1379401-08-7Relevant academic research and scientific papers
Characterisation of the l-Cystine β-Lyase PatB from Phaeobacter inhibens: An Enzyme Involved in the Biosynthesis of the Marine Antibiotic Tropodithietic Acid
Dickschat, Jeroen S.,Rinkel, Jan,Klapschinski, Tim,Petersen, J?rn
, p. 2260 - 2267 (2017)
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.
Epidithiol formation by an unprecedented twin carbon-sulfur lyase in the gliotoxin pathway
Scharf, Daniel H.,Chankhamjon, Pranatchareeya,Scherlach, Kirstin,Heinekamp, Thorsten,Roth, Martin,Brakhage, Axel A.,Hertweck, Christian
, p. 10064 - 10068 (2012)
Two in one go: The elucidation of a key step in the biosynthesis of gliotoxin, the infamous virulence factor of the human pathogen Aspergillus fumigatus, provides insight into the formation of an epidithiol. Isolation of a bis(cysteine) S-conjugate from a ΔgliI mutant and in vitro studies show that GliI concomitantly cleaves two C-S bonds, along with the formation of ammonia and pyruvate (see scheme). Copyright
