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Volumn 539, Issue 1, 2013, Pages 87-91
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7,8- and 5,8-linoleate diol synthases support the heterolytic scission of oxygen-oxygen bonds by different amide residues
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Author keywords
Heme peroxidase P450 class III; Mutagenesis site specific; Oxygenation mechanism; Oxylipin biosynthesis; Prostacyclin synthase
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Indexed keywords
ALANINE;
ALCOHOL;
AMIDE;
ASPARAGINE;
CYTOCHROME P450;
DIOXYGENASE;
GLUTAMINE;
HYDROPEROXIDE;
ISOMERASE;
LINOLEIC ACID;
OXYGEN;
AMINO ACID SUBSTITUTION;
ARTICLE;
ASPERGILLUS FUMIGATUS;
ASPERGILLUS TERREUS;
BIOINFORMATICS;
CHEMICAL BOND;
CHEMICAL INTERACTION;
CHEMICAL STRUCTURE;
ENZYME ACTIVITY;
NONHUMAN;
OXYGEN TRANSPORT;
OXYGENATION;
PRIORITY JOURNAL;
HEME PEROXIDASE;
MUTAGENESIS SITE-SPECIFIC;
OXYGENATION MECHANISM;
OXYLIPIN BIOSYNTHESIS;
P450 CLASS III;
PROSTACYCLIN SYNTHASE;
AMIDES;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ASCOMYCOTA;
ASPERGILLUS FUMIGATUS;
COMPUTATIONAL BIOLOGY;
CONSERVED SEQUENCE;
MODELS, MOLECULAR;
OXYGEN;
OXYGENASES;
PROTEIN STRUCTURE, SECONDARY;
ASPERGILLUS FUMIGATUS;
GAEUMANNOMYCES GRAMINIS;
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EID: 84884955239
PISSN: 00039861
EISSN: 10960384
Source Type: Journal
DOI: 10.1016/j.abb.2013.09.010 Document Type: Article |
Times cited : (15)
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References (27)
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