PMID: 8606158Apr 1, 1996Paper

Biochemical and molecular characterization of the extracellular esterase from Streptomyces diastatochromogenes

Journal of Bacteriology
C TeschC Bormann

Abstract

An esterase of Streptomyces diastatochromogenes was purified to homogeneity from culture filtrate. The purified enzyme had a molecular mass of 30,862 +/- 5.8 Da, as determined by electrospray mass spectrometry. The esterase-encoding gene was cloned on a 5.1-kb MboI fragment from S. diastatochromogenes genomic DNA into Streptomyces lividans TK23 by using plasmid vector pIJ702. Nucleotide sequence analysis predicted a 978-bp open reading frame, estA, encoding a protein of 326 amino acids, a potential ribosome binding site, and a putative 35- or 36-residue signal peptide for secretion in S. lividans or S. diastatochromogenes, respectively. The transcriptional initiation site was mapped 29 nucleotides upstream from the predicted translational start codon of estA in S. diastatochromogenes. The protein sequence deduced from the estA gene was similar to that of the esterase from the plant pathogen Streptomyces scabies. Both enzymes lacked the conserved motif GXSXG carrying the active-site serine of hydrolytic enzymes. A serine modified by [1,3-3H]diisopropyl fluorophosphate was located at position 11 of the mature enzyme in the sequence GDSYT. This finding and results obtained by site-directed mutagenesis studies indicate that serine ...Continue Reading

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Citations

May 8, 2013·Canadian Journal of Microbiology·Doaa KomeilCarole Beaulieu
Jun 8, 2007·Journal of Industrial Microbiology & Biotechnology·Sameh H SororJohn Cullum
May 25, 2010·Journal of Industrial Microbiology & Biotechnology·Amélie Côté, François Shareck
Dec 3, 2004·Applied and Environmental Microbiology·Dirk SchwartzWolfgang Wohlleben
Feb 10, 2009·Applied and Environmental Microbiology·Hanna KontkanenJohanna Buchert
Jan 31, 2021·Extremophiles : Life Under Extreme Conditions·Xin ChangBaojuan Wang
Sep 18, 1997·Applied and Environmental Microbiology·P SommerF Götz

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