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Journal article

Improving the affinity and activity of CYP101D2 for hydrophobic substrates.

Abstract:

CYP101D2 is a cytochrome P450 monooxygenase from Novosphingobium aromaticivorans which is closely related to CYP101A1 (P450cam) from Pseudomonas putida. Both enzymes selectively hydroxylate camphor to 5-exo-hydroxycamphor, and the residues that line the active sites of both enzymes are similar including the pre-eminent Tyr96 residue. However, Met98 and Leu253 in CYP101D2 replace Phe98 and Val247 in CYP101A1, and camphor binding only results in a maximal change in the spin state to 40 % high-s...

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Publication status:
Published

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Publisher copy:
10.1007/s00253-012-4278-7

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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Inorganic Chemistry
Role:
Author
Journal:
Applied microbiology and biotechnology
Volume:
97
Issue:
9
Pages:
3979-3990
Publication date:
2013-05-05
DOI:
EISSN:
1432-0614
ISSN:
0175-7598
URN:
uuid:98653e95-a0e7-453f-b61a-8a564a1e0d36
Source identifiers:
344148
Local pid:
pubs:344148

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