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The final acylation step in aromatic dithiolopyrrolone biosyntheses: Identification and characterization of the first bacterium N-benzoyltransferase from Saccharothrix algeriensis NRRL B-24137

Paper ID Volume ID Publish Year Pages File Format Full-Text
16882 42620 2015 7 PDF Available
Title
The final acylation step in aromatic dithiolopyrrolone biosyntheses: Identification and characterization of the first bacterium N-benzoyltransferase from Saccharothrix algeriensis NRRL B-24137
Abstract

•We identified a benzoyltransferase involved in aromatic dithiolopyrrolone biosyntheses.•This enzyme showed high selectivity to aromatic acyl-CoA groups.•Neither product nor transfers were detected for linear acyl-CoA groups.•Two N-acyltransferases, at least, are involved in dithiolopyrrolone pathway in Sa. algeriensis.•Holothin-derivative productions are limited by substrate availability more than the activities.

The last step in the biosynthesis of dithiolopyrrolone antibiotics was thought to involve the transfer of acyl group from acyl-CoA to pyrrothine/holothin core. In Saccharothrix algeriensis NRRL B-24137, two acyltransferases, an acetyltransferase and a benzoyltransferase were proposed to catalyze this step. We have previously identified, in Sa. algeriensis genome, two open read frames, actA and actB patiently encoded these enzymes. This study focuses primarily on the characterization of the protein encoded by actA. After cloning and expressing of actA in Escherichia coli BL21, the recombinant protein encoded by actA was purified. Selectivity of ActA for pyrrothine/holothin as substrate and different acyl-CoA as co-substrate was evaluated using two acyls-groups, linear and aromatic. The enzyme was shown to prefer aromatic groups over linear groups as donor group; further neither product nor transfer was observed for linear groups. Therefore ActA has been determined to be a pyrrothine/holothin N-benzoyltransferase which can either pyrrothine (Km of 72 μM) or holothin (Km of 129.5 μM) as substrates and benzoyl-CoA (Km of 348.65 and 395.28 μM) as co-substrates for pyrrothine and holothin, respectively. The optimum pH and temperature has been shown to be 8, 40 °C, respectively. ActA is the first enzyme characterized as N-benzoyltransferase in bacteria.

Keywords
Pyrrothine; Holothin; N-benzoyltransferase; Benzoyl-pyrrothine; Benzoyl-holothin; Saccharothrix algeriensis
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The final acylation step in aromatic dithiolopyrrolone biosyntheses: Identification and characterization of the first bacterium N-benzoyltransferase from Saccharothrix algeriensis NRRL B-24137
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Publisher
Database: Elsevier - ScienceDirect
Journal: Enzyme and Microbial Technology - Volume 72, May 2015, Pages 35–41
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us