Abstract:
:Homology modeling of Streptomyces peucetius CYP147F1 was constructed using three cytochrome P450 structures, CYP107L1, CYPVdh, and CYPeryF, as templates. The lowest energy SPCYP147F1 model was then assessed for stereochemical quality and side-chain environment by Accelrys Discovery Studio 3.1 software. Further activesite optimization of the SPCYP147F1 was performed by molecular dynamics to generate the final SPCYP147F1 model. The substrate limonene was then docked into the model. The model-limonene complex was used to validate the active-site architecture, and functionally important residues within the substrate recognition site were identified by subsequent characterization of the secondary structure. The docking of limonene suggested that SPCYP147F1 would have broad specificity with the ligand based on the two different orientations of limonene within the active site facing to the heme. Limonene with C7 facing the heme with distance of 3.4 Angstrom from the Fe was predominant.
journal_name
J Microbiol Biotechnoljournal_title
Journal of microbiology and biotechnologyauthors
Bhattarai S,Liou K,Oh TJdoi
10.4014/jmb.1112.12053subject
Has Abstractpub_date
2012-07-01 00:00:00pages
917-22issue
7eissn
1017-7825issn
1738-8872pii
JMB022-07-06journal_volume
22pub_type
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