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Journal of Bacteriology, April 2004, p. 2328-2339, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2328-2339.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

A New Amidohydrolase from Bordetella or Alcaligenes Strain FB188 with Similarities to Histone Deacetylases

Christian Hildmann,1,{dagger} Milena Ninkovic,1,{dagger} Rüdiger Dietrich,1,{dagger} Dennis Wegener,1 Daniel Riester,1 Thomas Zimmermann,2 Olwen M. Birch,2 Christine Bernegger,2 Peter Loidl,3 and Andreas Schwienhorst1*

Abteilung fuer Molekulare Genetik und Praeparative Molekularbiologie, Institut fuer Mikrobiologie und Genetik, D-37077 Goettingen, Germany,1 Lonza AG, Walliser Werke, CH-3930 Visp, Switzerland,2 Department of Molecular Biology, University of Innsbruck, A-6020 Innsbruck, Austria3

Received 28 April 2003/ Accepted 11 December 2003

The full-length gene encoding the histone deacetylase (HDAC)-like amidohydrolase (HDAH) from Bordetella or Alcaligenes (Bordetella/Alcaligenes) strain FB188 (DSM 11172) was cloned using degenerate primer PCR combined with inverse-PCR techniques and ultimately expressed in Escherichia coli. The expressed enzyme was biochemically characterized and found to be similar to the native enzyme for all properties examined. Nucleotide sequence analysis revealed an open reading frame of 1,110 bp which encodes a polypeptide with a theoretical molecular mass of 39 kDa. Interestingly, peptide sequencing disclosed that the N-terminal methionine is lacking in the mature wild-type enzyme, presumably due to the action of methionyl aminopeptidase. Sequence database searches suggest that the new amidohydrolase belongs to the HDAC superfamily, with the closest homologs being found in the subfamily assigned acetylpolyamine amidohydrolases (APAH). The APAH subfamily comprises enzymes or putative enzymes from such diverse microorganisms as Pseudomonas aeruginosa, Archaeoglobus fulgidus, and the actinomycete Mycoplana ramosa (formerly M. bullata). The FB188 HDAH, however, is only moderately active in catalyzing the deacetylation of acetylpolyamines. In fact, FB188 HDAH exhibits significant activity in standard HDAC assays and is inhibited by known HDAC inhibitors such as trichostatin A and suberoylanilide hydroxamic acid (SAHA). Several lines of evidence indicate that the FB188 HDAH is very similar to class 1 and 2 HDACs and contains a Zn2+ ion in the active site which contributes significantly to catalytic activity. Initial biotechnological applications demonstrated the extensive substrate spectrum and broad optimum pH range to be excellent criteria for using the new HDAH from Bordetella/Alcaligenes strain FB188 as a biocatalyst in technical biotransformations, e.g., within the scope of human immunodeficiency virus reverse transcriptase inhibitor synthesis.

* Corresponding author. Mailing address: Abteilung fuer Molekulare Genetik und Praeparative Molekularbiologie, Institut fuer Mikrobiologie und Genetik, Grisebachstr. 8, D-37077 Goettingen, Germany. Phone: 49-551-393822. Fax: 49-551-393805. E-mail: aschwie1{at}gwdg.de.

{dagger} C.H., M.N., and R.D. contributed equally to the data presented.

Journal of Bacteriology, April 2004, p. 2328-2339, Vol. 186, No. 8
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.8.2328-2339.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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