ISSN:
1573-4943
Keywords:
Alcohol dehydrogenase
;
interaction
;
europium
;
activation
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1020607818690
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