No abstract

None of the remaining 67 isolates utilized aminoacetone when washed suspensions of the bacteria grown on L-threonine were incubated under standard conditions (Higgins et al., 1968). It was concluded that none of the 83 isolates metabolized L-threonine via aminoacetone. Additional work (S. C. Bell & J. M. Turner, unpublished work) suggests that all the selected isolates possessing high L-threonine 3-dehydrogenase activity catabolize 2-amino-3-oxobutyrate by cleavage to glycine and acetyl-CoA, as shown for a species of Arthrobacter(McGi1vray &Morris, 1969). It seems unlikely that any commonly occurring bacterium degrades L-threonine by a route involving aminoacetone as an obligatory intermediate.