Threonine degradation by Serratia marcescens.

Abstract:

:The wild strain of Serratia marcescens rapidly degraded threonine and formed aminoacetone in a medium containing glucose and urea. Extracts of this strain showed high threonine dehydrogenase and "biosynthetic" threonine deaminase activities, but no threonine aldolase activity. Threonine dehydrogenase-deficient strain Mu-910 was selected among mutants unable to grow on threonine as the carbon source. This strain did not form aminoacetone from threonine, but it slowly degraded threonine. Strain D-60, deficient in both threonine dehydrogenase and threonine deaminase, was derived from strain Mu-910 and barely degraded threonine. A glycine-requiring strain derived from the wild strain grew in minimal medium containing threonine as the glycine source, whereas a glycine-requiring strain derived from strain Mu-910 did not grow. This indicates that threonine dehydrogenase participates in glycine formation from threonine (via alpha-amino-beta-ketobutyrate) as well as in threonine degradation to aminoacetone.

journal_name

J Bacteriol

journal_title

Journal of bacteriology

authors

Komatsubara S,Murata K,Kisumi M,Chibata I

doi

10.1128/JB.135.2.318-323.1978

subject

Has Abstract

pub_date

1978-08-01 00:00:00

pages

318-23

issue

2

eissn

0021-9193

issn

1098-5530

journal_volume

135

pub_type

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