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show all sequences of 1.2.1.57

Oxygen-tolerant coenzyme A-acylating aldehyde dehydrogenase facilitates efficient photosynthetic n-butanol biosynthesis in cyanobacteria

Lan, E.; Ro, S.; Liao, J.; Energy Environ. Sci. 6, 2672-2681 (2013)
No PubMed abstract available

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis
Synechococcus elongatus
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production
Clostridium saccharoperbutylacetonicum
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Lactobacillus brevis produces more n-butanol than ethanol
Lactobacillus brevis
Engineering
Amino acid exchange
Commentary
Organism
additional information
design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP
Synechococcus elongatus
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
no Michaelis-Menten behaviour
Clostridium saccharoperbutylacetonicum
0.076
-
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
0.534
-
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
acetyl-CoA + NADH + H+
Lactobacillus brevis
-
acetaldehyde + CoA + NAD+
-
-
r
acetyl-CoA + NADH + H+
Clostridium saccharoperbutylacetonicum
low activity
acetaldehyde + CoA + NAD+
-
-
r
butanoyl-CoA + NADH + H+
Lactobacillus brevis
-
butanal + CoA + NAD+
-
-
r
butanoyl-CoA + NADH + H+
Synechococcus elongatus
-
butanal + CoA + NAD+
-
-
?
butanoyl-CoA + NADH + H+
Clostridium saccharoperbutylacetonicum
best substrate
butanal + CoA + NAD+
-
-
r
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Clostridium saccharoperbutylacetonicum
-
-
-
Lactobacillus brevis
-
-
-
Synechococcus elongatus
-
-
-
Oxidation Stability
Oxidation Stability
Organism
oxygen sensitivity of CoA-acylating aldehyde dehydrogenase
Synechococcus elongatus
the enzyme is oxygen-tolerant
Lactobacillus brevis
the enzyme is oxygen-tolerant
Clostridium saccharoperbutylacetonicum
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.49
-
with butanoyl-CoA, pH 7.15, 30°C
Clostridium saccharoperbutylacetonicum
2.5
-
with butanoyl-CoA, pH 7.15, 30°C
Lactobacillus brevis
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetyl-CoA + NADH + H+
-
742372
Lactobacillus brevis
acetaldehyde + CoA + NAD+
-
-
-
r
acetyl-CoA + NADH + H+
low activity
742372
Clostridium saccharoperbutylacetonicum
acetaldehyde + CoA + NAD+
-
-
-
r
butanoyl-CoA + NADH + H+
-
742372
Lactobacillus brevis
butanal + CoA + NAD+
-
-
-
r
butanoyl-CoA + NADH + H+
-
742372
Synechococcus elongatus
butanal + CoA + NAD+
-
-
-
?
butanoyl-CoA + NADH + H+
best substrate
742372
Clostridium saccharoperbutylacetonicum
butanal + CoA + NAD+
-
-
-
r
additional information
substrate chain length specificity of the enzyme is C2-C12, highest activity with C6 substrate, overview
742372
Lactobacillus brevis
?
-
-
-
-
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Clostridium saccharoperbutylacetonicum
30
-
assay at
Lactobacillus brevis
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.26
-
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
3.37
-
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.15
-
assay at
Clostridium saccharoperbutylacetonicum
7.15
-
assay at
Lactobacillus brevis
Cofactor
Cofactor
Commentary
Organism
Structure
NADH
-
Clostridium saccharoperbutylacetonicum
NADH
-
Lactobacillus brevis
NADH
-
Synechococcus elongatus
Cloned(Commentary) (protein specific)
Commentary
Organism
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production
Clostridium saccharoperbutylacetonicum
gene pduP, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis. Recombinant coexpression of PduP with the enzymes of the n-butanol synthesis pathway in Synechococcus elongatus strain PCC 7942 results in autotrophic n-butanol production. PduP from Lactobacillus brevis produces more n-butanol than ethanol
Lactobacillus brevis
gene bldh, recombinant expression in Escherichia coli strain JCL166, strain JCL166 cannot grow anaerobically unless complemented by an exogenous fermentation pathway such as n-butanol biosynthesis
Synechococcus elongatus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NADH
-
Clostridium saccharoperbutylacetonicum
NADH
-
Lactobacillus brevis
NADH
-
Synechococcus elongatus
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
additional information
design of a coenzyme A (CoA) dependent n-butanol biosynthesis pathway tailored to the metabolic physiology of the cyanobacterium Synechococcus elongatus PCC 7942 by incorporating an ATP driving force and a kinetically irreversible trap. Oxygen-sensitive CoA-acylating butyraldehyde dehydrogenase (Bldh) is exchanged for the oxygen-tolerant PduP from Salmonella enterica. Replacing Bldh with PduP in the n-butanol synthesis pathway results in n-butanol production to a cumulative titer of 404 mg/l with peak productivity of 51 mg/l per day, exceeding the base strain by 20fold. Anaerobic growth rescue of Escherichia coli strain JCL166 by overexpression of the Clostridium butanol pathway with different aldehyde dehydrogenases PduP
Synechococcus elongatus
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
no Michaelis-Menten behaviour
Clostridium saccharoperbutylacetonicum
0.076
-
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
0.534
-
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
acetyl-CoA + NADH + H+
Lactobacillus brevis
-
acetaldehyde + CoA + NAD+
-
-
r
acetyl-CoA + NADH + H+
Clostridium saccharoperbutylacetonicum
low activity
acetaldehyde + CoA + NAD+
-
-
r
butanoyl-CoA + NADH + H+
Lactobacillus brevis
-
butanal + CoA + NAD+
-
-
r
butanoyl-CoA + NADH + H+
Synechococcus elongatus
-
butanal + CoA + NAD+
-
-
?
butanoyl-CoA + NADH + H+
Clostridium saccharoperbutylacetonicum
best substrate
butanal + CoA + NAD+
-
-
r
Oxidation Stability (protein specific)
Oxidation Stability
Organism
oxygen sensitivity of CoA-acylating aldehyde dehydrogenase
Synechococcus elongatus
the enzyme is oxygen-tolerant
Lactobacillus brevis
the enzyme is oxygen-tolerant
Clostridium saccharoperbutylacetonicum
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
0.49
-
with butanoyl-CoA, pH 7.15, 30°C
Clostridium saccharoperbutylacetonicum
2.5
-
with butanoyl-CoA, pH 7.15, 30°C
Lactobacillus brevis
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
acetyl-CoA + NADH + H+
-
742372
Lactobacillus brevis
acetaldehyde + CoA + NAD+
-
-
-
r
acetyl-CoA + NADH + H+
low activity
742372
Clostridium saccharoperbutylacetonicum
acetaldehyde + CoA + NAD+
-
-
-
r
butanoyl-CoA + NADH + H+
-
742372
Lactobacillus brevis
butanal + CoA + NAD+
-
-
-
r
butanoyl-CoA + NADH + H+
-
742372
Synechococcus elongatus
butanal + CoA + NAD+
-
-
-
?
butanoyl-CoA + NADH + H+
best substrate
742372
Clostridium saccharoperbutylacetonicum
butanal + CoA + NAD+
-
-
-
r
additional information
substrate chain length specificity of the enzyme is C2-C12, highest activity with C6 substrate, overview
742372
Lactobacillus brevis
?
-
-
-
-
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
30
-
assay at
Clostridium saccharoperbutylacetonicum
30
-
assay at
Lactobacillus brevis
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.26
-
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
3.37
-
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.15
-
assay at
Clostridium saccharoperbutylacetonicum
7.15
-
assay at
Lactobacillus brevis
General Information
General Information
Commentary
Organism
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
Clostridium saccharoperbutylacetonicum
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
Lactobacillus brevis
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
Synechococcus elongatus
General Information (protein specific)
General Information
Commentary
Organism
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
Clostridium saccharoperbutylacetonicum
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
Lactobacillus brevis
metabolism
the oxygen sensitivity of CoA-acylating aldehyde dehydrogenase appears to be a key limiting factor for cyanobacteria to produce alcohols through the CoA-dependent route
Synechococcus elongatus
KCat/KM [mM/s]
kcat/KM Value [1/mMs-1]
kcat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3
-
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
6
-
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
KCat/KM [mM/s] (protein specific)
KCat/KM Value [1/mMs-1]
KCat/KM Value Maximum [1/mMs-1]
Substrate
Commentary
Organism
Structure
3
-
acetyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
6
-
butanoyl-CoA
recombinant enzyme, pH 7.15, 30°C
Lactobacillus brevis
Other publictions for EC 1.2.1.57
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)
742138
Hwang
Engineering of a butyraldehyd ...
Clostridium saccharoperbutylacetonicum, Clostridium saccharoperbutylacetonicum KCTC5577
Biotechnol. Bioeng.
111
1374-1384
2014
-
-
1
-
12
-
-
1
-
-
-
8
-
4
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
2
-
-
-
-
-
1
2
-
12
-
-
-
-
1
-
-
-
8
-
-
-
-
-
-
-
-
8
-
-
-
-
-
-
-
-
-
-
1
1
-
-
-
743219
Bhandiwad
Metabolic engineering of Ther ...
Thermoanaerobacterium saccharolyticum, Thermoanaerobacterium saccharolyticum DSM 571
Metab. Eng.
21
17-25
2014
-
-
1
-
1
-
-
-
-
-
-
4
-
2
-
-
-
-
-
-
1
-
6
-
1
-
-
-
1
-
-
2
-
-
-
-
-
1
2
-
1
-
-
-
-
-
-
-
-
4
-
-
-
-
-
-
1
-
6
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
742372
Lan
-
Oxygen-tolerant coenzyme A-ac ...
Clostridium saccharoperbutylacetonicum, Lactobacillus brevis, Synechococcus elongatus
Energy Environ. Sci.
6
2672-2681
2013
-
-
3
-
1
-
-
3
-
-
-
5
-
3
3
-
-
-
-
-
2
-
6
-
2
-
-
2
2
-
-
3
-
-
-
-
-
3
3
-
1
-
-
-
-
3
-
-
-
5
-
3
-
-
-
-
2
-
6
-
2
-
-
2
2
-
-
-
-
3
3
-
2
2
11534
Palosaari
Purification and properties of ...
Clostridium acetobutylicum
J. Bacteriol.
170
2971-2976
1988
-
-
-
-
-
1
1
10
-
-
2
-
-
2
-
-
1
-
-
-
1
1
7
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
1
-
1
-
10
-
-
2
-
-
-
-
1
-
-
1
1
7
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-