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Information on EC 5.3.1.4 - L-arabinose isomerase and Organism(s) Escherichia coli and UniProt Accession P08202
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5.3.1.4 L-arabinose isomeraseIUBMB Comments
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+) . The enzyme binds beta-L-arabinopyranose and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism . The enzyme can also convert alpha-D-galactose to D-tagatose with lower efficiency .
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Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
l-arabinose isomerase, arabinose isomerase, l-ai us100, l-ai nc8, d-galactose isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Isomerase, L-arabinose
-
-
-
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L-arabinose ketol-isomerase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
isomerization
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-
SYSTEMATIC NAME
IUBMB Comments
beta-L-arabinopyranose aldose-ketose-isomerase
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+) [2]. The enzyme binds beta-L-arabinopyranose [4] and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [6]. The enzyme can also convert alpha-D-galactose to D-tagatose with lower efficiency [5].
CAS REGISTRY NUMBER
COMMENTARY
9023-80-7
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
Mn2+
-
essential for catalysis, but also competitive inhibitor for L-arabinose
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Mn2+
-
essential for catalysis, but also competitive inhibitor for L-arabinose
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
60000
60000
-
6 * 60000, sedimentation in the ultracentrifuge in presence of 8 M urea or pH 2 phosphate buffer
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
hexamer
hexamer
-
the enzyme is seen in two distinctly different orientations: the first has three subunits visible, with a 3fold axis of symmetry, corresponding to a face-on view of two stacked, eclipsed trimers. The second orientation is rectangular in shape with 2fold symmetry, suggesting a side-one view of the stacked trimers
hexamer
-
6 * 60000, sedimentation in the ultracentrifuge in presence of 8 M urea or pH 2 phosphate buffer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
G270D
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
L282M
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
R25C
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
T451P
-
the enzyme shows 31% increased activity compared to the wild type enzyme
Y496C
-
the mutation causes a decrease in activity of more than 20% compared to the wild type enzyme
additional information
-
mutation results in a change in the structure of isomerase which causes thermolability
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli of the selenomethionine-substituted enzyme
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
food industry
production of D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
synthesis
additional information
synthesis
-
an Escherichia coli galactose kinase gene knockout strain, which contains the L-arabinose isomerase gene to isomerize D-galactose to D-tagatose, shows a higher conversion yield of tagatose because galactose is not metabolized by endogenous galactose kinase. In whole cells of the galactose kinase knockout strain, the isomerase-catalyzed reaction exhibits an equilibrium shift towards tagatose, producing a tagatose fraction of 68% at 37°C, whereas the purified L-arabinose isomerase gives a tagatose equilibriumfraction of 36%
synthesis
-
expression of the Escherichia coli genes araA, araB, and araD encoding L-arabinose isomerase, L-ribulokinase, and L-ribulose-5-phosphate 4-epimerase, respectively, in Corynebacterium glutamicum under the control of a constitutive promoter. The recombinant strain is able to grow on mineral salts medium containing L-arabinose as the sole carbon and energy source. Under oxygen deprivation and with L-arabinose as the sole carbon and energy source, carbon flow of the recombinant strain is redirected to produce up to 40, 37, and 11%, respectively, of the theoretical yields of succinic, lactic, and acetic acids. Usinga sugar mixture containing 5% D-glucose and 1% L-arabinose under oxygen deprivation, cells metabolize L-arabinose at a constant rate, resulting in combined organic acids yield based on the amount of sugar mixture consumed after D-glucose depletion of 83% that is comparable to that before D-glucose depletion, 89%
synthesis
-
coexpression of beta-D-galactosidase gene and L-arabinose isomerase mutant Q299K for synthesis of D-tagatose. Recombinant cells exhibit maximum D-tagatose producing activity at 34°C and pH 6.5 and in the presence of borate, 10 mM Fe2+, and 1 mM Mn2+. Cells can hydrolyze more than 95% lactose and convert 43% D-galactose into D-tagatose
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
additional information
additionally, tagatose can potentially be used as a prescription drug additive to mask unpleasant tastes, and as a sweetener in toothpaste, mouthwash, and cosmetics such as flavoured lipstick
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sa-Nogueira, I.; Nogueira, T.V.; Soares, S.; de Lencastre, H.
The Bacillus subtilis L-arabinose (ara) operon: nucleotide sequence, genetic organization and expression
Microbiology
143
957-969
1997
Bacillus subtilis, Escherichia coli
Pauley, J.; Power, J.; Irr, J.
L-Arabinose isomerase formation in a conditional mutant of gene araA of Escherichia coli B/r
J. Bacteriol.
112
1247-1253
1972
Escherichia coli, Escherichia coli B/r
Patrick, J.; Lee, N.
L-Arabinose isomerase
Methods Enzymol.
41B
453-458
1975
Escherichia coli, Escherichia coli B/r
Wallace, L.J.; Eiserling, F.A.; Wilcox, G.
The shape of L-arabinose isomerase from Escherichia coli
J. Biol. Chem.
253
3717-3720
1978
Escherichia coli
Deanda, K.; Zhang, M.; Eddy, C.; Picataggio, S.
Development of an arabinose-fermenting Zymomonas mobilis strain by metabolic pathway engineering
Appl. Environ. Microbiol.
62
4465-4470
1996
Escherichia coli
Banerjee, S.; Anderson, F.; Farber, G.K.
The evolution of sugar isomerases
Protein Eng.
8
1189-1195
1995
Escherichia coli
Kim, P.
Current studies on biological tagatose production using L-arabinose isomerase: a review and future perspective
Appl. Microbiol. Biotechnol.
65
243-249
2004
Bacillus subtilis (P94523), Bacteroides thetaiotaomicron (Q8AAW1), Bifidobacterium longum (Q8G7J3), Clostridium acetobutylicum (Q97JE0), Clostridium acetobutylicum (Q97JE4), Escherichia coli (P08202), Escherichia coli (P58538), Escherichia coli (Q8FL89), Geobacillus stearothermophilus, Halalkalibacterium halodurans (Q9KBQ2), Klebsiella aerogenes, Lactiplantibacillus plantarum (Q88S84), Lactobacillus gayonii, Oceanobacillus iheyensis (Q8EMP4), Salmonella enterica subsp. enterica serovar Typhi (P58539), Salmonella enterica subsp. enterica serovar Typhimurium (P06189), Shigella flexneri (Q7UDT4), Thermoanaerobacter mathranii, Thermotoga maritima (Q9WYB3), Thermotoga neapolitana, Thermus sp., Vibrio parahaemolyticus, Yersinia pestis (P58540)
Kawaguchi, H.; Sasaki, M.; Vertes, A.A.; Inui, M.; Yukawa, H.
Engineering of an L-arabinose metabolic pathway in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
77
1053-1062
2008
Escherichia coli
Manjasetty, B.A.; Chance, M.R.
Crystal structure of Escherichia coli L-arabinose isomerase (ECAI), the putative target of biological tagatose production
J. Mol. Biol.
360
297-309
2006
Escherichia coli (P08202), Escherichia coli
Kim, J.H.; Lim, B.C.; Yeom, S.J.; Kim, Y.S.; Kim, H.J.; Lee, J.K.; Lee, S.H.; Kim, S.W.; Oh, D.K.
Differential selectivity of the Escherichia coli cell membrane shifts the equilibrium for the enzyme-catalyzed isomerization of galactose to tagatose
Appl. Environ. Microbiol.
74
2307-2313
2008
Escherichia coli
Kim, H.; Uhm, T.; Kim, S.; Kim, P.
Escherichia coli arabinose isomerase and Staphylococcus aureus tagatose-6-phosphate isomerase: Which is a better template for directed evolution of non-natural substrate isomerization?
J. Microbiol. Biotechnol.
20
1018-1021
2010
Escherichia coli
Wang, Y.; Luo, X.; Li, X.; Zhang, T.
Production of D-tagatose with recombinant Escherichia coli strain secreting beta-galactosidase and L-arabinose isomerase from E. coli K-12
J. Pure Appl. Microbiol.
7
1497-1504
2013
Escherichia coli
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