5.3.1.4: L-arabinose isomerase
This is an abbreviated version!
For detailed information about L-arabinose isomerase, go to the full flat file.
Word Map on EC 5.3.1.4
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5.3.1.4
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d-tagatose
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isomerization
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l-ribulose
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nutrition
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geobacillus
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sweetener
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isomerases
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synthesis
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stearothermophilus
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food industry
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thermodenitrificans
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low-calorie
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l-ribulokinase
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packed-bed
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arabad
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sakei
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4-epimerase
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industry
- 5.3.1.4
- d-tagatose
-
isomerization
- l-ribulose
- nutrition
- geobacillus
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sweetener
- isomerases
- synthesis
- stearothermophilus
- food industry
- thermodenitrificans
-
low-calorie
- l-ribulokinase
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packed-bed
-
arabad
- sakei
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4-epimerase
- industry
Reaction
Synonyms
AI, AraA, arabinose isomerase, D-galactose isomerase, ECAI, gali 152, gali 153, GSAI, GSAI 152, GSAI 153, Isomerase, L-arabinose, L-AI, L-AI NC8, L-AI US100, L-arabinose aldose-ketose-isomerase, L-arabinose isomerase, L-arabinose isomerase 1, L-arabinose isomerase 2, L-arabinose ketol-isomerase, pL 151, pL 152, pL 153, pL151, TNAI
ECTree
5.3.1.4 L-arabinose isomeraseAdvanced search results
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results (Engineering
Engineering on EC 5.3.1.4 - L-arabinose isomerase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
M33R
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the mutant has the pH optimum of stability shifted upward from acidic to basic pH
Q202R
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the mutant has the pH optimum of stability shifted upward from acidic to basic pH
V50R
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the mutant has the pH optimum of stability shifted upward from acidic to basic pH
Y218R
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the mutant has the pH optimum of stability shifted upward from acidic to basic pH
D478A
mutant retains more than 80 % of the maximum relative activity of the wild-type at 75°C
D478N
mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C. Mutant displays a decreased optimum pH value
D478Q
mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C and displays a decreased optimum pH value
D478A
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mutant retains more than 80 % of the maximum relative activity of the wild-type at 75°C
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D478N
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mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C. Mutant displays a decreased optimum pH value
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D478Q
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mutant shows increased activity for D-galactose isomerization and retains more than 80 % of the maximum relative activity of the wild-type at 75°C and displays a decreased optimum pH value
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R200E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R216E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R31E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R48E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
R200E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
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R216E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
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R31E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
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R48E
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the mutant has the pH optimum of stability shifted downward from basic to acidic pH
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I370A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
L345A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
M185A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
M349A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
T276A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
W439A
site-directed mutagenesis, the mutant catalytic activity is similar to the wild-type enzyme
Y333A
site-directed mutagenesis, the catalytic site mutant shows 97.2% reduced activity compared to the wild-type enzyme
Y333D
site-directed mutagenesis, the catalytic site mutant shows no activity
Y333E
site-directed mutagenesis, the catalytic site mutant shows no activity
Y333I
site-directed mutagenesis, the catalytic site mutant shows 72% reduced activity compared to the wild-type enzyme
Y333K
site-directed mutagenesis, the catalytic site mutant shows no activity
Y333V
site-directed mutagenesis, the catalytic site mutant shows 82% reduced activity compared to the wild-type enzyme
Y333X
replacing Y333 with the aromatic amino acid Phe does not alter catalytic efficiency toward L-arabinose. In contrast, the activities of mutants containing a hydrophobic amino acid, Ala, Val, or Leu, decrease as the size of the hydrophobic side chain of the amino acid decreases. However, mutants containing hydrophilic and charged amino acids, such as Asp, Glu, and Lys, show almost no activity with L-arabinose
E305A
E330A
H347A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
H446A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
E305A
E330A
H446A
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site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
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G270D
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the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
L282M
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the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
R25C
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the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
T451P
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the enzyme shows 31% increased activity compared to the wild type enzyme
Y496C
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the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
D228N/D384G/T393S/N428K/K475N
site directed mutagenesis, GSAI 152
H175N
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the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
M322V/S393T/V408A
error prone PCR mutagenesis using gali 152 as template, gali 153 with changes in 3 amino acids revealed a higher activity than gali 152
N175H
site-directed mutagenesis, the N175H mutant has a broad optimal temperature range from 50 to 65°C
Q268K
Q268K/H175N
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the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
Q268K/N175H
site-directed mutagenesis, the Q268K mutant is more acidotolerant, the N175H mutant has a broad optimal temperature range from 50 to 65°C
M322V/S393T/V408A
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error prone PCR mutagenesis using gali 152 as template, gali 153 with changes in 3 amino acids revealed a higher activity than gali 152
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H175N
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the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
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N175H
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site-directed mutagenesis, the N175H mutant has a broad optimal temperature range from 50 to 65°C
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Q268K
Q268K/H175N
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the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
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Q268K/N175H
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site-directed mutagenesis, the Q268K mutant is more acidotolerant, the N175H mutant has a broad optimal temperature range from 50 to 65°C
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C450S/N475K
F280N/C450S/N475K
mutat catalyzes the isomerization of D-galactose to D-tagatose
D268E
the mutant shows 58% activity compared to the wild type enzyme
D268K
the mutant shows 48% activity compared to the wild type enzyme
D268K/D269K
the mutant shows 65% activity compared to the wild type enzyme
D268K/D269K/D299K
the mutant with 115% activity compared to the wild type enzyme exhibits significant optimum pH shifts (from 6.5 to 5.0) and enhancement of pH stability (half-life time increased from 30 to 62 h at pH 6.0). With the addition of borate, D-galactose is isomerized into D-tagatose by this mutant at pH 5.0, resulting in a high conversion rate of 62%
D268K/D299K
the mutant shows 42% activity compared to the wild type enzyme
D268R
the mutant shows 88% activity compared to the wild type enzyme
D269E
the mutant shows 62% activity compared to the wild type enzyme
D269K
the mutant shows 130% activity compared to the wild type enzyme
D269K/D299K
the mutant shows 84% activity compared to the wild type enzyme
D269R
the mutant shows 88% activity compared to the wild type enzyme
D299E
the mutant shows 109% activity compared to the wild type enzyme
D299K
the mutant shows 90% activity compared to the wild type enzyme
D299R
the mutant shows 68% activity compared to the wild type enzyme
D268E
Limosilactobacillus fermentum CGMCC2921
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the mutant shows 58% activity compared to the wild type enzyme
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D268K
Limosilactobacillus fermentum CGMCC2921
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the mutant shows 48% activity compared to the wild type enzyme
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D268K/D269K/D299K
Limosilactobacillus fermentum CGMCC2921
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the mutant with 115% activity compared to the wild type enzyme exhibits significant optimum pH shifts (from 6.5 to 5.0) and enhancement of pH stability (half-life time increased from 30 to 62 h at pH 6.0). With the addition of borate, D-galactose is isomerized into D-tagatose by this mutant at pH 5.0, resulting in a high conversion rate of 62%
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D268R
Limosilactobacillus fermentum CGMCC2921
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the mutant shows 88% activity compared to the wild type enzyme
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D269E
Limosilactobacillus fermentum CGMCC2921
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the mutant shows 62% activity compared to the wild type enzyme
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additional information
E305A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
E305A
site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
E330A
site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
E330A
site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
E305A
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site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
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E305A
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site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
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E330A
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site-directed mutagenesis, inactive mutant, structure comparison to the wild-type enzyme
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E330A
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site-directed mutagenesis, mutation of the conserved catalytic residue leads to complete loss of catalytic activity, structure comparison to the wild-type enzyme
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Q268K
site-directed mutagenesis, the mutant enzyme shows increased acidotolerance and is more stable at acidic pH than the wild-type enzyme
Q268K
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the mutant shows a pH optimum of 6.0-6.5 and a higher stability at acidic pH compared to the wild type enzyme, the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
Q268K
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the mutant shows a pH optimum of 6.0-6.5 and a higher stability at acidic pH compared to the wild type enzyme, the mutant exhibits faster D-galactose bioconversion compared to the wild type enzyme
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Q268K
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site-directed mutagenesis, the mutant enzyme shows increased acidotolerance and is more stable at acidic pH than the wild-type enzyme
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C450S/N475K
site directed mutagenesis, 20% higher tagatose conversion than the wild type enzyme
C450S/N475K
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mutant strain is able to produce 95 g L-ribulose per l from 500 g L-arabinose per l under optimum conditions of pH 8, 70°C, and 10 units enzyme per ml with a conversion yield of 19% over 2 h. The half-lives of the mutated enzyme at 70 and 75°C are 35 and 4.5 h, respectively
C450S/N475K
mutant catalyzes the isomerization of D-galactose to D-tagatose
additional information
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immobilization of Escherichia coli cells, recombinantly expressing the L-arabinose isomerase from Bacillus licheniformis, on alginate stabilizes the cells, optimal at 2% w/v alginate, 0.1 M Ca2+, 50 g/l cell mass, and 4 h curing time, 89% remaining enzyme activity after 33 days at 50°C
additional information
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immobilization of the enzyme on different matrices, e.g. activated carboxymethylcellulose, Eupergit C, CNBr-activated agarose, chitosan, and alginate, for semi-continous production of L-ribulose, method optimization, overview. 85.1% remaining activity after 8 cycles and 86.4% activity compared to the wild-type enzyme
additional information
expression of N- and C-terminal His-tagged protein in Escherichia coli. The C-His-tagged enzyme is preferentially hexameric in solution, whereas the N-His-tagged protein is mainly monomeric. The N-His-tagged variant shows a maximum bioconversion yield of 26% at 50°C for D-tagatose biosynthesis, the C-His-tagged variant is more active and stable at alkaline pH than the N-His-tagged variant
additional information
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expression of N- and C-terminal His-tagged protein in Escherichia coli. The C-His-tagged enzyme is preferentially hexameric in solution, whereas the N-His-tagged protein is mainly monomeric. The N-His-tagged variant shows a maximum bioconversion yield of 26% at 50°C for D-tagatose biosynthesis, the C-His-tagged variant is more active and stable at alkaline pH than the N-His-tagged variant
additional information
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expression of N- and C-terminal His-tagged protein in Escherichia coli. The C-His-tagged enzyme is preferentially hexameric in solution, whereas the N-His-tagged protein is mainly monomeric. The N-His-tagged variant shows a maximum bioconversion yield of 26% at 50°C for D-tagatose biosynthesis, the C-His-tagged variant is more active and stable at alkaline pH than the N-His-tagged variant
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additional information
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mutation results in a change in the structure of isomerase which causes thermolability
additional information
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mutation results in a change in the structure of isomerase which causes thermolability
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additional information
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five point mutations increase the activity 11fold in the first round of evolution, and three point mutations in the second round of evolution increase the activity 5fold beyond the activity from the first round
additional information
construction of three Bacillus stearothermophilus US100 L-arabinose isomerase mutants with increased activity for D-galactose and increased D-tagatose production
additional information
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construction of three Bacillus stearothermophilus US100 L-arabinose isomerase mutants with increased activity for D-galactose and increased D-tagatose production
additional information
evaluation and optimization of Escherichia coli and Bacilus subtilis expression systems for toxic byproducts in L-ribulose and/or D-tagatose production by the recombinant engineered enzyme
additional information
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construction of three Bacillus stearothermophilus US100 L-arabinose isomerase mutants with increased activity for D-galactose and increased D-tagatose production
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