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Biochemistry of coenzyme B12-dependent glycerol and diol dehydratases and organization of the encoding genes.

Authors
Type
Published Article
Journal
FEMS microbiology reviews
Publication Date
Volume
22
Issue
5
Pages
553–566
Identifiers
PMID: 9990728
Source
Medline

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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