Putrid Pathway Probed | April 9, 2012 Issue - Vol. 90 Issue 15 | Chemical & Engineering News
Volume 90 Issue 15 | p. 11 | News of The Week
Issue Date: April 9, 2012

Putrid Pathway Probed

Natural Products: Studies of odorant biosynthesis could aid water remediation
Department: Science & Technology | Collection: Life Sciences
News Channels: Biological SCENE, Environmental SCENE
Keywords: crystal structure, enzymes, biosynthesis, terpenoids, water quality, camembert
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GPPMT enzyme (left) methylates geranyl diphosphate, and MIBS (enzyme on right) then cyclizes the product (bottom right) to form MIB—an unprecedented order of affairs in terpenoid biosynthesis.
Credit: Mustafa Köksal
A rendering of two proteins (GPPMT and MIBS as ribbon structures) and 3 molecules (as line drawings) involved in the biosynthesis of terpenoids. GPPMT is shaped like a star of David.
 
GPPMT enzyme (left) methylates geranyl diphosphate, and MIBS (enzyme on right) then cyclizes the product (bottom right) to form MIB—an unprecedented order of affairs in terpenoid biosynthesis.
Credit: Mustafa Köksal

Structural and mechanistic analyses have revealed how two bacterial enzymes biosynthesize the terpenoid odorant 2-methylisoborneol (MIB) (Biochemistry, DOI: 10.1021/bi300109c and 10.1021/bi201827a). The work could lead to an improved understanding of factors promoting MIB production and ways to mitigate MIB odors and off-flavors in food, beverages, and the water supply.

MIB is a volatile terpenoid produced by microorganisms. Its musty odor can be detected at low concentrations. It contributes to the scent of moist soil and Brie and Camembert cheeses. But its odor can also taint fish and cause off-taste and odor in drinking water.

“We expect that the structures of the enzymes responsible for MIB biosynthesis will lead to new approaches for inhibiting the generation of this contaminant, which threatens the public water supply and causes multi-million-dollar annual losses in the food and beverage industry,” says chemistry professor David W. Christianson of the University of Pennsylvania. He carried out the work with Penn postdoc Mustafa Köksal and chemistry professor David E. Cane and postdoc Wayne K. W. Chou of Brown University.

The structures show that one enzyme, geranyl diphosphate C-methyltransferase (GPPMT), is a hexamer resembling a Star of David and that the other, MIB synthase (MIBS), is a homodimer of 13-α-helix bundles.

Scientists already knew that GPPMT methylates a 10-carbon monoterpene substrate and that MIBS then cyclizes the product to MIB. In all other terpenoid biosyntheses, methylation occurs only after cyclization. The new studies have uncovered further details about this unique biosynthetic process. For example, they show the three-dimensional relationship of reacting species in GPPMT’s active site.

MIB is currently removed during water treatment by activated carbon filtration; biological filtration with immobilized bacteria; or UV-, ozone-, or hydrogen peroxide-based oxidation. But MIB contamination is difficult and expensive to remedy by such means, and water utilities are seeking better methods.

Christianson believes the new studies could aid rational design of GPPMT or MIBS inhibitors that might mitigate MIB generation in water sources. Research scientist Susan B. Watson of the National Water Research Institute, in Burlington, Ontario, believes jurisdictions are unlikely to permit treatment of water with enzyme inhibitors. However, she adds, the studies aid understanding of factors controlling expression of genes for the two enzymes, which could lead to better mitigation methods.

 
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