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. 2005 Feb;187(4):1415–1425. doi: 10.1128/JB.187.4.1415-1425.2005

TABLE 3.

Molecular and catalytic properties of l-malyl-CoA lyase from R. capsulatus

Property Characteristic or value
Reaction catalyzed Acetyl-CoA + glyoxylate ↔ l-malyl-CoA Propionyl-CoA + glyoxylate ↔ erythro-β-methylmalyl-CoA
Specific activity (μmol min−1 mg−1)
    l-malyl-CoA cleavage 18 ± 1
    erythro-β-Methylmalyl-CoA cleavage 5.7 ± 0.2
    Acetyl-CoA + glyoxylate condensation 37 ± 1a (25b, 15c)
    Propionyl-CoA + glyoxylate condensation 28b
Apparent Km value (mM)
    Malyl-CoA 0.015 ± 0.003d
    erythro-β-Methylmalyl-CoA 0.021 ± 0.003d
    Acetyl-CoA 0.14 ± 0.01a
Native molecular mass (kDa) 195 ± 20
Subunit molecular mass (kDa) 34
Suggested compostion α6
N-terminal sequence SFRTQPP
Influence of divalent cations (mM) Mn2+ (5), 100%; Mg2+ (5), 50%; Co2+ (5), 45%; Zn2+ (1), 33%; Ca2+ (1), 33%; no addition, 33%
Inhibitor (mM) EDTA (0.5), <5% activity
a

Determined by coupling malyl-CoA formation to citrate synthase (l-malyl-CoA hydrolysis) with Mg2+.

b

Activity from HPLC assay with Mn2+.

c

Activity from HPLC assay with Mg2+.

d

Determined by following the cleavage reaction.