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1.14.14.133: 1,8-cineole 2-endo-monooxygenase

This is an abbreviated version!
For detailed information about 1,8-cineole 2-endo-monooxygenase, go to the full flat file.

Word Map on EC 1.14.14.133

Reaction

1,8-cineole
+
[reduced flavodoxin]
 +
O2
=
2-endo-hydroxy-1,8-cineole
 +
[oxidized flavodoxin]
 +
H2O

Synonyms

CinA, CYP176A, CYP176A1, EC 1.14.13.156, P450cin

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.14.133 1,8-cineole 2-endo-monooxygenase

Crystallization

Crystallization on EC 1.14.14.133 - 1,8-cineole 2-endo-monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with substrate 1,8-cineole, to 1.7 A resolution, and comparison with P450cam, EC 1.14.15.1. The active site of cytochrome P450cin is substantially different from that of cytochrome P450cam in that the B' helix, essential for substrate binding in many cytochrome P450s, is replaced by an ordered loop that results in substantial changes in active site topography. Cytochrome P450cin does not have the conserved threonine, Thr252 in cytochrome P450cam. Instead, the analogous residue in cytochrome P450cin is Asn242, which provides the only direct protein H-bonding interaction with the substrate. Cytochrome P450cin uses a flavodoxin-like redox partner to reduce the heme iron rather than the more traditional ferredoxin-like Fe2S2 redox partner used by cytochrome P450cam
X-ray crystal structures of the substrate-free and -bound N242A mutant to 2.0 and 3.0 A resolution, respcetively. Mutation results in a reorientation of the substrate such that (R)-6'-hydroxycineole should be a major product