Work

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

Year: 1998

Type: article

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.

Source: FEMS Microbiology Reviews

DOI: 10.1016/s0168-6445(98)00021-7

Authors: Rolf Daniel, Thomas A. Bobik, Gerhard Gottschalk

Institutions: University of Göttingen, University of Florida

Language: English

Topic: Porphyrin Metabolism and Disorders

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: Deutsche Forschungsgemeinschaft

OpenAlex ID: W2149616487