BRENDA - Enzyme Database
show all sequences of 4.1.3.43

Characterization of an aldolase-dehydrogenase complex that exhibits substrate channeling in the polychlorinated biphenyls degradation pathway

Baker, P.; Pan, D.; Carere, J.; Rossi, A.; Wang, W.; Seah, S.Y.K.; Biochemistry 48, 6551-6558 (2009)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
Organism
Structure
BphJ
15fold increased activity
Paraburkholderia xenovorans
Cloned(Commentary)
Cloned (Commentary)
Organism
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yielded soluble proteins
Paraburkholderia xenovorans
Inhibitors
Inhibitors
Commentary
Organism
Structure
Cd2+
56.0% activity at 0.1 mM and 5.4% activity at 1 mM chloride salt
Paraburkholderia xenovorans
Co2+
19.3% activity at 0.1 mM and 18.3% activity at 1 mM chloride salt
Paraburkholderia xenovorans
Mg2+
3.4% activity at 0.1 mM and 14.8% activity at 1 mM chloride salt
Paraburkholderia xenovorans
Mn2+
100% activity at 0.1 mM and 1 mM chloride salt
Paraburkholderia xenovorans
Ni2+
2.6% activity at 0.1 mM and 17.5% activity at 1 mM chloride salt
Paraburkholderia xenovorans
oxalate
-
Paraburkholderia xenovorans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
presence of NAD+, NADP+, NADH or CoA leads to an at least 5fold reduction in the Km for 4-hydroxy-2-oxopentanoate
Paraburkholderia xenovorans
0.18
-
4-hydroxy-2-oxohexanoate
pH 8.0, 25C
Paraburkholderia xenovorans
0.22
-
4-hydroxy-2-oxopentanoate
pH 8.0, 25C
Paraburkholderia xenovorans
0.35
-
4-hydroxy-2-oxoheptanoate
pH 8.0, 25C
Paraburkholderia xenovorans
7.5
-
oxaloacetate
pH 8.0, 25C
Paraburkholderia xenovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI
Paraburkholderia xenovorans
37000
-
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
Paraburkholderia xenovorans
140000
-
native molecular mass of the purified BphI-BphJ-complex, estimated by gel filtration
Paraburkholderia xenovorans
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(S)-4-hydroxy-2-oxohexanoate
Paraburkholderia xenovorans
-
propanal + pyruvate
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Paraburkholderia xenovorans
P51015
-
-
Purification (Commentary)
Purification (Commentary)
Organism
BphI and BphJ form a stable complex as they bind and coelute from Ni2+-NTA column, although only BphJ has the histidine tag. After purification, the N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
Paraburkholderia xenovorans
Storage Stability
Storage Stability
Organism
purified enzyme can be stored at -80C, without loss of activity for at least 12 months
Paraburkholderia xenovorans
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
(S)-4-hydroxy-2-oxohexanoate
-
721615
Paraburkholderia xenovorans
propanal + pyruvate
-
-
-
?
4-hydroxy-2-oxoheptanoate
-
721615
Paraburkholderia xenovorans
pyruvate + butanal
-
-
-
?
4-hydroxy-2-oxohexanoate
-
721615
Paraburkholderia xenovorans
pyruvate + propionaldehyde
-
-
-
?
4-hydroxy-2-oxopentanoate
-
721615
Paraburkholderia xenovorans
pyruvate + acetaldehyde
-
-
-
?
Oxaloacetate
-
721615
Paraburkholderia xenovorans
Pyruvate + CO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI
Paraburkholderia xenovorans
Synonyms
Synonyms
Commentary
Organism
BphI
-
Paraburkholderia xenovorans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
2 and 5fold increases in kcat observed when BphI reaction is conducted in the presence of NAD+ and NADH
Paraburkholderia xenovorans
0.63
-
4-hydroxy-2-oxoheptanoate
pH 8.0, 25C
Paraburkholderia xenovorans
3.8
-
4-hydroxy-2-oxohexanoate
pH 8.0, 25C
Paraburkholderia xenovorans
4.1
-
4-hydroxy-2-oxopentanoate
pH 8.0, 25C
Paraburkholderia xenovorans
16.5
-
oxaloacetate
pH 8.0, 25C
Paraburkholderia xenovorans
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00093
-
oxalate
pH 8.0, 25C
Paraburkholderia xenovorans
Activating Compound (protein specific)
Activating Compound
Commentary
Organism
Structure
BphJ
15fold increased activity
Paraburkholderia xenovorans
Cloned(Commentary) (protein specific)
Commentary
Organism
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yielded soluble proteins
Paraburkholderia xenovorans
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Cd2+
56.0% activity at 0.1 mM and 5.4% activity at 1 mM chloride salt
Paraburkholderia xenovorans
Co2+
19.3% activity at 0.1 mM and 18.3% activity at 1 mM chloride salt
Paraburkholderia xenovorans
Mg2+
3.4% activity at 0.1 mM and 14.8% activity at 1 mM chloride salt
Paraburkholderia xenovorans
Mn2+
100% activity at 0.1 mM and 1 mM chloride salt
Paraburkholderia xenovorans
Ni2+
2.6% activity at 0.1 mM and 17.5% activity at 1 mM chloride salt
Paraburkholderia xenovorans
oxalate
-
Paraburkholderia xenovorans
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
0.00093
-
oxalate
pH 8.0, 25C
Paraburkholderia xenovorans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
presence of NAD+, NADP+, NADH or CoA leads to an at least 5fold reduction in the Km for 4-hydroxy-2-oxopentanoate
Paraburkholderia xenovorans
0.18
-
4-hydroxy-2-oxohexanoate
pH 8.0, 25C
Paraburkholderia xenovorans
0.22
-
4-hydroxy-2-oxopentanoate
pH 8.0, 25C
Paraburkholderia xenovorans
0.35
-
4-hydroxy-2-oxoheptanoate
pH 8.0, 25C
Paraburkholderia xenovorans
7.5
-
oxaloacetate
pH 8.0, 25C
Paraburkholderia xenovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI
Paraburkholderia xenovorans
37000
-
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
Paraburkholderia xenovorans
140000
-
native molecular mass of the purified BphI-BphJ-complex, estimated by gel filtration
Paraburkholderia xenovorans
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
(S)-4-hydroxy-2-oxohexanoate
Paraburkholderia xenovorans
-
propanal + pyruvate
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
BphI and BphJ form a stable complex as they bind and coelute from Ni2+-NTA column, although only BphJ has the histidine tag. After purification, the N-terminal histidine tag of BphJ is proteolytically cleaved by thrombin digestion
Paraburkholderia xenovorans
Storage Stability (protein specific)
Storage Stability
Organism
purified enzyme can be stored at -80C, without loss of activity for at least 12 months
Paraburkholderia xenovorans
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
(S)-4-hydroxy-2-oxohexanoate
-
721615
Paraburkholderia xenovorans
propanal + pyruvate
-
-
-
?
4-hydroxy-2-oxoheptanoate
-
721615
Paraburkholderia xenovorans
pyruvate + butanal
-
-
-
?
4-hydroxy-2-oxohexanoate
-
721615
Paraburkholderia xenovorans
pyruvate + propionaldehyde
-
-
-
?
4-hydroxy-2-oxopentanoate
-
721615
Paraburkholderia xenovorans
pyruvate + acetaldehyde
-
-
-
?
Oxaloacetate
-
721615
Paraburkholderia xenovorans
Pyruvate + CO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI
Paraburkholderia xenovorans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
2 and 5fold increases in kcat observed when BphI reaction is conducted in the presence of NAD+ and NADH
Paraburkholderia xenovorans
0.63
-
4-hydroxy-2-oxoheptanoate
pH 8.0, 25C
Paraburkholderia xenovorans
3.8
-
4-hydroxy-2-oxohexanoate
pH 8.0, 25C
Paraburkholderia xenovorans
4.1
-
4-hydroxy-2-oxopentanoate
pH 8.0, 25C
Paraburkholderia xenovorans
16.5
-
oxaloacetate
pH 8.0, 25C
Paraburkholderia xenovorans
General Information
General Information
Commentary
Organism
metabolism
enzyme forms a bifunctional complex with EC 1.2.1.87 (BphJ), propanal dehydrogenase (CoA-propanoylating) and is part of the polychlorinated biphenyl degradation pathway
Paraburkholderia xenovorans
General Information (protein specific)
General Information
Commentary
Organism
metabolism
enzyme forms a bifunctional complex with EC 1.2.1.87 (BphJ), propanal dehydrogenase (CoA-propanoylating) and is part of the polychlorinated biphenyl degradation pathway
Paraburkholderia xenovorans
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
highest catalytic efficiency of BphI occurs when NADH is present, which is 25fold higher than the value obtained without nucleotides
Paraburkholderia xenovorans
1.8
-
4-hydroxy-2-oxoheptanoate
pH 8.0, 25C
Paraburkholderia xenovorans
2.2
-
oxaloacetate
pH 8.0, 25C
Paraburkholderia xenovorans
18.6
-
4-hydroxy-2-oxopentanoate
pH 8.0, 25C
Paraburkholderia xenovorans
21.1
-
4-hydroxy-2-oxohexanoate
pH 8.0, 25C
Paraburkholderia xenovorans
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
highest catalytic efficiency of BphI occurs when NADH is present, which is 25fold higher than the value obtained without nucleotides
Paraburkholderia xenovorans
1.8
-
4-hydroxy-2-oxoheptanoate
pH 8.0, 25C
Paraburkholderia xenovorans
2.2
-
oxaloacetate
pH 8.0, 25C
Paraburkholderia xenovorans
18.6
-
4-hydroxy-2-oxopentanoate
pH 8.0, 25C
Paraburkholderia xenovorans
21.1
-
4-hydroxy-2-oxohexanoate
pH 8.0, 25C
Paraburkholderia xenovorans
Other publictions for EC 4.1.3.43
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Synonyms
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
721659
Baker
Protein-protein interactions a ...
Thermus thermophilus
Biochemistry
51
1942-1952
2012
-
-
1
-
1
-
-
16
-
-
7
-
-
4
-
-
1
-
-
-
-
-
4
1
1
-
-
1
15
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
-
-
16
-
-
7
-
-
-
-
1
-
-
-
-
4
1
-
-
1
15
-
-
-
-
-
1
1
-
15
15
722458
Baker
Rational design of stereoselec ...
Paraburkholderia xenovorans
J. Am. Chem. Soc.
134
507-513
2012
-
-
1
-
6
-
-
24
-
-
-
-
-
1
-
-
-
-
-
-
-
-
10
-
1
-
-
-
24
-
-
-
-
-
-
-
-
-
1
-
-
6
-
-
-
-
24
-
-
-
-
-
-
-
-
-
-
-
-
10
-
-
-
-
24
-
-
-
-
-
-
-
-
31
31
714244
Baker
Probing the molecular basis of ...
Paraburkholderia xenovorans
Biochemistry
50
3559-3569
2011
-
-
1
-
7
-
-
20
-
-
-
-
-
1
-
-
-
-
-
-
-
-
9
-
1
-
-
-
21
-
-
-
-
-
-
-
-
-
1
-
-
7
-
-
-
-
20
-
-
-
-
-
-
-
-
-
-
-
-
9
-
-
-
-
21
-
-
-
-
-
1
1
-
31
31
721651
Carere
Investigating the molecular de ...
Paraburkholderia xenovorans
Biochemistry
50
8407-8416
2011
-
-
1
-
10
-
-
19
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
1
-
-
-
19
-
-
-
-
-
-
-
-
-
1
-
-
10
-
-
-
-
19
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
19
-
-
-
-
-
1
1
-
-
-
702377
Wang
Comparison of two metal-depend ...
Paraburkholderia xenovorans
Biochemistry
49
3774-3782
2010
-
-
-
-
-
-
5
5
-
1
-
-
-
1
-
-
-
-
-
-
-
-
6
-
1
-
-
-
4
-
-
-
-
6
-
-
-
-
-
-
-
-
-
-
5
6
5
-
1
-
-
-
-
-
-
-
-
-
-
6
-
-
-
-
4
-
-
-
-
-
-
-
-
6
6
721615
Baker
Characterization of an aldolas ...
Paraburkholderia xenovorans
Biochemistry
48
6551-6558
2009
1
-
1
-
-
-
6
5
-
-
3
1
-
1
-
-
1
-
-
-
-
1
5
1
1
-
-
-
5
-
-
-
-
1
-
-
1
-
1
-
-
-
-
-
6
1
5
-
-
3
1
-
-
-
1
-
-
-
1
5
1
-
-
-
5
-
-
-
-
-
1
1
-
5
5