Mutual conversion of fatty‐acid substrate specificity by a single amino‐acid exchange at position 527 in P‐450Cm2 and P‐450Alk3A

The two eukaryotic fatty‐acid hydroxylases P‐450Cm2 and P‐450Alk3A, which represent CYP52A4 variants naturally occurring in the yeast Candida maltosa, were characterized with respect to their substrate specificity. Whereas P‐450Cm2 was found to catalyse lauric acid ω‐hydroxylation with greater effic...

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Veröffentlicht in:	European journal of biochemistry 1998-09, Vol.256 (2), p.398-403
Hauptverfasser:	Zimmer, Thomas, Scheller, Ulrich, Takagi, Masamichi, Schunck, Wolf‐Hagen
Format:	Artikel
Sprache:	eng
Schlagworte:	active site Amino Acid Sequence Binding Sites - genetics Candida - enzymology Candida maltosa Cytochrome P-450 Enzyme System - chemistry cytochrome P‐450 Fatty Acids - metabolism fatty‐acid substrate specificity Hydroxylation Lauric Acids - metabolism Mixed Function Oxygenases - chemistry Molecular Sequence Data Mutagenesis, Site-Directed - genetics Palmitic Acid - metabolism Recombinant Fusion Proteins - genetics Sequence Alignment site‐directed mutagenesis Substrate Specificity
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