TABLE 7.

The defect for each of the attenuated but nonlethal mutants can be explained by a change of the permitted stoichiometry between oxygen, TAG, and biomass for in vitro growth in lipid-only media in high levels of oxygen^a

Gene removed from the reaction set in each KO mutant	Enzymatic activityb	Reaction catalyzed	Optimal rate of biomass production (1/h)	Import rates during optimal growth (fmol/h-BU)
				TAG	Oxygen
WT	NA	NA	0.034	0.003	0.272
tpi/Rv1438	Triose-phosphate isomerase	DHAP ⇔ G3P	0.023	0.005	0.272
pgk/Rv1437	Phosphoglycerate kinase	ADP + 13PDG ⇔ ATP + 3PG	0.013	0.007	0.272
nuoA/Rv3145, nuoB/Rv3146, nuoD/Rv3148, nuoE/Rv3149, nuoF/Rv3150, nuoG/Rv3151, nuoH/Rv3152, nuoI/Rv3153, nuoJ/Rv3154, nuoK/Rv3155, nuoL/Rv3156, nuoM/Rv3157, nuoN/Rv3158	Type I NADH dehydrogenase, NuoA-N	MK + NADH → MKH2 + NAD + 4 H	0.025	0.003	0.272
glcB/Rv1837c	Malate synthase	ACCOA + GLX → COA + MAL	0.010	0.007	0.272
gap/Rv1436	Glyceraldehyde-3-phosphate dehydrogenase	NAD + PI + G3P ⇔ NADH + 13PDG	0.013	0.007	0.272
eno/Rv1023	Phosphopyruvate hydratase	2PG ⇔ PEP	0.010	0.007	0.272
ctaB/Rv1451, Rv1456c, ctaE/Rv2193, qcrC/Rv2194, qcrA/Rv2195, qcrB/Rv2196, ctaC/Rv2200c, fixB/Rv3028c, fixA/Rv3029c, ctaD/Rv3043c	aa3-type cytochrome c oxidase, ctaCDE AND cytochrome bc1	0.5 O2 + 2 HEME-FE2 → 6 H + 2 HEME-FE3	0.019	0.002	0.272

^aAttenuated mutants were identified by hypothesis testing using GranSim-CBM data. The nonlethality of the mutants was determined by CBM in lipid-only media. NA, not applicable.

^bAnnotation is provided in reference 45.