Vitamin B-12: Insights into biosynthesis's mount improbable

Raux-Deery, Evelyne and Schubert, Heidi L. and Roper, Jennifer M. and Wilson, Keith S. and Warren, Martin J. (1999) Vitamin B-12: Insights into biosynthesis's mount improbable. Bioorganic Chemistry, 27 (2). pp. 100-118. ISSN 0045-2068 . (The full text of this publication is not available from this repository)

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Official URL
http://dx.doi.org/10.1006/bioo.1998.1125

Abstract

The biosynthesis of the corrin ring component of cobalamin (vitamin B12) is reviewed with regard to how two separate though broadly similar pathways may have evolved. The more ancient "anaerobic" pathway is characterized by the early chelation of cobalt and the release of acetaldehyde whereas the "aerobic" pathway is characterized by an absolute dependency on molecular oxygen, the late chelation of cobalt and the release of acetic acid. Both pathways require the addition of 8 S-adenosyl-L-methionine-derived methyl groups to the periphery of the tetrapyrrole framework. The sequences of these enzymes reveal that they are clearly related, most likely having evolved from an ancestral methylase gene. The three-dimensional structure of one of these methyltransferases is highlighted and discussed in light of a common mechanism for this family of enzymes. Moreover, the aerobic and anaerobic chelatases are described and parallels with the chelatases found in heme and chlorophyll synthesis are drawn, (C) 1999 Academic Press.

Item Type: Article
Uncontrolled keywords: cobyrinic acid a,c-diamide complete genome sequence adenosyl-l-methionine cysg gene encodes x-ray structure uroporphyrinogen-iii methyltransferase pseudomonas-denitrificans salmonella-typhimurium cobalamin vitamin-b-12 escherichia-coli
Subjects: Q Science
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: Martin Warren
Date Deposited: 12 Oct 2009 08:34
Last Modified: 22 Apr 2014 14:36
Resource URI: http://kar.kent.ac.uk/id/eprint/11073 (The current URI for this page, for reference purposes)
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