PMID: 8599535Mar 1, 1996Paper

Pentalenolactone-insensitive glyceraldehyde-3-phosphate dehydrogenase from Streptomyces arenae is closely related to GAPDH from thermostable eubacteria and plant chloroplasts

Archives of Microbiology
K U FröhlichD Mecke

Abstract

Streptomyces arenae produces the antibiotic pentalenolactone, a highly specific inhibitor of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). During the phase of pentalenolactone production, S. arenae expresses a pentalenolactone-insensitive GAPDH isoform; otherwise, a pentalenolactone-sensitive form is expressed. The gene of the pentalenolactone-insensitive GAPDH was cloned and sequenced. Regulatory elements typical for genes encoding antibiotic resistance and production are localized upstream and downstream of the open reading frame. No expression of pentalenolactone-insensitive GAPDH was detected in Streptomyces lividans transformed with the gene. In Escherichia coli, the gene was expressed from an induced lac promoter. Amino-terminal sequencing of the heterologously expressed GAPDH proved its identity with pentalenolactone-insensitive GAPDH from S. arenae. Sequence comparisons with GAPDH from other organisms showed a close relationship to GAPDH of plant chloroplasts, of other gram-positive bacteria, and of thermophilic gram-negative bacteria. Pentalenolactone-insensitive GAPDH differs from all closely related GAPDHs only in a few residues, none of which are directly involved in catalysis or substrate binding. The total ami...Continue Reading

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Citations

May 7, 2010·Journal of Industrial Microbiology & Biotechnology·Eric Cundliffe, Arnold L Demain
Oct 19, 2007·The Journal of Biological Chemistry·Zheng YouGerwald Jogl
May 31, 2002·Bioscience, Biotechnology, and Biochemistry·Yoshimitsu HamanoHaruo Seto
Sep 9, 2020·European Journal of Medicinal Chemistry·Andrea GalbiatiPaola Conti
Jul 30, 2014·The Journal of Organic Chemistry·Steven A LopezK N Houk

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