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Information on EC 4.1.3.39 - 4-hydroxy-2-oxovalerate aldolase
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4.1.3.39 4-hydroxy-2-oxovalerate aldolaseIUBMB Comments
Requires Mn2+ for maximal activity . The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH . In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase [4,5].
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Word Map
- 4.1.3.39
-
hydratase
-
meta-cleavage
- catechols
- 4-oxalocrotonate
-
2-hydroxymuconic
-
2,3-dioxygenase
- 2-hydroxypenta-2,4-dienoate
- putida
- biphenyls
- semialdehyde
- dioxygenase
-
extradiol
-
enol
-
tautomerase
-
polychlorinated
- ethylbenzene
-
meta-pathway
-
isofunctional
- stearothermophilus
-
xylf
- propionaldehyde
- aldolases
The enzyme appears in viruses and cellular organisms
Synonyms
4-hydroxy-2-oxovalerate aldolase, 4-hydroxy-2-ketovalerate aldolase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-hydroxy-2-ketovalerate aldolase
4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylation)
BphI
DmpFG
HOA
HsaF
4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylation)
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4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylation)
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-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
-
-
-
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(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
rapid equilibrium random order mechanism
(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
active site structure, molecular channeling of substrate and intermediate
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(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
compulsory order mechanism, with pyruvate binding first
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(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
reaction mechanism
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(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
active site structure, molecular channeling of substrate and intermediate
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-
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PATHWAY SOURCE
PATHWAYS
KEGG
-
-
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SYSTEMATIC NAME
IUBMB Comments
4-hydroxy-2-oxopentanoate pyruvate-lyase (acetaldehyde-forming)
Requires Mn2+ for maximal activity [1]. The enzyme from the bacterium Pseudomonas putida is also stimulated by NADH [1]. In some bacterial species the enzyme forms a bifunctional complex with EC 1.2.1.10, acetaldehyde dehydrogenase (acetylating). The enzymes from the bacteria Burkholderia xenovorans and Thermus thermophilus also perform the reaction of EC 4.1.3.43, 4-hydroxy-2-oxohexanoate aldolase [4,5].
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CAS REGISTRY NUMBER
COMMENTARY
37325-52-3
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
pyruvate + acetaldehyde
(4S)-hydroxy-2-oxopentanoate
-
-
-
?
pyruvate + succinic semialdehyde
(4RS)-4-hydroxy-2-oxoheptane-1,7-dioate
-
racemic product
-
?
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
-
-
-
?
(S)-4-hydroxy-2-oxopentanoate
ethanal + 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
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-
?
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
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-
?
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
-
last but one step in meta-cleavage pathway for catechol degradation
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-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
the enzyme utilizes the L-(S)-isomer or the racemate
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-
?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
-
last but one step in meta-cleavage pathway for catechol degradation
-
-
?
pyruvate + glycolaldehyde
4,5-dihydroxy-2-oxo-pentanoic acid
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-
-
-
?
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
?
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-
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
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
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-
?
additional information
?
-
substrate specificity, substrate docking into the active site and modeling, binding structures, overview
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-
?
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-4-hydroxy-2-oxohexanoate
propanal + 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
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
-
BphI is activated in the presence of the BphJ cofactor, NADH, by about 5fold
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Ni2+
additional information
additional information
not stimulated by Ca2+, Cd2+, Zn2+, and Cu2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
BphJ
-
the aldehyde dehydrogenase BphJ coordinates the catalytic activity of BphI through allostery rather than through aldehyde channeling
-
HsaG
the enzyme is active only in complex with the dehydrogenase HsaG
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0048
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 0.4 mM NADH, 1 mM MgCl2, at 25°C
0.012
(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
64.28
acetaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
124.6
glycolaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
135.9
propionaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.38
(S)-4-hydroxy-2-oxohexanoate
in 100 mM HEPES (pH 8.0), 1 mM MgCl2, at 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
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
0.4
glycolaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
1.79
propionaldehyde
at 25°C with 120 microg of BphI, 2 mM MnCl2 and 100 mM pyruvate
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