Heterotrophic fixation of carbon dioxide by extracts of Nocardia corallina

Catabolic Pathways of Coryneforms, Nocardias, and Mycobacteria

“…enzymes that facilitate replen ishment of the Krebs cycle by generation of four-carbon dicarboxylic acids, have also been demonstrated. Phosphoenolpyruvate carboxykinase (Be 4.1.1.32) has been reported in Arthrobacter globiformis (23), Arthrobacter pyridinolis (92), Arthrobacter crystallopoietes (92), and Nocardia corallina (12). In A. pyridinolis and A. crystallopoietes, a gluconeogenic rather than anaplerotic role for the enzyme is consistent with the finding of considerably higher levels in ma1ate-than in hexose-grown cells (92).…”

“…In A. pyridinolis and A. crystallopoietes, a gluconeogenic rather than anaplerotic role for the enzyme is consistent with the finding of considerably higher levels in ma1ate-than in hexose-grown cells (92). In N. corallina, phosphoenolpyruvate carboxykinase was found by Baugh et al (12) to be dependent upon sulfhydryl groups for its activity and to exhibit a nucleotide specifi city similar to that for the activity in eukaryotes. Activity of the malic enzyme (BC 1.1.1.40) has been reported in both A. pyridinolis and A. crystallopoietes, in which the enzyme appears to serve a synthetic rather than an anaplerotic role (92).…”

Characterization of phosphoenolpyruvate carboxykinase from Corynebacterium glutamicum

“…In contrast to other prokaryotic PEP carboxykinases, the enzyme from C. glutamicum did not use ADP as cosubstrate, but was completely dependent on the presence of IDP, which is the common nucleotide observed for the enzyme from eukaryotes [8][9][10][11]. The g m for the various substrates is in the same range as observed for other PEP carboxykinases.…”

“…The g m for the various substrates is in the same range as observed for other PEP carboxykinases. Also the dependence on divalent manganese ions for full activity has been reported for several other enzymes [8][9][10][11].…”

“…184 One of the enzymes could be PEP carboxykinase, which catalyzes the ADP or IDP dependent carboxylation of PEP to OAA. PEP carboxykinase from various eukaryotic sources has been studied, but reports on PEP carboxykinase activity in bacteria have been sporadic [8,9]. PEP carboxykinase has been observed in Arthrobacter, Escherichia coli, Nocardia, Salmonella and very recently in Anaerobiospirillum, but has not yet been reported in C. glutamicum [8][9][10][11].…”