BRENDA - Enzyme Database
show all sequences of 1.2.1.87

Protein-protein interactions and substrate channeling in orthologous and chimeric aldolase-dehydrogenase complexes

Baker, P.; Hillis, C.; Carere, J.; Seah, S.Y.K.; Biochemistry 51, 1942-1952 (2012)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
chimeric complexes of Burkholderia xenovorans and Thermus thermophilus enzymes, TTHB246-BphJ and BphI-TTHB247 created by coexpression of the relevant genes in Escherichia coli using separate expression plasmids
Thermus thermophilus
separate expression of TTHB247 in recombinant Escherichia coli
Thermus thermophilus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.5
-
acetaldehyde
app. Km-value, single TTHB247, pH 8.0, 25°C
Thermus thermophilus
6.4
-
propionaldehyde
app. Km-value, single TTHB247, pH 8.0, 25°C
Thermus thermophilus
9.4
-
acetaldehyde
app. Km-value, TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
9.6
-
propionaldehyde
app. Km-value, TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
15.4
-
acetaldehyde
app. Km-value, TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
15.7
-
acetaldehyde
app. Km-value, BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
16.1
-
propionaldehyde
app. Km-value, BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
16.1
-
propionaldehyde
app. Km-value, TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
23.1
-
propionaldehyde
app. Km-value, BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
23.6
-
acetaldehyde
app. Km-value, BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33000
-
estimated by SDS-PAGE, in agreement with predicted molecular mass calculated from amino acid sequences
Thermus thermophilus
33000
-
native molecular mass of TTHB247, determined by static light scattering
Thermus thermophilus
40000
-
native molecular mass of TTHB247, determined by gel filtration
Thermus thermophilus
137000
-
molecular mass of BphI-TTHB247 chimeric complex, determined by static light scattering
Thermus thermophilus
142000
-
native molecular mass of TTHB246-TTHB247 complex, determined by gel filtration
Thermus thermophilus
144000
-
molecular mass of BphI-TTHB247 chimeric complex, determined by gel filtration
Thermus thermophilus
152000
-
native molecular mass of TTHB246-TTHB247 complex, determined by static light scattering
Thermus thermophilus
Organism
Organism
UniProt
Commentary
Textmining
Thermus thermophilus
Q53WH9
-
-
Purification (Commentary)
Purification (Commentary)
Organism
purified to homogeneity using Ni2+-NTA chromatography
Thermus thermophilus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
acetaldehyde + CoA + NAD+
-
721659
Thermus thermophilus
acetyl-CoA + NADH + H+
-
-
-
?
propionaldehyde + CoA + NAD+
-
721659
Thermus thermophilus
propanoyl-CoA + NADH + H+
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 33000, SDS-PAGE, enzyme can form a stable heterotetrameric complex with TTHB246 in vitro, consisting of two aldolase and two dehydrogenase subunits
Thermus thermophilus
Synonyms
Synonyms
Commentary
Organism
TTHB247
-
Thermus thermophilus
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
half-life in complex with TTHB246 is 5.9 h
Thermus thermophilus
50
-
half-life of chimeric BphI-TTHB247 complex is 0.54 h for BphI activity and 2.47 for TTHB247 activity
Thermus thermophilus
50
-
half-life of single enzyme is 1.6 h
Thermus thermophilus
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.2
-
acetaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
2.3
-
propionaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
2.6
-
propionaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
2.8
-
acetaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
3.5
-
acetaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
3.6
-
propionaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
7.4
-
acetaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
8.4
-
propionaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
16.3
-
propionaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
17.2
-
acetaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
Cloned(Commentary) (protein specific)
Commentary
Organism
chimeric complexes of Burkholderia xenovorans and Thermus thermophilus enzymes, TTHB246-BphJ and BphI-TTHB247 created by coexpression of the relevant genes in Escherichia coli using separate expression plasmids
Thermus thermophilus
separate expression of TTHB247 in recombinant Escherichia coli
Thermus thermophilus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
5.5
-
acetaldehyde
app. Km-value, single TTHB247, pH 8.0, 25°C
Thermus thermophilus
6.4
-
propionaldehyde
app. Km-value, single TTHB247, pH 8.0, 25°C
Thermus thermophilus
9.4
-
acetaldehyde
app. Km-value, TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
9.6
-
propionaldehyde
app. Km-value, TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
15.4
-
acetaldehyde
app. Km-value, TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
15.7
-
acetaldehyde
app. Km-value, BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
16.1
-
propionaldehyde
app. Km-value, BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
16.1
-
propionaldehyde
app. Km-value, TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
23.1
-
propionaldehyde
app. Km-value, BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
23.6
-
acetaldehyde
app. Km-value, BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
33000
-
estimated by SDS-PAGE, in agreement with predicted molecular mass calculated from amino acid sequences
Thermus thermophilus
33000
-
native molecular mass of TTHB247, determined by static light scattering
Thermus thermophilus
40000
-
native molecular mass of TTHB247, determined by gel filtration
Thermus thermophilus
137000
-
molecular mass of BphI-TTHB247 chimeric complex, determined by static light scattering
Thermus thermophilus
142000
-
native molecular mass of TTHB246-TTHB247 complex, determined by gel filtration
Thermus thermophilus
144000
-
molecular mass of BphI-TTHB247 chimeric complex, determined by gel filtration
Thermus thermophilus
152000
-
native molecular mass of TTHB246-TTHB247 complex, determined by static light scattering
Thermus thermophilus
Purification (Commentary) (protein specific)
Commentary
Organism
purified to homogeneity using Ni2+-NTA chromatography
Thermus thermophilus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
acetaldehyde + CoA + NAD+
-
721659
Thermus thermophilus
acetyl-CoA + NADH + H+
-
-
-
?
propionaldehyde + CoA + NAD+
-
721659
Thermus thermophilus
propanoyl-CoA + NADH + H+
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 33000, SDS-PAGE, enzyme can form a stable heterotetrameric complex with TTHB246 in vitro, consisting of two aldolase and two dehydrogenase subunits
Thermus thermophilus
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
half-life in complex with TTHB246 is 5.9 h
Thermus thermophilus
50
-
half-life of chimeric BphI-TTHB247 complex is 0.54 h for BphI activity and 2.47 for TTHB247 activity
Thermus thermophilus
50
-
half-life of single enzyme is 1.6 h
Thermus thermophilus
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
2.2
-
acetaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
2.3
-
propionaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
2.6
-
propionaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
2.8
-
acetaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
3.5
-
acetaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
3.6
-
propionaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
7.4
-
acetaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
8.4
-
propionaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
16.3
-
propionaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
17.2
-
acetaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
General Information
General Information
Commentary
Organism
metabolism
together with TTHB246, EC 4.1.3.43, the enzyme forms a bacterial aldolase-dehydrogenase complex catalyzing the last steps in the meta cleavage pathway of aromatic hydrocarbon degradation
Thermus thermophilus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
together with TTHB246, EC 4.1.3.43, the enzyme forms a bacterial aldolase-dehydrogenase complex catalyzing the last steps in the meta cleavage pathway of aromatic hydrocarbon degradation
Thermus thermophilus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.14
-
acetaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
0.14
-
propionaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
0.22
-
propionaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
0.23
-
acetaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
0.27
-
propionaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
0.3
-
acetaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
0.7
-
propionaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
0.73
-
acetaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
1.31
-
propionaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
1.35
-
acetaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
0.14
-
acetaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
0.14
-
propionaldehyde
BphJ-TTHB246 complex, pH 8.0, 25°C
Thermus thermophilus
0.22
-
propionaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
0.23
-
acetaldehyde
TTHB246-TTHB247 complex, pH 8.0, 25°C
Thermus thermophilus
0.27
-
propionaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
0.3
-
acetaldehyde
TTHB247-BphI complex, pH 8.0, 25°C
Thermus thermophilus
0.7
-
propionaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
0.73
-
acetaldehyde
BphJ-BphI complex, pH 8.0, 25°C
Thermus thermophilus
1.31
-
propionaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
1.35
-
acetaldehyde
single TTHB247, pH 8.0, 25°C
Thermus thermophilus
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
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)
742372
Lan
-
Oxygen-tolerant coenzyme A-ac ...
Salmonella enterica, Klebsiella pneumoniae, Listeria monocytogenes, Listeria monocytogenes M7
Energy Environ. Sci.
6
2672-2681
2013
-
-
3
-
1
-
-
7
-
-
-
12
-
4
3
-
-
-
-
-
2
-
18
-
13
3
-
-
6
3
-
-
3
-
-
-
-
-
3
3
-
1
-
-
-
-
7
-
-
-
12
-
3
-
-
-
-
2
-
18
-
3
-
-
6
3
-
-
-
-
2
2
-
6
6
721659
Baker
Protein-protein interactions a ...
Thermus thermophilus
Biochemistry
51
1942-1952
2012
-
-
2
-
-
-
-
10
-
-
7
-
-
1
-
-
1
-
-
-
-
-
2
1
1
-
-
3
10
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
10
-
-
7
-
-
-
-
1
-
-
-
-
2
1
-
-
3
10
-
-
-
-
-
1
1
-
10
10
721651
Carere
Investigating the molecular de ...
Paraburkholderia xenovorans
Biochemistry
50
8407-8416
2011
-
-
1
-
2
-
-
6
-
-
-
-
-
1
-
-
1
-
-
-
-
-
2
-
1
-
-
-
6
-
-
-
-
-
-
-
-
-
1
-
-
2
-
-
-
-
6
-
-
-
-
-
-
-
1
-
-
-
-
2
-
-
-
-
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
1
-
-
-
6
-
-
-
2
-
-
-
-
-
1
2
-
-
-
-
-
-
6
-
-
3
1
-
-
-
1
-
-
-
1
8
1
-
-
-
6
-
-
-
-
-
1
1
-
7
7