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show all sequences of 1.2.1.87

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:

Cloned(Commentary)
Commentary
Organism
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yield soluble proteins
Paraburkholderia xenovorans
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0348
-
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
0.561
-
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
7.7
-
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
23.1
-
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
23.6
-
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
31.7
-
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
Paraburkholderia xenovorans
37000
-
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
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
propanal + CoA + NAD+
Paraburkholderia xenovorans
-
propanoyl-CoA + NADH + H+
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Paraburkholderia xenovorans
Q79AF6
-
-
Purification (Commentary)
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 -80°C, 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
acetaldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
acetyl-CoA + NADH + H+
-
-
-
?
acetaldehyde + CoA + NADP+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
721615
Paraburkholderia xenovorans
acetyl-CoA + NADPH + H+
-
-
-
?
butyraldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
butyryl-CoA + NAD+ + H+
-
-
-
?
isobutyraldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
isobutyryl-CoA + NAD+ + H+
-
-
-
?
additional information
no activity with succinic semialdehyde and picolinaldehyde
721615
Paraburkholderia xenovorans
?
-
-
-
-
pentaldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
pentanoyl-CoA + NADH + H+
-
-
-
?
propanal + CoA + NAD+
-
721615
Paraburkholderia xenovorans
propanoyl-CoA + NADH + H+
-
-
-
?
propionaldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
propanoyl-CoA + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
Paraburkholderia xenovorans
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
9.5
-
Butyraldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
11.2
-
Isobutyraldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
12.9
-
NADP+
with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
14.1
-
NAD+
with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
16.3
-
propionaldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
17.2
-
acetaldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
Cofactor
Cofactor
Commentary
Organism
Structure
NAD+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
Paraburkholderia xenovorans
NADP+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
Paraburkholderia xenovorans
Cloned(Commentary) (protein specific)
Commentary
Organism
coexpression of bphI and bphJ in Escherichia coli using two compatible plasmids (pBTL4 and pET28a) yield soluble proteins
Paraburkholderia xenovorans
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
Paraburkholderia xenovorans
NADP+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
Paraburkholderia xenovorans
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.0348
-
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
0.561
-
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
7.7
-
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
23.1
-
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
23.6
-
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
31.7
-
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
SDS-PAGE, in agreement with the predicted molecular mass calculated from amino acid sequence
Paraburkholderia xenovorans
37000
-
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
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
propanal + CoA + NAD+
Paraburkholderia xenovorans
-
propanoyl-CoA + NADH + H+
-
-
?
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 -80°C, 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
acetaldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
acetyl-CoA + NADH + H+
-
-
-
?
acetaldehyde + CoA + NADP+
BphJ is able to utilize NAD+ and NADP+ with comparable kcat values, but the apparent Km-value for NAD+ is 16fold lower than for NADP+
721615
Paraburkholderia xenovorans
acetyl-CoA + NADPH + H+
-
-
-
?
butyraldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
butyryl-CoA + NAD+ + H+
-
-
-
?
isobutyraldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
isobutyryl-CoA + NAD+ + H+
-
-
-
?
additional information
no activity with succinic semialdehyde and picolinaldehyde
721615
Paraburkholderia xenovorans
?
-
-
-
-
pentaldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
pentanoyl-CoA + NADH + H+
-
-
-
?
propanal + CoA + NAD+
-
721615
Paraburkholderia xenovorans
propanoyl-CoA + NADH + H+
-
-
-
?
propionaldehyde + CoA + NAD+
-
721615
Paraburkholderia xenovorans
propanoyl-CoA + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
heterotetramer
BphI-BphJ-complex, alpha2beta2, 2 * 32000 BphJ, 2 * 37000 BphI, estimated by gel filtration
Paraburkholderia xenovorans
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
9.5
-
Butyraldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
11.2
-
Isobutyraldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
12.9
-
NADP+
with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
14.1
-
NAD+
with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
16.3
-
propionaldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
17.2
-
acetaldehyde
pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
General Information
General Information
Commentary
Organism
metabolism
enzyme forms a bifunctional complex with EC 4.1.3.43 (BphI), 4-hydroxy-2-oxohexanoate aldolase 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 4.1.3.43 (BphI), 4-hydroxy-2-oxohexanoate aldolase 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
0.076
-
pentaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
0.3
-
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
0.7
-
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
0.73
-
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
1.4
-
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
22.99
-
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
405.2
-
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
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
0.076
-
pentaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
0.3
-
Butyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
0.7
-
propionaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
0.73
-
acetaldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
1.4
-
Isobutyraldehyde
app. Km-value, pH 8.0 and 25°C, NAD+
Paraburkholderia xenovorans
22.99
-
NADP+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
405.2
-
NAD+
app. Km-value with acetaldehyde as substrate, pH 8.0 and 25°C
Paraburkholderia xenovorans
Other publictions for EC 1.2.1.87
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
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)
742372
Lan
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Oxygen-tolerant coenzyme A-ac ...
Klebsiella pneumoniae, Listeria monocytogenes, Listeria monocytogenes M7, Salmonella enterica
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-
3
-
1
-
-
7
-
-
-
12
-
4
3
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-
-
2
-
18
-
3
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6
3
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3
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3
3
-
1
-
-
-
-
7
-
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-
12
-
3
-
-
-
-
2
-
18
-
3
-
-
6
3
-
-
-
-
2
2
-
6
6
721659
Baker
Protein-protein interactions a ...
Thermus thermophilus
Biochemistry
51
1942-1952
2012
-
-
1
-
-
-
-
9
-
-
6
-
-
1
-
-
1
-
-
-
-
-
2
1
-
-
1
10
-
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1
-
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-
-
-
-
-
9
-
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6
-
-
-
-
1
-
-
-
-
2
1
-
-
1
10
-
-
-
-
-
1
1
-
10
10
721651
Carere
Investigating the molecular de ...
Paraburkholderia xenovorans
Biochemistry
50
8407-8416
2011
-
-
1
-
2
-
-
6
-
-
-
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-
1
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1
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2
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6
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1
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2
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6
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1
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2
-
-
-
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6
-
-
-
-
-
1
1
-
-
-
721615
Baker
Characterization of an aldolas ...
Paraburkholderia xenovorans
Biochemistry
48
6551-6558
2009
-
-
1
-
-
-
-
6
-
-
3
1
-
1
-
-
1
-
-
-
-
1
8
1
-
-
-
6
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
6
-
-
3
1
-
-
-
1
-
-
-
1
8
1
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6
-
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-
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1
1
-
7
7