A catalase-peroxidase for oxidation of β-lactams to their (R)-sulfoxides.

Sanger, Shefali and Pal, Mohan and Moon, Lomary S and Jolly, R S (2012) A catalase-peroxidase for oxidation of β-lactams to their (R)-sulfoxides. Bioresource technology, 115. pp. 102-10. ISSN 1873-2976

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Abstract

In this communication we report for the first time a biocatalytic method for stereoselective oxidation of β-lactams, represented by penicillin-G, penicillin-V and cephalosporin-G to their (R)-sulfoxides. The method involves use of a bacterium, identified as Bacillus pumilis as biocatalyst. The enzyme responsible for oxidase activity has been purified and characterized as catalase-peroxidase (KatG). KatG of B. pumilis is a heme containing protein showing characteristic heme spectra with soret peak at 406 nm and visible peaks at 503 and 635 nm. The major properties that distinguish B. pumilis KatG from other bacterial KatGs are (i) it is a monomer and contains one heme per monomer, whereas KatGs of other bacteria are dimers or tetramers and have low heme content of about one per dimer or two per tetramer and (ii) its 12-residue, N-terminal sequence obtained by Edman degradation did not show significant similarity with any of known KatGs.

Item Type:	Article
Additional Information:	Copyright of this article belongs to Elsevier Science.
Uncontrolled Keywords:	Catalase–peroxidase;β-Lactam; Bacillus pumilis; KatG; Biocatalyzed sulfoxidation
Subjects:	Q Science > QH Natural history > QH301 Biology QH301 Biology
Depositing User:	Dr. K.P.S.Sengar
Date Deposited:	23 Jan 2013 09:19
Last Modified:	09 Jan 2015 11:24
URI:	http://crdd.osdd.net/open/id/eprint/1284

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