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TitleThe role of conformational flexibility in Baeyer-Villiger monooxygenase catalysis and structure.
Journal, issue, pagesBiochim Biophys Acta, Vol. 1864, Issue 12, Page 1641-1648, Year 2016
Publish dateAug 26, 2016
AuthorsBrahm J Yachnin / Peter C K Lau / Albert M Berghuis /
PubMed AbstractBACKGROUND: The Baeyer-Villiger monooxygenases (BMVOs) are a group of microbial enzymes that have garnered interest as industrial biocatalysts. While great strides have been made in recent years to ...BACKGROUND: The Baeyer-Villiger monooxygenases (BMVOs) are a group of microbial enzymes that have garnered interest as industrial biocatalysts. While great strides have been made in recent years to understand the mechanism of these enzymes from a structural perspective, our understanding remains incomplete. In particular, the role of a twenty residue loop (residues 487-504), which we refer to as the "Control Loop," that is observed in either an ordered or disordered state in various crystal structures remains unclear.
METHODS: Using SAXS, we have made the first observations of the Loop in solution with two BVMOs, cyclohexanone monooxygenase (CHMO) and cyclopentadecanone monooxygenase. We also made a series of mutants of CHMO and analyzed them using SAXS, ITC, and an uncoupling assay.
RESULTS: These experiments show that Control Loop ordering results in an overall more compact enzyme without altering global protein foldedness. We have also demonstrated that the Loop plays a critical and complex role on enzyme structure and catalysis. The Control Loop appears to have a direct impact on the organization of the overall structure of the protein, as well as in influencing the active site environment.
CONCLUSIONS: The data imply that the Loop can be divided into two regions, referred to as "sub-loops," that coordinate overall domain movements to changes in the active site.
GENERAL SIGNIFICANCE: A better understanding of the mechanistic role of the Control Loop may ultimately be helpful in designing mutants with altered specificity and improved catalytic efficiency.
External linksBiochim Biophys Acta / PubMed:27570148
MethodsSAS (X-ray synchrotron)
Structure data

SASDBA5: Cyclohexanone monooxygenase, wild-type (Cyclohexanone monooxygenase, CHMO)
Method: SAXS/SANS

SASDBB5: Cyclohexanone monooxygenase, NADP+, wild-type (Cyclohexanone monooxygenase, CHMO)
Method: SAXS/SANS

SASDBC5: Cyclohexanone monooxygenase, NADP+ and cyclohexanone, wild-type
Method: SAXS/SANS

SASDBD5: Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, wild-type
Method: SAXS/SANS

SASDBE5: Cyclohexanone monooxygenase, W492A (Cyclohexanone monooxygenase, CHMO-W492A)
Method: SAXS/SANS

SASDBF5: Cyclohexanone monooxygenase, NADP+, K501A (Cyclohexanone monooxygenase, CHMO-K501A)
Method: SAXS/SANS

SASDBG5: Cyclohexanone monooxygenase, NADP+, W492A (Cyclohexanone monooxygenase, CHMO-W492A)
Method: SAXS/SANS

SASDBH5: Cyclohexanone monooxygenase, NADP+ and cyclohexanone, W492A
Method: SAXS/SANS

SASDBJ5: Cyclohexanone monooxygenase, NADP+ and ε-caprolactone, W492A
Method: SAXS/SANS

SASDBK5: Cyclohexanone monooxygenase, K328A (Cyclohexanone monooxygenase)
Method: SAXS/SANS

SASDBL5: Cyclohexanone monooxygenase, NADP+, K328A (Cyclohexanone monooxygenase)
Method: SAXS/SANS

SASDBM5: Cyclohexanone monooxygenase, K328A-W492A (Cyclohexanone monooxygenase, CHMO-K328A-W492A)
Method: SAXS/SANS

SASDBN5: Cyclohexanone monooxygenase, NADP+, K328A-W492A (Cyclohexanone monooxygenase, CHMO-K328A-W492A)
Method: SAXS/SANS

SASDBP5: Cyclohexanone monooxygenase, N497A (Cyclohexanone monooxygenase, CHMO-N497A)
Method: SAXS/SANS

SASDBQ5: Cyclohexanone monooxygenase, NADP+, N497A (Cyclohexanone monooxygenase, CHMO-N497A)
Method: SAXS/SANS

SASDBR5: Cyclohexanone monooxygenase, K501A (Cyclohexanone monooxygenase, CHMO-K501A)
Method: SAXS/SANS

SASDBS5: Cyclohexanone monooxygenase, N497A-K501A (Cyclohexanone monooxygenase, CHMO-K501A)
Method: SAXS/SANS

SASDBT5: Cyclohexanone monooxygenase, NADP+, N497A-K501A (Cyclohexanone monooxygenase, CHMO-N497A-K501A)
Method: SAXS/SANS

SASDBU5: Cyclopentadecanone monooxygenase, wild-type (Cyclopentadecanone 1,2-monooxygenase)
Method: SAXS/SANS

SASDBV5: Cyclopentadecanone monooxygenase, NADP+, wild-type
Method: SAXS/SANS

SASDBW5: Cyclopentadecanone monooxygenase, NADP+ and cyclopentadecanone, wild-type
Method: SAXS/SANS

SASDBX5: Cyclopentadecanone monooxygenase, NADP+ and ω-pentadecalactone, wild-type
Method: SAXS/SANS

Source
  • Rhodococcus sp. hi-31 (bacteria)
  • Pseudomonas sp. hi-70 (bacteria)

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