Phosphotriesterase: an enzyme in search of its natural substrate

Autor:	F M, Raushel, H M, Holden
Rok vydání:	2000
Předmět:	Insecticides Organophosphorus Compounds Aryldialkylphosphatase Molecular Sequence Data Esterases Amino Acid Sequence Cholinesterase Inhibitors Protein Structure Tertiary Substrate Specificity
Zdroj:	Advances in enzymology and related areas of molecular biology. 74
ISSN:	0065-258X
Popis:	The bacterial PTE is able to catalyze the hydrolysis of a wide range of organophosphate nerve agents. The active site has been shown to consist of a unique binuclear metal center that has evolved to deliver hydroxide to the site of bond cleavage. The reaction rate for the hydrolysis of activated substrates such as paraoxon is limited by product release or an associated protein conformational change.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::7ae1bf4acb66e9fd3e6c7b90b28116f8 https://pubmed.ncbi.nlm.nih.gov/10800593 Zobrazit plný text záznamu