Ontology highlight
ABSTRACT:
SUBMITTER: Moore TC
PROVIDER: S-EPMC3911174 | biostudies-literature | 2014 Feb
REPOSITORIES: biostudies-literature
Moore Theodore C TC Mera Paola E PE Escalante-Semerena Jorge C JC
Journal of bacteriology 20131213 4
ATP:co(I)rrinoid adenosyltransferase (ACAT) enzymes convert vitamin B12 to coenzyme B12. EutT is the least understood ACAT. We report the purification of EutT to homogeneity and show that, in vitro, free dihydroflavins drive the adenosylation of cob(II)alamin bound to EutT. Results of chromatography analyses indicate that EutT is dimeric in solution, and unlike other ACATs, EutT catalyzes the reaction with sigmoidal kinetics indicative of positive cooperativity for cob(II)alamin. Maximal EutT ac ...[more]