The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450).

The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Research Abstract Details 

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The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Abstract Text:

Y Nitahara,K Kishimoto,Y Yabusaki,O Gotoh,Y Yoshida,T Horiuchi,Y Aoyama,

The amino acid residues affecting the function of rat sterol 14-demethylase P450 (CYP51) were examined by means of point mutation. Forty-five mutants with respect to 27 amino acid sites were constructed and expressed in Escherichia coli. Substitution of highly conserved Y131, E369, R372, or R382 decreased the expression of CYP51 protein, indicating some structural importance of these residues. Substitution of H314, T315, or S316 caused considerable effects on the catalytic activity, and T315 was identified as the "conserved threonine" of CYP51. H314 was important for maintenance of the activity of CYP51 and was a characteristic residue of this P450, because the position corresponding to this residue is occupied by an acidic amino acid in most other P450 species. A144 was identified as a residue affecting the interaction of CYP51 with ketoconazole. Substitution of A144 with I, which occupies the corresponding position in fungal CYP51, enhanced the ketoconazole susceptibility of rat CYP51 with little change in the catalytic activity, indicating an important role of this residue in determination of the ketoconazole susceptibility of CYP51. Alteration of the catalytic activity was caused by the substitution at some other sites, whereas substitution of a few highly conserved amino acids caused little alteration of the activity of CYP51.

The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Publishing Authors By Initials

Y Nitahara,K Kishimoto,Y Yabusaki,O Gotoh,Y Yoshida,T Horiuchi,Y Aoyama,

For similar investigative techniques: genetic techniques: sequence alignment research abstracts see: investigative techniques: genetic techniques: sequence alignment research

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The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Journal Published:

PUBLICATION TYPE: Journal Article

Journal: Journal of biochemistry

VOLUME: 129

Page Numbers: 761-8

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: May

YEAR: 2001

The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Information

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LANGUAGE: eng

NlmUniqueID: 376600

The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Keywords Mesh Terms:

KEYWORDS: Sequence Alignment

MESH TERMS: physiology

Chemical & Substance for Abstract: The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450). Information

Substance Name: lanosterol 14 alpha-demethylase

Registry Number: EC 1.14.13.70

Grant and Affiliation Information for The amino acid residues affecting the activity and azole susceptibility of rat CYP51 (sterol 14-demethylase P450).

AFFILIATION: Department of Bioengineering, Faculty of Engineering, Soka University, Hachioji, Tokyo 192-8577, Japan. aoyama@t.soka.ac.jp

Country: Japan

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MEDLINETA: J Biochem

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