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. 2000 Oct;182(19):5462–5469. doi: 10.1128/jb.182.19.5462-5469.2000

TABLE 1.

Acetyl-CoA and propionyl-CoA carboxylase activitiesa in wild-type and accA mutant strains

Fraction Acetyl-CoA carboxylase
Propionyl-CoA carboxylase
Total activity (mU) Sp act (mU/mg of protein) Total activity (mU) Sp act (mU/mg of protein)
Wild type 22.3 1.0 69.0 3.1
accA mutant 12.3 0.6 60.9 3.0
a

The acetyl-CoA and propionyl-CoA carboxylase activities were determined with acetyl-CoA and propionyl-CoA as substrates from the rate of malonyl-CoA and methylmalonyl-CoA formations, respectively. The total and specific activities were expressed as means of triplicate enzyme assays.