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2006-09-02 18:08:54 · 2 answers · asked by shobana5bio 1 in Science & Mathematics Biology

2 answers

Metalloenzymes contain metals that are tightly bound, always isolated together with the protein, removing the metal ion from them cannot be done without destroying their structure and usually the metal ion is in the active site and taking part in the catalysis.

Non-metalloenzymes which are activated by metal ions do not bind so tightly the metal ions. Thus they can be isolated without the specific ions present and usually you can remove these ions from an enzyme-ion complex without disturbing the enzyme's structure. The metal ion usually will not be in the active site but bind at a different position and induce a conformational change in the enzyme that increases its activity.

2006-09-02 22:43:29 · answer #1 · answered by bellerophon 6 · 0 0

metal activated needs metal added to it, metalloenzyme contains metal

2006-09-02 22:28:07 · answer #2 · answered by John S 2 · 0 0

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