BRENDA - Enzyme Database show
show all sequences of 1.1.1.383

Cofactor engineering of ketol-acid reductoisomerase (IlvC) and alcohol dehydrogenase (YqhD) improves the fusel alcohol yield in algal protein anaerobic fermentation

Wu, W.; Tran-Gyamfi, M.; Jaryenneh, J.; Davis, R.; Algal Res. 19, 162-167 (2016)
No PubMed abstract available

Data extracted from this reference:

Application
Application
Commentary
Organism
biofuel production
combination of high activity alcohol dehydrogenase YqhD mutants with IlvC mutants, both accepting NADH as a redox cofactor, in an engineered Escherichia coli strain, enabling comprehensive utilization of the biomass for biofuel applications. The refined strain, shows an increased fusel alcohol yield of about 60% compared to wild type under anaerobic fermentation on amino acid mixtures.When applied to real algal protein hydrolysates, the strain produces 100% and 38% more total mixed alcohols than the wild type strain on two different algal hydrolysates, respectively
Escherichia coli
Cloned(Commentary)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Engineering
Amino acid exchange
Commentary
Organism
A71S/R76D/S78D/Q110V
strain engineered to switch the cofactor specificity fromNADPH to NADH, application in an engineered Escherichia coli strain, enabling comprehensive utilization of the biomass for biofuel applications
Escherichia coli
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Escherichia coli
P05793
-
-
Application (protein specific)
Application
Commentary
Organism
biofuel production
combination of high activity alcohol dehydrogenase YqhD mutants with IlvC mutants, both accepting NADH as a redox cofactor, in an engineered Escherichia coli strain, enabling comprehensive utilization of the biomass for biofuel applications. The refined strain, shows an increased fusel alcohol yield of about 60% compared to wild type under anaerobic fermentation on amino acid mixtures.When applied to real algal protein hydrolysates, the strain produces 100% and 38% more total mixed alcohols than the wild type strain on two different algal hydrolysates, respectively
Escherichia coli
Cloned(Commentary) (protein specific)
Commentary
Organism
expression in Escherichia coli
Escherichia coli
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
A71S/R76D/S78D/Q110V
strain engineered to switch the cofactor specificity fromNADPH to NADH, application in an engineered Escherichia coli strain, enabling comprehensive utilization of the biomass for biofuel applications
Escherichia coli
Other publictions for EC 1.1.1.383
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)
737411
Wu
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Cofactor engineering of ketol- ...
Escherichia coli
Algal Res.
19
162-167
2016
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738975
Milne
Excessive by-product formation ...
Escherichia coli
Metab. Eng. Commun.
3
39-51
2016
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731279
Cahn
Cofactor specificity motifs an ...
Azotobacter vinelandii, Azotobacter vinelandii ATCC BAA-1303
Biochem. J.
468
475-484
2015
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1
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732457
Brinkmann-Chen
Uncovering rare NADH-preferrin ...
Hydrogenobaculum sp. Y04AAS1, Ignisphaera aggregans, Metallosphaera sedula
Metab. Eng.
26C
17-22
2014
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3
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6
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6
739528
Brinkmann-Chen
General approach to reversing ...
Escherichia coli, Lactococcus lactis subsp. lactis, Lactococcus lactis subsp. lactis IL1403, Shewanella sp., Shewanella sp. ANA-3, Slackia exigua, Slackia exigua DSM 15923
Proc. Natl. Acad. Sci. USA
110
10946-10951
2013
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10
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26
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738976
Bastian
Engineered ketol-acid reductoi ...
Escherichia coli
Metab. Eng.
13
345-352
2011
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1
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8
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14
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