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Publication Abstract from PubMed

Cysteine is a semiessential amino acid and plays an important role in metabolism and protein structure and has also been applied in various industrial fields, such as pharmaceutical, food, cosmetic, and animal feed industries. Metabolic engineering studies have been conducted for the cysteine production through bacterial fermentation, but studies on the cysteine biosynthetic pathway in microorganisms are limited. We report the biochemical characteristics of cystathionine gamma-lyase from Bacillus cereus ATCC 14579 (BcCGL). We also determined the crystal structure of BcCGL in complex with the PLP cofactor and identified the substrate binding mode. We observed that the replacement of the conserved Glu321 residue to alanine showed increased activity by providing wider active site entrance and hydrophobic interaction for the substrate. We suggest that the structural differences of the alpha13-alpha14 region in CGL enzymes might determine the active site conformation.

Structural and Functional Characterization of Cystathionine gamma-lyase from Bacillus cereus ATCC 14579.,Sagong HY, Kim B, Joo S, Kim KJ J Agric Food Chem. 2020 Dec 23;68(51):15267-15274. doi: 10.1021/acs.jafc.0c06503., Epub 2020 Dec 10. PMID:33301683^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.