The Journal of General and Applied Microbiology
Online ISSN : 1349-8037
Print ISSN : 0022-1260
ISSN-L : 0022-1260
OXIDATIVE DECARBOXYLATION OF 6-PHOSPHOGLUCONATE IN LEUCONOSTOC MESENTEROIDES B07
II. PURIFICATION AND PROPERTIES OF A NEW ENZYME CATALYZING DECARBOXYLATION OF 2-KETO-6-PHOSPHOGLUCONATE
SHIGETAKA YASHIMAKAKUO KITAHARA
Author information
JOURNAL FREE ACCESS

1969 Volume 15 Issue 2 Pages 169-180

Details
Abstract
Leuconostoc mesenteroides B07, a typical heterolactic fermenting coccus, contains a new enzyme catalyzing the decarboxylation of 2-keto-6-phosphogluconate.
Basic properties of 2-keto-6-phosphogluconate decarboxylase were studied and decarboxylation product was isolated and identified as ribulose 5-phosphate.
It is postulated that, in this organism, 6-phosphogluconate may be oxidized to 2-keto-6-phosphogluconate by an NAD-linked dehydrogenase (not decarboxylating) (EC 1.1.1.43) and, thereafter, ribulose 5-phosphate and CO2 are formed by enzymatic decarboxylation.
Content from these authors
© The Microbiology Research Foundation
Previous article Next article
feedback
Top