Autor:	P D, Parshin, A A, Pometun, U A, Martysuk, S Yu, Kleymenov, D L, Atroshenko, E V, Pometun, S S, Savin, V I, Tishkov
Rok vydání:	2020
Předmět:	Acetone Kinetics Structure-Activity Relationship Histidine Oligopeptides Thermobifida Recombinant Proteins Mixed Function Oxygenases Substrate Specificity
Zdroj:	Biochemistry. Biokhimiia. 85(5)
ISSN:	1608-3040
Popis:	Phenylacetone monooxygenase (EC 1.14.13.92, PAMО) catalyzes oxidation of ketones with molecular oxygen and NADPH with the formation of esters. PAMО is a promising enzyme for biotechnological processes. In this work, we generated genetic constructs coding for PAMO from Thermobifida fusca, containing N- or C-terminal His
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=pmid________::ef8d3233e004b8e3389c16708c2f4056 https://pubmed.ncbi.nlm.nih.gov/32571187 Zobrazit plný text záznamu Full text from SpringerLink