4.1.3.39: 4-hydroxy-2-oxovalerate aldolase
This is an abbreviated version!
For detailed information about 4-hydroxy-2-oxovalerate aldolase, go to the full flat file.
Word Map on EC 4.1.3.39
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4.1.3.39
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hydratase
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meta-cleavage
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catechols
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4-oxalocrotonate
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2-hydroxymuconic
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2,3-dioxygenase
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2-hydroxypenta-2,4-dienoate
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putida
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biphenyls
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semialdehyde
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dioxygenase
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extradiol
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enol
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tautomerase
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polychlorinated
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ethylbenzene
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meta-pathway
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isofunctional
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stearothermophilus
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xylf
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propionaldehyde
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aldolases
- 4.1.3.39
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hydratase
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meta-cleavage
- catechols
- 4-oxalocrotonate
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2-hydroxymuconic
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2,3-dioxygenase
- 2-hydroxypenta-2,4-dienoate
- putida
- biphenyls
- semialdehyde
- dioxygenase
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extradiol
-
enol
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tautomerase
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polychlorinated
- ethylbenzene
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meta-pathway
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isofunctional
- stearothermophilus
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xylf
- propionaldehyde
- aldolases
Reaction
Synonyms
4-hydroxy-2-ketovalerate aldolase, 4-hydroxy-2-ketovalerate aldolase-aldehyde dehydrogenase (acylation), BphI, class II pyruvate aldolase BphI, DmpFG, HOA, HsaF, MhpE, pyruvate aldolase
ECTree
4.1.3.39 4-hydroxy-2-oxovalerate aldolaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 4.1.3.39 - 4-hydroxy-2-oxovalerate aldolase
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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
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?
pyruvate + succinic semialdehyde
(4RS)-4-hydroxy-2-oxoheptane-1,7-dioate
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racemic product
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?
(S)-4-hydroxy-2-oxohexanoate
propanal + pyruvate
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?
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
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?
4-hydroxy-2-oxovalerate
acetaldehyde + pyruvate
physiological substrate
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?
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
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?
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
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?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
enzyme acts stereospecifically on the L-enantiomer
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?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
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last but one step in meta-cleavage pathway for catechol degradation
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?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
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the enzyme utilizes the L-(S)-isomer or the racemate
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?
4-hydroxy-2-oxovalerate
pyruvate + acetaldehyde
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last but one step in meta-cleavage pathway for catechol degradation
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?
pyruvate + glycolaldehyde
4,5-dihydroxy-2-oxo-pentanoic acid
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?
additional information
?
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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
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?
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
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?
additional information
?
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BphJ forms a heterotetrameric complex with BphI that channels aldehydes produced in the aldol cleavage reaction to the dehydrogenase via a molecular tunnel
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?
additional information
?
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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
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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
?
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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
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?
additional information
?
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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
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?
additional information
?
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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
?
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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
?
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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
?
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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
?
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substrate specificity, substrate docking into the active site and modeling, binding structures, overview
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?
additional information
?
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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
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?
additional information
?
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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
?
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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
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?
additional information
?
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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
?
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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
?
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substrate specificity, substrate docking into the active site and modeling, binding structures, overview
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?
