SUMMARY: -Aminopropan-2-ol is a component of vitamin B (Cooley, Ellis &Petrow, 1950) possessing the g-configuration (Wolf, Jones, Valiant &Folkers, 1950). X-Ray crystallography confirmed that the amino alcohol linked the substituted corrin and nucleotide-like ring systems (Hodgkin . 1956; Hodgkin, 1958).

The metabolic origin of the nitrogen atom of -aminopropan-2-ol in vitamin B was established using [N]--threonine, added to the growth medium of (Krasna, Rosenblum &Sprinson, 1957). It was suggested that the carbon skeleton of the aminopropanol moiety was also derived from threonine by decarboxylation, although this was not investigated. Direct decarboxylation of the amino acid has never been demonstrated, and neither the threonine nor threonine--phos-phate analogues of vitamin B serve as precursors of cobinamide in either or (Bernhauer &Wagner, 1961, 1962). The discovery of -threonine dehydrogenase (Neuberger &Tait, 1960, 1962) and -aminopropan-2-ol dehydrogenase activity (Turner, 1966; Dekker &Swain, 1968; Lowe &Turner, 1968) revived interest in the possibility that the free amino alcohol, formed from -threonine via aminoacetone, served as a precursor. The roles of -threonine and -aminopropan-2-ol in vitamin B biosynthesis by a Streptomyces strain were therefore investigated using C-labelled compounds.


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