Biology:Isoleucine N-monooxygenase

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Short description: Class of enzymes
Isoleucine N-monooxygenase
Identifiers
EC number1.14.13.117
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Isoleucine N-monooxygenase (EC 1.14.13.117, CYP79D3, CYP79D4) is an enzyme with systematic name L-isoleucine,NADPH:oxygen oxidoreductase (N-hydroxylating).[1][2] This enzyme catalyses the following chemical reaction

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

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

References

  1. "Cytochromes P-450 from cassava (Manihot esculenta Crantz) catalyzing the first steps in the biosynthesis of the cyanogenic glucosides linamarin and lotaustralin. Cloning, functional expression in Pichia pastoris, and substrate specificity of the isolated recombinant enzymes". The Journal of Biological Chemistry 275 (3): 1966–75. January 2000. doi:10.1074/jbc.275.3.1966. PMID 10636899. 
  2. "Biosynthesis of the nitrile glucosides rhodiocyanoside A and D and the cyanogenic glucosides lotaustralin and linamarin in Lotus japonicus". Plant Physiology 135 (1): 71–84. May 2004. doi:10.1104/pp.103.038059. PMID 15122013. 

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