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Information on EC 4.1.3.39 - 4-hydroxy-2-oxovalerate aldolase and Organism(s) Paraburkholderia xenovorans and UniProt Accession P51015

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.39 4-hydroxy-2-oxovalerate aldolase
IUBMB 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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This record set is specific for:
Paraburkholderia xenovorans
UNIPROT: P51015
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Word Map
The taxonomic range for the selected organisms is: Paraburkholderia xenovorans
The enzyme appears in selected viruses and cellular organisms
Synonyms
4-hydroxy-2-oxovalerate aldolase, 4-hydroxy-2-ketovalerate aldolase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
class II pyruvate aldolase BphI
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(S)-4-hydroxy-2-oxopentanoate = acetaldehyde + pyruvate
show the reaction diagram
compulsory order mechanism, with pyruvate binding first
-
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].
CAS REGISTRY NUMBER
COMMENTARY hide
37325-52-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4R)-4-hydroxy-2-oxopentanoate
acetaldehyde + pyruvate
show the reaction diagram
-
-
-
-
r
(4S)-4-hydroxy-2-oxopentanoate
acetaldehyde + pyruvate
show the reaction diagram
-
-
-
-
r
(S)-4-hydroxy-2-oxopentanoate
ethanal + pyruvate
show the reaction diagram
-
-
-
-
?
butyraldehyde + pyruvate
4-hydroxy-2-oxoheptanoate
show the reaction diagram
-
-
-
-
r
hexaldehyde + pyruvate
4-hydroxy-2-oxononanoate
show the reaction diagram
-
-
-
-
r
pentaldehyde + pyruvate
4-hydroxy-2-oxooctanoate
show the reaction diagram
-
-
-
-
r
propionaldehyde + pyruvate
4-hydroxy-2-oxohexanoate
show the reaction diagram
-
-
-
-
r
pyruvate + acetaldehyde
(4S)-4-hydroxy-2-oxovalerate
show the reaction diagram
-
-
-
-
?
pyruvate + butyraldehyde
?
show the reaction diagram
-
-
-
-
?
pyruvate + glycolaldehyde
4,5-dihydroxy-2-oxo-pentanoic acid
show the reaction diagram
-
-
-
-
?
pyruvate + isobutyraldehyde
?
show the reaction diagram
-
-
-
-
?
pyruvate + propionaldehyde
?
show the reaction diagram
-
-
-
-
?
pyruvate + succinic semialdehyde
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADH
-
BphI is activated in the presence of the BphJ cofactor, NADH, by about 5fold
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-ketobutanoate
-
-
2-ketopentanoate
-
-
4-methyl-2-oxopentanoate
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
BphJ
-
the aldehyde dehydrogenase BphJ coordinates the catalytic activity of BphI through allostery rather than through aldehyde channeling
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.012 - 0.013
(4R)-4-hydroxy-2-oxopentanoate
0.013 - 0.228
(4S)-4-hydroxy-2-oxopentanoate
0.089 - 0.158
(S)-4-hydroxy-2-oxopentanoate
64.2 - 80.5
acetaldehyde
49.2 - 323
Butyraldehyde
124.6
glycolaldehyde
-
pH 8.0, 25°C
24.8 - 33.3
pentaldehyde
16.8 - 136
propionaldehyde
11 - 20.2
pyruvate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.131 - 0.17
(4R)-4-hydroxy-2-oxopentanoate
0.089 - 4.07
(4S)-4-hydroxy-2-oxopentanoate
0.79 - 4.07
(S)-4-hydroxy-2-oxopentanoate
0.86 - 0.94
acetaldehyde
0.26 - 0.64
Butyraldehyde
0.4
glycolaldehyde
-
pH 8.0, 25°C
0.13 - 0.58
pentaldehyde
0.29 - 1.79
propionaldehyde
0.32 - 1.2
pyruvate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
10.4 - 14.1
(4R)-4-hydroxy-2-oxopentanoate
0.012 - 44.7
(4S)-4-hydroxy-2-oxopentanoate
0.00042 - 13.4
acetaldehyde
0.00079 - 2.19
Butyraldehyde
3.7
glycolaldehyde
-
pH 8.0, 25°C
0.00001 - 0.00013
hexaldehyde
0.00033 - 0.0233
pentaldehyde
0.00673 - 13.2
propionaldehyde
0.0159 - 0.0915
pyruvate
0.5
Succinic semialdehyde
-
pH 8.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.34
2-ketobutanoate
-
pH 8.0, 25°C
1.09
2-ketopentanoate
-
pH 8.0, 25°C
2.71
4-methyl-2-oxopentanoate
-
pH 8.0, 25°C
0.21
glyoxylate
-
pH 8.0, 25°C
0.55
pyruvate
-
pH 8.0, 25°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
polychlorinated biphenyl degradation pathway
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H20A
-
decrease in kcat/Km value
H20S
-
decrease in kcat/Km value
L87A
-
3-fold reduction in kcat/Km
L87A/L89A
-
improved specificity for aldehydes at least four carbons in length
L89A
-
kcat/Km similar to wild type
R16A
-
no detectable activity
R16K
-
increased Km value for 4-hydroxy-2-oxopentanoate
Y290F
-
lower kcat value
Y290S
-
lower kcat value
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21(lambdaDE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Escherichia coli (Q47098), Paraburkholderia xenovorans, Paraburkholderia xenovorans LB400 (P51015)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team