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Digitale Medien

Interaction of Eu3+ with Yeast Alcohol Dehydrogenase (1999)

Zhang, Ying-Xia ; Duan, Chun-Li ; Zhou, Hai-Meng

Springer

The protein journal 18 (1999), S. 97-101

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Details

ISSN: 1573-4943

Schlagwort(e): Alcohol dehydrogenase ; interaction ; europium ; activation

Quelle: Springer Online Journal Archives 1860-2000

Thema: Chemie und Pharmazie

Notizen: Abstract The activity of yeast alcohol dehydrogenase is markedly enhanced by Eu3+ ions. At pH 7.0 two binding constants for Eu3+, 1.0 × 10−2 and 2.0 × 10−3 μM, were obtained using a Scatchard plot. The presence of Zn2+ ions restricts the Eu3+-induced increase in the activity of yeast alcohol dehydrogenase. Studies on the tryptophan fluorescence of the enzyme in the absence and presence of Eu3+ or Zn2+ ions showed that Eu3+ affects tertiary or quaternary structures, which is consistent with its activation of the enzyme. The presence of Zn2+ reverses the conformational changes caused by Eu3+. Comparison of the effects of Eu3+ with Zn2+ for apo-yeast alcohol dehydrogenase indicates that their binding sites on the protein are different.

Materialart: Digitale Medien

URL: http://dx.doi.org/10.1023/A:1020607818690

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