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