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Applied and Environmental Microbiology, August 1999, p. 3470-3472, Vol. 65, No. 8
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Purification and Properties of an Esterase from the Yeast Saccharomyces cerevisiae and Identification of the Encoding Gene

Giuliano Degrassi,1,* Lasse Uotila,2 Raffaella Klima,3 and Vittorio Venturi1

Bacteriology Group1 and DNA Replication Group,3 International Centre for Genetic Engineering and Biotechnology, I-34012 Trieste, Italy, and Department of Clinical Chemistry, University of Helsinki, Meilahti Hospital, SF-00290 Helsinki, Finland2

Received 15 December 1998/Accepted 8 June 1999

We purified an intracellular esterase that can function as an S-formylglutathione hydrolase from the yeast Saccharomyces cerevisiae. Its molecular mass was 40 kDa, as determined by gel filtration and sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point was 5.0 by isoelectric focusing. The enzyme activity was optimal at 50°C and pH 7.0. The corresponding gene, YJLO68C, was identified by its N-terminal amino acid sequence and is not essential for cell viability. Null mutants have reduced esterase activities and grow slowly in the presence of formaldehyde. This enzyme may be involved in the detoxification of formaldehyde, which can be metabolized to S-formylglutathione by S. cerevisiae.

* Corresponding author. Mailing address: International Centre for Genetic Engineering and Biotechnology, Area Science Park, Padriciano 99, I-34012, Trieste, Italy. Phone: 39-40-3757317. Fax: 39-40-226555. E-mail: degrassi{at}icgeb.trieste.it.

Applied and Environmental Microbiology, August 1999, p. 3470-3472, Vol. 65, No. 8
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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