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
-
sweetener
- isomerases
- synthesis
- stearothermophilus
- food industry
- thermodenitrificans
-
low-calorie
- l-ribulokinase
-
packed-bed
-
arabad
- sakei
-
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
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Temperature Stability
Temperature Stability on EC 5.3.1.4 - L-arabinose isomerase
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25 - 55
the enzyme maintains its full activity for 2 days at 25 and 35°C, and over 50% of its full activity for 2 days at 45°C (half-life 52 h). At 55°C, the activity decreases rapidly (half-life 3 h)
30 - 60
the enzyme retains more than 80% activity after 2 h when incubated at 30, 40, 50, or 60°C
35 - 50
45
45 - 70
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the enzyme possesses good stability at 45-50°C, with half-life of 10 h at 50°C. The stability strongly decreases in the range 55-70°C
50
50 - 60
50 - 65
100% activity in absence of metallic ions during 12 h
50 - 70
over 90% of the initial activity is retained after 72 h incubation at 50°C. At 60 and 65°C, over 50% of initial activity is lost in incubations of 60 and 30 min, respectively. The enzyme is completely inactivated by 15 min at 70°C
55 - 75
the activity is fully retained after 2 h incubation at 55-65°C. In the presence of 0.1 mM Mn2+ and 0.05 mM Co2+, the enzyme can remain stable for 2 h during the incubation at 55-65°C, and the half-life of the enzyme is about 150 and 15 min at 70 and 75°C, respectively
60
60 - 65
stable at temperatures below 60°C, above 65°C the enzyme activity decreases with increasing reaction time, the enzyme has a half-life of 1316 min at 65°C, 203 min at 70°C, 30.5 min at 75°C, 24.9 min at 80°C, EDTA treated enzyme has a half-life of 366 min at 70°C with Mn2+, 229 min at 75°C with Mn2+, 41.7 min at 70°C without Mn2+ and 29.8 min at 75°C without Mn2+
65
70
70 - 80
decrease in activity in absence of metallic ions
75
75 - 85
the enzyme shows half-lives of 30 min at 85°C and 220 min at 75°C
80
90
additional information
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when treated with EDTA, the enzym is fully stable at temperatures up to 35°C for 24 h, but after 2 h at 40 and 45°C the enzyme retains only 95% and 55% of its activity, respectively, and at 50°C the half-life is evaluated to 80 min. At higher temperatures the enzyme is rapidly inactivated
35 - 50
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the enzyme is fully stable at temperatures until 35°C after 24 h. After 2 h at 40 and 45°C the enzyme maintains 95% and 60% of its initial activity, respectively, and at 50°C the half-life is 80 min. At higher temperatures the enzyme is rapidly inactivated
50
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the half life of the free enzyme is 2 h and the half life of the aminopropyl glass-immobilized enzyme is 275 h at 50°C
50
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half life for tagatose production in free cells: 8.7 h, in immobilized cells: 632 h
50
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at 50°C, the enzyme retains 100% of its initial activity after 2 h of incubation. Increasing the temperature (above 50°C) significantly reduces the enzyme stability
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the immobilized cells show high stability at 50 and 60°C, and little activity loss occurs after 24-h incubation, the immobilized cells show half-lives of 150 days, 86 days, and 61.7 h
50 - 60
at 55 and 60°C the enzyme stability decreases with half-lives of 2 h and 0.8 h, respectively. The enzyme is perfectly stable showing above 80% of its maximal activity after a 3 h incubation at 50°C in the presence of 0.6 mM Mn2+ or 0.6 mM Mn2+ plus 0.8 mM Co2+
60
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half life for tagatose production in free cells: 2.8 h, in immobilized cells: 144 h
60
the wild type shows a half-life time of 36 h at pH 5.0 and 60°C
65
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half life for tagatose production in free cells: 1.4 h, in immobilized cells: 26.0 h
65
until 65°C independent from metallic ions, above 65°C stability is improved in presence of 0.2 mM Co2+ and 1 mM Mn2+
65
pH 7.5, wild-type enzyme: half-life 70 h, mutant Q268K: half-life 69 h, mutant N175H: half-life 70 h, mutant Q268K/N175H: half-life 71 h
70
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half life for tagatose production in free cells: 0.6 h, in immobilized cells: 12.5 h
70
pH 7.5, wild-type enzyme: half-life 1.8 h, mutant Q268K: half-life 1.6 h, mutant N175H: half-life 0.7 h, mutant Q268K/N175H: half-life 0.6 h
pH 7.5, wild-type enzyme: half-life 1.0 h, mutant Q268K: half-life 0.9 h, mutant N175H: half-life 0.4 h, mutant Q268K/N175H: half-life 0.4 h
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half life for tagatose production in free cells: 0.25 h, in immobilized cells: 7.0 h
80
pH 7.5, wild-type enzyme: half-life 0.2 h, mutant Q268K: half-life 0.2 h, mutants N175H and Q268K/N175H are inactivated
80
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240 min, incubation in presence of Mn2+ or Co2+ causes little loss of activity, apoenzyme is very unstable in absence of metal ions
80
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2 h, in absence of metal ions more than 50% loss of activity, in presence of Co2+ and Mn2+ the enzyme retains 80% of its original activity
90
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half-life without metal ions: 70 min, half-life with 1 mM CoCl2 and 1 mM MnCl2: 120 min
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EDTA-treated AI has a lower melting temperature (72°C) than the holoenzyme (78°C)
additional information
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thermostability is totally independent of metallic ions up to 65°C, above 65°C, thermostability is improved in the presence of only 0.2 mM Co2+ and 1 mM Mn2+
additional information
thermostability is totally independent of metallic ions up to 65°C, above 65°C, thermostability is improved in the presence of only 0.2 mM Co2+ and 1 mM Mn2+
additional information
Halalkalibacterium halodurans
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Tm is 65-67°C, unaffected by the presence of metal ions
additional information
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more thermostable in presence of Mn2+ and/or Co2+ than in absence