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Literature summary for 1.14.14.133 extracted from

  • Meharenna, Y.T.; Slessor, K.E.; Cavaignac, S.M.; Poulos, T.L.; De Voss, J.J.
    The critical role of substrate-protein hydrogen bonding in the control of regioselective hydroxylation in p450cin (2008), J. Biol. Chem., 283, 10804-10812.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Citrobacter braakii

Protein Variants

Protein Variants Comment Organism
N242A no change in characteristic CO-bound spectrum and spectrally determined KD for substrate binding. Mutation leads to modest effects on enzyme activity and on the diversion of the NADPH-reducing equivalent toward unproductive peroxide formation, but results in a reorientation of the substrate such that (R)-6'-hydroxycineole is a major product Citrobacter braakii

Organism

Organism UniProt Comment Textmining
Citrobacter braakii Q8VQF6
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1,8-cineole + [reduced flavodoxin] + O2
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Citrobacter braakii 6beta-hydroxycineole + [oxidized flavodoxin] + H2O
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