Engineering of microheterogeneity-resistantp-hydroxybenzoate hydroxylase fromPseudomonas fluorescens

Autor:	Kor H. Kalk, Wim G. J. Hol, Galina Obmolova, Arie de Kok, Klaus Eschrich, Willem J. H. van Berkel, Andrea Mattevi, Adrie H. Westphal
Rok vydání:	1990
Předmět:	Models Molecular Protein Conformation Thiol-reactivity DNA Mutational Analysis Molecular Sequence Data Mutant Oligonucleotides Biophysics Pseudomonas fluorescens Biochemistry chemistry.chemical_compound Structural Biology Pseudomonas Genetics Cloning Molecular Hydrogen peroxide Site-directed mutagenesis Protein-engineering Molecular Biology p-Hydroxybenzoate hydroxylase chemistry.chemical_classification Base Sequence biology Sulfhydryl Reagents Mutagenesis Cell Biology 4-Hydroxybenzoate-3-Monooxygenase biology.organism_classification Enzyme chemistry Pseudomonadales Crystallization Pseudomonadaceae
Zdroj:	FEBS Letters. 277:197-199
ISSN:	0014-5793
DOI:	10.1016/0014-5793(90)80843-8
Popis:	By site-directed mutagenesis, Cys-116 was converted to Ser-116 in p-hydroxybenzoate hydroxylase (EC 1.14.13.2) from Pseudomonas fluorescens. In contrast to wild-type enzyme, the C116S mutant is no longer susceptible to oxidation by hydrogen peroxide and shows no reactivity towards 5,5'-dithiobis(2-nitrobenzoate). Crystals of the C116S mutant are isomorphous with the crystal form of wild-type enzyme. A difference electron density confirms the mutation made.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a94db1cd0c6108057c2d7520c3c97025 https://doi.org/10.1016/0014-5793(90)80843-8 Zobrazit plný text záznamu Plný text