ENTRY EC 1.14.15.1
NAME Camphor 5-monooxygenase
Camphor 5-exo-methylene hydroxylase
CLASS Oxidoreductases
Acting on paired donors with incorporation of molecular oxygen
With a reduced iron-sulfur protein as one donor, and
incorporation of one atom of oxygen
SYSNAME (+)-Camphor,reduced-putidaredoxin:oxygen oxidoreductase
(5-hydroxylating)
REACTION (+)-Camphor + Putidaredoxin + O2 = (+)-exo-5-Hydroxycamphor +
Oxidized putidaredoxin + H2O
SUBSTRATE (+)-Camphor
Putidaredoxin
O2
(-)-Camphor
1,2-Campholide
PRODUCT (+)-exo-5-Hydroxycamphor
Oxidized putidaredoxin
H2O
5-exo-Hydroxy-1,2-campholide
COFACTOR Heme
COMMENT A heme-thiolate protein (P-450)
Also acts on (-)-camphor and 1,2-campholide, forming
5-exo-hydroxy-1,2-campholide.
#STRUCTURE:
Helcies E(149-156), F(176-185), G(192-205), and I(234-267) form an
antiparallel Greek key helical bundle.
Heme: the heme is embedded between the proximal (helix L) and
distal (helix I) helicies. The heme propionates interact with
Arg112, Arg299, and His355. Gly249 is close approach to the distal
heme surface. Gly249 is conxerved among other P-450.
Axial heme ligand: Cys357 of the N-terminal end of helix L binds
to Fe(III) in the high-spin state. Phe350, Leu358, and Gln360 form
a pocket for Cys357.
Camphor: The carbonyl oxygen form hydrogen bonding to Tyr96 and
makes hydrophobic contact with Phe87, Leu244, Val247, Thr252,
Val295. Tyr96 is unique to P-450cam.
(Poulos et al. J.Biol.Chem., 260, 16122-16130, 1985)
MOTIF PS: PS00086 F-[SGNH]-x-[GD]-x-[RHPT]-x-C-[LIVMFAP]-[GAD]
STRUCTURES PDB: 1NOO 1PHA 1PHB 1PHC 1PHD 1PHE 1PHF 1PHG 2CP4 2CPP
3CP4 3CPP 4CP4 4CPP 5CPP 6CPP 7CPP 8CPP 1CP4
DBLINKS University of Geneva ENZYME DATA BANK: 1.14.15.1
WIT (What Is There) Metabolic Reconstruction: 1.14.15.1
SCOP (Structural Classificaion of Proteins): 1.14.15.1
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