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(4R)-4-hydroxy-2-oxopentanoate
acetaldehyde + pyruvate
-
-
-
-
r
(4S)-4-hydroxy-2-oxopentanoate
acetaldehyde + pyruvate
-
-
-
-
r
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
4-hydroxy-2-oxo-4-benzylbutanoate
benzaldehyde + pyruvate
-
-
-
?
4-hydroxy-2-oxo-isoheptanoate
isobutyraldehyde + pyruvate
-
-
-
?
4-hydroxy-2-oxoheptanoate
butyraldehyde + pyruvate
-
-
-
?
4-hydroxy-2-oxohexanoate
propionaldehyde + pyruvate
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
butyraldehyde + pyruvate
4-hydroxy-2-oxoheptanoate
-
-
-
-
r
hexaldehyde + pyruvate
4-hydroxy-2-oxononanoate
-
-
-
-
r
pentaldehyde + pyruvate
4-hydroxy-2-oxooctanoate
-
-
-
-
r
propionaldehyde + pyruvate
4-hydroxy-2-oxohexanoate
-
-
-
-
r
pyruvate + (R,S)-glyceraldehyde
?
-
-
-
?
pyruvate + acetaldehyde
(4S)-4-hydroxy-2-oxovalerate
-
-
-
-
?
pyruvate + acetaldehyde
(4S)-hydroxy-2-oxopentanoate
-
-
-
?
pyruvate + acetaldehyde
4-hydroxy-2-oxopentanoate
-
-
-
?
pyruvate + butyraldehyde
?
pyruvate + glycolaldehyde
4,5-dihydroxy-2-oxo-pentanoic acid
pyruvate + glycolaldehyde
?
-
-
-
?
pyruvate + isobutyraldehyde
?
pyruvate + pentaldehyde
?
-
-
-
?
pyruvate + propionaldehyde
?
pyruvate + succinic semialdehyde
(4RS)-4-hydroxy-2-oxoheptane-1,7-dioate
-
racemic product
-
?
pyruvate + succinic semialdehyde
?
-
-
-
-
?
additional information
?
-
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
-
-
-
-
?
4-hydroxy-2-oxohexanoate
propionaldehyde + pyruvate
-
-
-
?
4-hydroxy-2-oxohexanoate
propionaldehyde + pyruvate
-
-
-
?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate
-
-
?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate, the R and the S forms are both accommodated within the DmpG active site
-
-
?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate
-
-
?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate, the R and the S forms are both accommodated within the DmpG active site
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
-
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
step in a meta pathway
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
enzyme acts stereospecifically on the L-enantiomer
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
-
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
last but one step in meta-cleavage pathway for catechol degradation
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
the enzyme utilizes the L-(S)-isomer or the racemate
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
-
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
last but one step in meta-cleavage pathway for catechol degradation
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
-
-
-
?
pyruvate + butyraldehyde
?
-
-
-
?
pyruvate + butyraldehyde
?
-
-
-
-
?
pyruvate + butyraldehyde
?
-
-
-
?
pyruvate + glycolaldehyde
4,5-dihydroxy-2-oxo-pentanoic acid
-
-
-
?
pyruvate + glycolaldehyde
4,5-dihydroxy-2-oxo-pentanoic acid
-
-
-
-
?
pyruvate + isobutyraldehyde
?
-
-
-
?
pyruvate + isobutyraldehyde
?
-
-
-
-
?
pyruvate + isobutyraldehyde
?
-
-
-
?
pyruvate + propionaldehyde
?
-
-
-
?
pyruvate + propionaldehyde
?
-
-
-
-
?
pyruvate + propionaldehyde
?
-
-
-
?
additional information
?
-
HpaI is able to utilize aldehyde acceptors two to five carbons in length, shows broad specificity and has a preference for aldehydes containing longer linear alkyl chains or C2-OH substitutions. HpaI is able to bind 2-keto acids larger than pyruvate, and to utilize both pyruvate and 2-ketobutanoate as carbonyl donors in the aldol addition reaction. HpaI lacks stereospecific control producing racemic mixtures of 4-hydroxy-2-oxopentanoate from pyruvate and acetaldehyde
-
-
?
additional information
?
-
-
BphI is able to utilize aldehyde acceptors two to five carbons in length. BphI is able to bind 2-keto acids larger than pyruvate. BphI synthesizes only (4S)-4-hydroxy-2-oxopentanoate from pyruvate and acetaldehyde. BphI is also able to utilize acetaldehyde produced by the reduction of acetyl-CoA catalyzed by the associated aldehyde dehydrogenase, BphJ. This aldehyde is directly channeled from the dehydrogenase to the aldolase active sites, with an efficiency of 84%. The BphJ reductive deacylation reaction increases 4-fold when BphI is catalyzing the aldol addition reaction. The BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation
-
-
?
additional information
?
-
-
BphJ forms a heterotetrameric complex with BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel
-
-
?
additional information
?
-
BphI exhibits a compulsory order mechanism, with pyruvate binding first. BphI is able to utilize acetaldehyde produced by the reduction of acetyl-CoA catalyzed by the associated aldehyde dehydrogenase, BphJ. This aldehyde is directly channeled from the dehydrogenase to the aldolase active sites, with an efficiency of 84%. The BphJ reductive deacylation reaction increases 4fold when BphI is catalyzing the aldol addition reaction. The BphI-BphJ enzyme complex exhibits unique bidirectionality in substrate channeling and allosteric activation
-
-
?
additional information
?
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA, molecular channeling of substrate and intermediate
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA, product channeling mechanism
-
-
?
additional information
?
-
DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
-
-
?
additional information
?
-
substrate specificity, substrate docking into the active site and modeling, binding structures, overview
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA, product channeling mechanism
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, which acts on acetaldehyde to form acetyl-CoA, molecular channeling of substrate and intermediate
-
-
?
additional information
?
-
DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
-
-
?
additional information
?
-
substrate specificity, substrate docking into the active site and modeling, binding structures, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
additional information
?
-
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
-
-
-
?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate
-
-
?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
step in a meta pathway
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
-
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
last but one step in meta-cleavage pathway for catechol degradation
-
-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
last but one step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
-
the enzyme acts in an enzyme complex with the aldehyde dehydrogenase, EC 1.2.1.10, performs the final step in meta-cleavage pathway for catechol degradation
-
-
?
additional information
?
-
DmpFG is a bifunctional enzyme comprised of an aldolase subunit, DmpG, and a dehydrogenase subunit, DmpF. The aldehyde intermediate produced by the aldolase is channeled directly through a buried molecular channel in the protein structure from the aldolase to the dehydrogenase active site. Binding and channeling of alternative substrates in the enzyme DmpFG, molecular dynamics, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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0.012 - 0.013
(4R)-4-hydroxy-2-oxopentanoate
0.013 - 0.228
(4S)-4-hydroxy-2-oxopentanoate
88.6
(R,S)-glyceraldehyde
pH 8.0, 25°C
0.0048
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
0.0044 - 0.158
(S)-4-hydroxy-2-oxopentanoate
33.3 - 124.6
glycolaldehyde
16.8 - 136
propionaldehyde
73.8
Succinic semialdehyde
pH 8.0, 25°C
0.012
(4R)-4-hydroxy-2-oxopentanoate
-
Y290S mutant protein, pH 8.0, 25°C
0.013
(4R)-4-hydroxy-2-oxopentanoate
-
Y290F mutant protein, pH 8.0, 25°C
0.013
(4S)-4-hydroxy-2-oxopentanoate
-
Y290F mutant protein, pH 8.0, 25°C
0.013
(4S)-4-hydroxy-2-oxopentanoate
-
Y290S mutant protein, pH 8.0, 25°C
0.089
(4S)-4-hydroxy-2-oxopentanoate
-
wild type protein, pH 8.0, 25°C
0.222
(4S)-4-hydroxy-2-oxopentanoate
-
H20A mutant protein, pH 8.0, 25°C
0.228
(4S)-4-hydroxy-2-oxopentanoate
-
H20S mutant protein, pH 8.0, 25°C
0.0044
(S)-4-hydroxy-2-oxopentanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
0.089
(S)-4-hydroxy-2-oxopentanoate
-
in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C
0.158
(S)-4-hydroxy-2-oxopentanoate
-
in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C
62.9
acetaldehyde
pH 8.0, 25°C
64.2
acetaldehyde
-
wild type protein, pH 8.0, 25°C
64.28
acetaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
64.8
acetaldehyde
-
pH 8.0, 25°C
80.5
acetaldehyde
-
L89A mutant protein, pH 8.0, 25°C
13.4
Butyraldehyde
pH 8.0, 25°C
49.2
Butyraldehyde
-
L89A mutant protein, pH 8.0, 25°C
289
Butyraldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
323
Butyraldehyde
-
L87A mutant protein, pH 8.0, 25°C
33.3
glycolaldehyde
pH 8.0, 25°C
124.6
glycolaldehyde
-
pH 8.0, 25°C
124.6
glycolaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
24.8
pentaldehyde
-
L89A mutant protein, pH 8.0, 25°C
33.3
pentaldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
16.8
propionaldehyde
-
L87A mutant protein, pH 8.0, 25°C
32.9
propionaldehyde
pH 8.0, 25°C
40.2
propionaldehyde
-
L89A mutant protein, pH 8.0, 25°C
135.9
propionaldehyde
-
pH 8.0, 25°C
135.9
propionaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
136
propionaldehyde
-
wild type protein, pH 8.0, 25°C
11
pyruvate
-
aldol addition reaction with propionaldehyde, L89A mutant protein, pH 8.0, 25°C
13
pyruvate
-
aldol addition reaction with propionaldehyde, wild type protein, pH 8.0, 25°C
20.2
pyruvate
-
aldol addition reaction with propionaldehyde, L87A mutant protein, pH 8.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.131 - 0.17
(4R)-4-hydroxy-2-oxopentanoate
0.089 - 4.07
(4S)-4-hydroxy-2-oxopentanoate
5.6
(R,S)-glyceraldehyde
pH 8.0, 25°C
0.38
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C
0.41 - 4.07
(S)-4-hydroxy-2-oxopentanoate
0.86 - 205.4
acetaldehyde
0.26 - 132.5
Butyraldehyde
0.4 - 175.5
glycolaldehyde
0.29 - 358.4
propionaldehyde
64.9
Succinic semialdehyde
pH 8.0, 25°C
0.131
(4R)-4-hydroxy-2-oxopentanoate
-
Y290F mutant protein, pH 8.0, 25°C
0.17
(4R)-4-hydroxy-2-oxopentanoate
-
Y290S mutant protein, pH 8.0, 25°C
0.089
(4S)-4-hydroxy-2-oxopentanoate
-
H20S mutant protein, pH 8.0, 25°C
0.099
(4S)-4-hydroxy-2-oxopentanoate
-
H20A mutant protein, pH 8.0, 25°C
0.132
(4S)-4-hydroxy-2-oxopentanoate
-
Y290F mutant protein, pH 8.0, 25°C
0.171
(4S)-4-hydroxy-2-oxopentanoate
-
Y290S mutant protein, pH 8.0, 25°C
4.07
(4S)-4-hydroxy-2-oxopentanoate
-
wild type protein, pH 8.0, 25°C
0.41
(S)-4-hydroxy-2-oxopentanoate
in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 25°C
0.79
(S)-4-hydroxy-2-oxopentanoate
-
in the absence of NADH, in 100 mM HEPES pH 8.0, at 25°C
4.07
(S)-4-hydroxy-2-oxopentanoate
-
in the presence of NADH, in 100 mM HEPES pH 8.0, at 25°C
0.86
acetaldehyde
-
pH 8.0, 25°C
0.86
acetaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.86
acetaldehyde
-
wild type protein, pH 8.0, 25°C
0.94
acetaldehyde
-
L89A mutant protein, pH 8.0, 25°C
205.4
acetaldehyde
pH 8.0, 25°C
0.26
Butyraldehyde
-
L87A mutant protein, pH 8.0, 25°C
0.3
Butyraldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.64
Butyraldehyde
-
L89A mutant protein, pH 8.0, 25°C
132.5
Butyraldehyde
pH 8.0, 25°C
0.4
glycolaldehyde
-
pH 8.0, 25°C
0.4
glycolaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
175.5
glycolaldehyde
pH 8.0, 25°C
0.13
pentaldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.58
pentaldehyde
-
L89A mutant protein, pH 8.0, 25°C
0.29
propionaldehyde
-
L87A mutant protein, pH 8.0, 25°C
0.63
propionaldehyde
-
L89A mutant protein, pH 8.0, 25°C
1.79
propionaldehyde
-
pH 8.0, 25°C
1.79
propionaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
1.79
propionaldehyde
-
wild type protein, pH 8.0, 25°C
358.4
propionaldehyde
pH 8.0, 25°C
0.32
pyruvate
-
aldol addition reaction with propionaldehyde, L87A mutant protein, pH 8.0, 25°C
0.64
pyruvate
-
aldol addition reaction with propionaldehyde, L89A mutant protein, pH 8.0, 25°C
1.2
pyruvate
-
aldol addition reaction with propionaldehyde, wild type protein, pH 8.0, 25°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
10.4 - 14.1
(4R)-4-hydroxy-2-oxopentanoate
0.012 - 44.7
(4S)-4-hydroxy-2-oxopentanoate
0.063
(R,S)-glyceraldehyde
pH 8.0, 25°C
79.1
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
93.1
(S)-4-hydroxy-2-oxopentanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
0.00042 - 13.4
acetaldehyde
0.00079 - 9.9
Butyraldehyde
0.0037 - 5.27
glycolaldehyde
0.00001 - 0.00013
hexaldehyde
0.0005
Isobutyraldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.00033 - 0.0233
pentaldehyde
0.00673 - 13.2
propionaldehyde
0.5 - 22.5
Succinic semialdehyde
10.4
(4R)-4-hydroxy-2-oxopentanoate
-
Y290F mutant protein, pH 8.0, 25°C
14.1
(4R)-4-hydroxy-2-oxopentanoate
-
Y290S mutant protein, pH 8.0, 25°C
0.012
(4S)-4-hydroxy-2-oxopentanoate
-
R16K mutant protein, pH 8.0, 25°C
0.34
(4S)-4-hydroxy-2-oxopentanoate
-
H20S mutant protein, pH 8.0, 25°C
0.45
(4S)-4-hydroxy-2-oxopentanoate
-
H20A mutant protein, pH 8.0, 25°C
12.6
(4S)-4-hydroxy-2-oxopentanoate
-
Y290F mutant protein, pH 8.0, 25°C
13.4
(4S)-4-hydroxy-2-oxopentanoate
-
Y290S mutant protein, pH 8.0, 25°C
44.7
(4S)-4-hydroxy-2-oxopentanoate
-
wild type protein, pH 8.0, 25°C
0.00042
acetaldehyde
-
L87A mutant protein, pH 8.0, 25°C
0.00049
acetaldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.0117
acetaldehyde
-
L89A mutant protein, pH 8.0, 25°C
0.0134
acetaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.0134
acetaldehyde
-
wild type protein, pH 8.0, 25°C
3.3
acetaldehyde
pH 8.0, 25°C
13.4
acetaldehyde
-
pH 8.0, 25°C
0.00079
Butyraldehyde
-
L87A mutant protein, pH 8.0, 25°C
0.00104
Butyraldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.00219
Butyraldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.00219
Butyraldehyde
-
wild type protein, pH 8.0, 25°C
0.0129
Butyraldehyde
-
L89A mutant protein, pH 8.0, 25°C
2.19
Butyraldehyde
-
pH 8.0, 25°C
9.9
Butyraldehyde
pH 8.0, 25°C
0.0037
glycolaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
3.7
glycolaldehyde
-
pH 8.0, 25°C
5.27
glycolaldehyde
pH 8.0, 25°C
0.00001
hexaldehyde
-
L87A mutant protein, pH 8.0, 25°C
0.00001
hexaldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.00001
hexaldehyde
-
wild type protein, pH 8.0, 25°C
0.00013
hexaldehyde
-
L89A mutant protein, pH 8.0, 25°C
0.00033
pentaldehyde
-
L87A mutant protein, pH 8.0, 25°C
0.00047
pentaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.00047
pentaldehyde
-
wild type protein, pH 8.0, 25°C
0.0038
pentaldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.0233
pentaldehyde
-
L89A mutant protein, pH 8.0, 25°C
0.00673
propionaldehyde
-
L87A/L89A mutant protein, pH 8.0, 25°C
0.0132
propionaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.0132
propionaldehyde
-
wild type protein, pH 8.0, 25°C
0.0156
propionaldehyde
-
L89A mutant protein, pH 8.0, 25°C
0.0175
propionaldehyde
-
L87A mutant protein, pH 8.0, 25°C
10.9
propionaldehyde
pH 8.0, 25°C
13.2
propionaldehyde
-
pH 8.0, 25°C
0.0159
pyruvate
-
aldol addition reaction with propionaldehyde, L87A mutant protein, pH 8.0, 25°C
0.0587
pyruvate
-
aldol addition reaction with propionaldehyde, L89A mutant protein, pH 8.0, 25°C
0.0915
pyruvate
-
aldol addition reaction with propionaldehyde, wild type protein, pH 8.0, 25°C
0.5
Succinic semialdehyde
-
pH 8.0, 25°C
22.5
Succinic semialdehyde
pH 8.0, 25°C
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dimer
-
1 * 32500 + 1 * 37500, active unit is an enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE and crystal structure
dimer
-
1 * 32500 + 1 * 37500, active unit is an enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE and crystal structure
-
homodimer
2 * 38000, SDS-PAGE
homodimer
-
2 * 38000, SDS-PAGE
-
tetramer
-
2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE
tetramer
-
2 * 35000 + 2 * 40000, enzyme complex of aldehyde dehydrogenase and 4-hydroxy-2-ketovalerate aldolase, SDS-PAGE
-
additional information
-
enzyme complex structure analysis
additional information
-
the enzyme forms a heterodimer of 71 kDa with the aldehyde dehydrogenase, EC 1.2.1.10
additional information
-
the enzyme is encoded in the dmp operon with aldehyde dehydrogenase, EC 1.2.1.10, with which it forms an enzyme complex
additional information
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
additional information
-
the enzyme is encoded in the dmp operon with aldehyde dehydrogenase, EC 1.2.1.10, with which it forms an enzyme complex
-
additional information
-
the enzyme forms a heterodimer of 71 kDa with the aldehyde dehydrogenase, EC 1.2.1.10
-
additional information
-
enzyme complex structure analysis
-
additional information
-
DmpFG is a microbial enzyme comprised of two subunits DmpG and DmpF
-
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in complex with HsaG, sitting drop vapor diffusion method, using 18% (w/v) PEG 4000, 0.2 M MgCl2, 0.1 M Tris pH 8.5, 10% glycerol, and 10 mM sodium oxalate
purified enzyme complex of 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating), protein solution contains 9 mg/ml protein in 50 mM Tris-HCl, pH 7.4, 1 mM DTT, and 2 mM NAD+, mixing of equal volumes of 0.001 ml of protein and reservoir solutions, the latter contains 15% PEG 8000, 100 mM ammonium sulfate, and 100 mM PIPES, pH 7.5, 3 days, soaking of crystals in 5 mM samarium acetate and 0.25 mM PCMBS, X-ray diffraction structure determination and analysis at 2.1 A resolution
-
purified selenomethionine-labeled enzyme complex of 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating), protein solution contains 9 mg/ml protein in 50 mM Tris-HCl, pH 7.4, 1 mM DTT, and 2 mM NAD+, mixing of equal volumes of 0.001 ml of protein and reservoir solutions, the latter contains 18% PEG 8000, 100 mM ammonium sulfate, and 100 mM PIPES, pH 7.5, 3 days, crystals are used for microseeding, cryoprotection by soaking in mother liquor with 20% v/v 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 1.7 A resolution
-
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Powlowski, J.; Sahlman, L.; Shingler, V.
Purification and properties of the physically associated meta-cleavage pathway enzymes 4-hydroxy-2-ketovalerate aldolase and aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600
J. Bacteriol.
175
377-385
1993
Pseudomonas sp., Pseudomonas sp. CF 600
brenda
Manjasetty, B.A.; Croteau, N.; Powlowski, J.; Vrielink, A.
Crystallization and preliminary x-ray analysis of dmpFG-encoded 4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylating) from Pseudomonas sp. strain CF600
Acta Crystallogr. Sect. D
57
582-585
2001
Pseudomonas sp., Pseudomonas sp. CF 600
brenda
Manjasetty, B.A.; Powlowski, J.; Vrielink, A.
Crystal structure of a bifunctional aldolase-dehydrogenase: sequestering a reactive and volatile intermediate
Proc. Natl. Acad. Sci. USA
100
6992-6997
2003
Pseudomonas sp., Pseudomonas sp. CF 600
brenda
Platt, A.; Shingler, V.; Taylor, S.C.; Williams, P.A.
The 4-hydroxy-2-oxovalerate aldolase and acetaldehyde dehydrogenase (acylating) encoded by the nahM and nahO genes of the naphthalene catabolic plasmid pWW60-22 provide further evidence of conservation of meta-cleavage pathway gene sequences
Microbiology
141
2223-2233
1995
Pseudomonas putida (P51017)
brenda
Lee, S.J.; Ko, J.H.; Kang, H.Y.; Lee, Y.
Coupled expression of MhpE aldolase and MhpF dehydrogenase in Escherichia coli
Biochem. Biophys. Res. Commun.
346
1009-1015
2006
Escherichia coli
brenda
Wang, W.; Baker, P.; Seah, S.Y.
Comparison of two metal-dependent pyruvate aldolases related by convergent evolution: substrate specificity, kinetic mechanism, and substrate channeling
Biochemistry
49
3774-3782
2010
Paraburkholderia xenovorans, Paraburkholderia xenovorans LB400 (P51015), Escherichia coli (Q47098)
brenda
Baker, P.; Carere, J.; Seah, S.Y.
Probing the molecular basis of substrate specificity, stereospecificity, and catalysis in the class II pyruvate aldolase, BphI
Biochemistry
50
3559-3569
2011
Paraburkholderia xenovorans
brenda
Baker, P.; Carere, J.; Seah, S.Y.
Substrate specificity, substrate channeling, and allostery in BphJ: an acylating aldehyde dehydrogenase associated with the pyruvate aldolase BphI
Biochemistry
51
4558-4567
2012
Paraburkholderia xenovorans
brenda
Carere, J.; McKenna, S.E.; Kimber, M.S.; Seah, S.Y.
Characterization of an aldolase-dehydrogenase complex from the cholesterol degradation pathway of Mycobacterium tuberculosis
Biochemistry
52
3502-3511
2013
Mycobacterium tuberculosis (P9WMK5), Mycobacterium tuberculosis H37Rv (P9WMK5)
brenda
Smith, N.E.; Vrielink, A.; Attwood, P.V.; Corry, B.
Binding and channeling of alternative substrates in the enzyme DmpFG: a molecular dynamics study
Biophys. J.
106
1681-1690
2014
Pseudomonas sp. (P51016), Pseudomonas sp. CF 600 (P51016)
brenda