Structural and Functional Characterization of Cystathionine γ-lyase from Bacillus cereus ATCC 14579

Autor:	Hye-Young Sagong, Seongjoon Joo, Kyung-Jin Kim, Bongsang Kim
Rok vydání:	2020
Předmět:	Alanine chemistry.chemical_classification biology Bacillus cereus Active site General Chemistry biology.organism_classification Cystathionine beta synthase Amino acid Protein structure Enzyme Biochemistry chemistry biology.protein General Agricultural and Biological Sciences Cysteine
Zdroj:	Journal of Agricultural and Food Chemistry. 68:15267-15274
ISSN:	1520-5118 0021-8561
DOI:	10.1021/acs.jafc.0c06503
Popis:	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 γ-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 α13-α14 region in CGL enzymes might determine the active site conformation.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::bb20f7ef9046c0c47c59a7a8829cf83e https://doi.org/10.1021/acs.jafc.0c06503 Zobrazit plný text záznamu