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Applied and Environmental Microbiology, October 2009, p. 6306-6311, Vol. 75, No. 19
0099-2240/09/$08.00+0     doi:10.1128/AEM.01160-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Acetolactate Synthase from Bacillus subtilis Serves as a 2-Ketoisovalerate Decarboxylase for Isobutanol Biosynthesis in Escherichia coli{triangledown}

Shota Atsumi, Zhen Li, and James C. Liao*

Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, California 90095

Received 19 May 2009/ Accepted 4 August 2009

A pathway toward isobutanol production previously constructed in Escherichia coli involves 2-ketoacid decarboxylase (Kdc) from Lactococcus lactis that decarboxylates 2-ketoisovalerate (KIV) to isobutyraldehyde. Here, we showed that a strain lacking Kdc is still capable of producing isobutanol. We found that acetolactate synthase from Bacillus subtilis (AlsS), which originally catalyzes the condensation of two molecules of pyruvate to form 2-acetolactate, is able to catalyze the decarboxylation of KIV like Kdc both in vivo and in vitro. Mutational studies revealed that the replacement of Q487 with amino acids with small side chains (Ala, Ser, and Gly) diminished only the decarboxylase activity but maintained the synthase activity.

* Corresponding author. Mailing address: Department of Chemical and Biomolecular Engineering, University of California, Los Angeles, CA 90095. Phone: (310) 825-1656. Fax: (310) 206-4107. E-mail: liaoj{at}seas.ucla.edu

{triangledown} Published ahead of print on 14 August 2009.

Applied and Environmental Microbiology, October 2009, p. 6306-6311, Vol. 75, No. 19
0099-2240/09/$08.00+0     doi:10.1128/AEM.01160-09
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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