Spectroscopic studies reveal details of substrate-induced conformational changes distant from the active site in isopenicillin N synthase

Autor:	Patrick Rabe, Carla C. Walla, Noelle K. Goodyear, Jordan Welsh, Rebecca Southwart, Ian Clifton, James D.S. Linyard, Anthony Tumber, Tim D.W. Claridge, William K. Myers, Christopher J. Schofield
Rok vydání:	2022
Předmět:	Protein Conformation Iron Electron Spin Resonance Spectroscopy Cell Biology Penicillins Nitric Oxide Biochemistry Substrate Specificity Oxygen Catalytic Domain Oxygenases Thiazolidines Ferrous Compounds Oxidoreductases Molecular Biology
Zdroj:	The Journal of biological chemistry. 298(9)
ISSN:	1083-351X
Popis:	Isopenicillin N synthase (IPNS) catalyzes formation of the β-lactam and thiazolidine rings of isopenicillin N from its linear tripeptide l-δ-(α-aminoadipoyl)-l-cysteinyl-d-valine (ACV) substrate in an iron- and dioxygen (O
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f147457c265dd7cf4d7010eea4ecf4a2 https://pubmed.ncbi.nlm.nih.gov/35835215 Zobrazit plný text záznamu