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Characterisation of the l ‐Cystine β‐Lyase PatB from Phaeobacter inhibens : An Enzyme Involved in the Biosynthesis of the Marine Antibiotic Tropodithietic Acid
Author(s) -
Dickschat Jeroen S.,
Rinkel Jan,
Klapschinski Tim,
Petersen Jörn
Publication year - 2017
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201700358
Subject(s) - biochemistry , lyase , enzyme , biosynthesis , cystine , heterologous expression , chemistry , escherichia coli , recombinant dna , biology , cysteine , gene
The l ‐cystine β‐lyase from Phaeobacter inhibens is involved in the biosynthesis of the sulfur‐containing antibiotic tropodithietic acid. The recombinant enzyme was obtained by heterologous expression in Escherichia coli and biochemically characterised by unambiguous chemical identification of the products formed from the substrate l ‐cystine, investigation of the substrate spectrum, determination of the enzyme kinetics, sequence alignment with closely related homologues and site‐directed mutagenesis to identify a highly conserved lysine residue that is critical for functionality. PatB from P. inhibens is a new member of the small group of characterised l ‐cystine β‐lyases and the first example of an enzyme with such an activity that is required for the biosynthesis of an antibiotic. A comparison of PatB to previously reported enzymes with l ‐cystine β‐lyase activity from bacteria and plants is given.