241. doi:10.1016/s0003-9861(02)00567-2. PMID 12464264.
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