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11.8
-
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
353.5
-
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
0.089
-
H20S mutant protein, pH 8.0, 25°C
0.099
-
H20A mutant protein, pH 8.0, 25°C
0.132
-
Y290F mutant protein, pH 8.0, 25°C
0.171
-
Y290S mutant protein, pH 8.0, 25°C
0.41
-
in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C
0.79
-
in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C
4.07
-
wild type protein, pH 8.0, 25°C
4.07
-
in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C
0.089
-
H20S variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.099
-
H20A variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.132
-
Y290F variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.171
-
Y290S variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
4
-
wild-type BphI, steady-state kinetic parameter, pH 8.0, 25°C
4.07
-
wild-type BphI, steady-state kinetic parameter, pH 8.0, 25°C
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0.38
-
wild type enzyme, with 0.5 mM Co2+, at pH 8.0 and 25°C
3.32
-
mutant enzyme R70K, with 0.5 mM Co2+, at pH 8.0 and 25°C
0.0044
-
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
0.013
-
Y290F mutant protein, pH 8.0, 25°C
0.013
-
Y290S mutant protein, pH 8.0, 25°C
0.089
-
wild type protein, pH 8.0, 25°C
0.089
-
in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C
0.158
-
in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C
0.222
-
H20A mutant protein, pH 8.0, 25°C
0.228
-
H20S mutant protein, pH 8.0, 25°C
0.013
-
Y290F variant of BphI, app. Km-value, steady-state kinetic parameter, pH 8.0, 25°C
0.013
-
Y290F variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.013
-
Y290S variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.089
-
wild-type BphI, app. Km-value, steady-state kinetic parameter, pH 8.0, 25°C
0.089
-
wild-type BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.222
-
H20A variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
0.228
-
H20S variant of BphI, steady-state kinetic parameter, pH 8.0, 25°C
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Probing the molecular basis of substrate specificity, stereospecificity, and catalysis in the class II pyruvate aldolase, BphI
2011
Baker, P.; Carere, J.; Seah, S.Y.
Biochemistry
50
3559-3569
Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes
2012
Baker, P.; Hillis, C.; Carere, J.; Seah, S.Y.K.
Biochemistry
51
1942-1952
Rational design of stereoselectivity in the class II pyruvate aldolase BphI
2012
Baker, P.; Seah, S.Y.K.
J. Am. Chem. Soc.
134
507-513
Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI
2012
Baker, P.; Carere, J.; Seah, S.Y.
Biochemistry
51
4558-4567
Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis
2013
Carere, J.; McKenna, S.E.; Kimber, M.S.; Seah, S.Y.
Biochemistry
52
3502-3511
Crystal structure of reaction intermediates in pyruvate class II aldolase: substrate cleavage, enolate stabilization, and substrate specificity
2012
Coincon, M.; Wang, W.; Sygusch, J.; Seah, S.Y.
J. Biol. Chem.
287
36208-36221
Show all BRENDA pathways known for (4S)-4-hydroxy-2-oxopentanoate
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