Skip to main content
. Author manuscript; available in PMC: 2012 Nov 15.
Published in final edited form as: Biochemistry. 2011 Oct 13;50(45):9724–9737. doi: 10.1021/bi2012788

Table 5.

Specific activities of the biotin carboxylase domain mutants for the oxamate induced decarboxylation of oxaloacetatea.

kcat
(min−1)b
% wild-
type rate
wild-type 9.03 ± 0.04 (100)
E218A 0.42 ± 0.01 4
E218Q 0.59 ± 0.01 6
K245Q 2.01 ± 0.01 22
E305A 3.28 ± 0.07 36
E305Q 1.27 ± 0.02 14
E305D 7.45 ± 0.05 82
R301Q 6.0 ± 0.1 66
R301K 5.67 ± 0.07 63
R353K 4.23 ± 0.09 47
R353M 5.8 ± 0.2 64
E305A/K1119Q NAc ---
R353M/K1119Q NA ---
a

Reaction conditions: 50 mM Bis-Tris, 25 mM Tricine, 25 mM glycine (pH 7.5), 25° C, 1 mM oxamate, 0.95 mM oxaloacetate, 0.25 mM acetyl-CoA.

b

Number of determinations = 3, error reported is standard deviations of 3 trials

c

NA = No activity detected.