OXIDATIVE ENZYMES OF BACTERIAL SPORE EXTRACTS 



147 



>ilO: 



50 



25 



glucose 



/ 



-/- 



/ 





o^' 



.o^^ 



'6-0-" 



_ pyruvate 

 ■ o2KG 

 gluconate- 



t 



W 



ribose,arabinose 

 encl,HDF^F-6-P,F-l-f?F 



30 60 90 120 



Minutes 



Fig. 4. Oxidate capacity of spore extracts. See legend Fig. 3 for details. 

 Substrates were added at a level of 5 ^mole/ml. DPN was added to flasks 

 containing glucose and pyruvate; TPN to flasks containing gluconate and 

 2KG. All others received both TPN and DPN. 



explained by the presence of an active pyruvate-oxidizing system in the ex- 

 tract. When pyruvate oxidation is suppressed (Edwaros et al, 1956) by the 

 addition of the thiamine antagonist, Bis-1, 3-beta ethylhexyl-5-methyl amino 

 hexahydropyrimidine (W-1435), higher recoveries of pyruvate are ob- 

 served from glucose oxidation. 



The study of carbohydrate metabolism by microorganisms over the past 

 two decades has revealed a number of diverse pathways by which pyruvate 

 can be formed from glucose (Gunsalus et al, 1955). The three major path- 

 ways for this are outlined in Fig. 6. The historical and widely distributed 

 Embden-Meyerhoif pathways of glycolysis operate in lactobacilli, strepto- 

 cocci and members of the coli-aerogenes group. However, in obligate aerobes 

 and in some faculative aerobes, such as pseudomonads and acetocbacter, 

 carbohvdrate oxidation follows different pathways. The first alternate path- 

 way is the hexose monophosphate (HMP) oxidative route, which diverges 

 at the level of G-6P; the 6-phospho— gluconate (6-P-G) in converted to pyru- 



