Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes |
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Authors: | R Daniel TA Bobik G Gottschalk |
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Affiliation: | Institut für Mikrobiologie und Genetik der Georg-August-Universit?t, G?ttingen, Germany. rdaniel@gwdg.de |
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Abstract: | Glycerol and diol dehydratases exhibit a subunit composition of alpha 2 beta 2 gamma 2 and contain coenzyme B12 in the base-on form. The dehydratase reaction proceeds via a radical mechanism. The dehydratases are subject to reaction inactivation by the substrate glycerol which is caused by a cessation of the catalytic cycle because coenzyme B12 is not regenerated, instead 5'-deoxyadenosine and a catalytically inactive cobalamin are formed. The genetic organization of the dehydratase genes is quite similar in all organisms. Downstream of the dehydratase genes an open reading frame encoding a polypeptide of approximately 600 amino acids was identified which is apparently involved in the reactivation of suicide-inactivated enzyme. |
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