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Titolo:
STRUCTURE-FUNCTION STUDIES OF HUMAN AROMATASE
Autore:
CHEN SU; ZHOU DJ; SWIDEREK KM; KADOHAMA N; OSAWA Y; HALL PF;
Indirizzi:
CITY HOPE NATL MED CTR,BECKMAN RES INT,DIV IMMUNOL DUARTE CA 91010 MED FDN BUFFALO INC,RES INST BUFFALO NY 14203 UNIV NEW S WALES,DEPT ENDOCRINOL KENSINGTON NSW 2033 AUSTRALIA
Titolo Testata:
Journal of steroid biochemistry and molecular biology
fascicolo: 4-6, volume: 44, anno: 1993,
pagine: 347 - 356
SICI:
0960-0760(1993)44:4-6<347:SSOHA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ENCODING HUMAN AROMATASE; CRYSTAL-STRUCTURE; SEQUENCE-ANALYSIS; CYTOCHROME-P-450; CDNA; EXPRESSION; CELLS; AROMATIZATION; ESTROGEN; OXYGEN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
33
Recensione:
Indirizzi per estratti:
Citazione:
S.U. Chen et al., "STRUCTURE-FUNCTION STUDIES OF HUMAN AROMATASE", Journal of steroid biochemistry and molecular biology, 44(4-6), 1993, pp. 347-356

Abstract

Site-directed mutagenesis experiments have been carried out to determine the structure-function relationship of human aromatase. By sequence comparison, the region in aromatase that corresponds to the distal helix of cytochrome P-450cam has been identified to be Gln-298 to Val-313. Eight aromatase mutants with changes in this region, i.e. C299A, E302L, P308F, D309N, D309A, T310S, T310C, and S312C, have been generated using a mammalian cell stable-expression system. The results from site-directed mutagenesis studies indicate that the region containing Gln-298 to Val-313 is indeed a very important part of the active site ofaromatase. The catalytic properties of P308F, D309N, and D309A have been examined in detail and are discussed. Active site-directed labeling is also an important approach to investigate the structure-function relationship of aromatase. HPLC-linked electrospray mass spectrometry is indicated as a useful technique for the characterization of active site-directed probe-modified enzyme. The mass spectral analysis of aromatase suggests that aromatase is glycosylated.

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Documento generato il 30/11/20 alle ore 06:53:35