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Information on EC 5.3.1.4 - L-arabinose isomerase and Organism(s) Bacillus subtilis and UniProt Accession P94523
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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: Bacillus subtilis
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 nc8, l-ai us100, d-galactose isomerase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Isomerase, L-arabinose
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-
-
-
L-arabinose ketol-isomerase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
-
-
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intramolecular oxidoreduction
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-
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-
PATHWAY SOURCE
PATHWAYS
BRENDA
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-
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
L-ribulose
L-arabinose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
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-
r
L-arabinose
L-ribulose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
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-
r
L-arabinose
L-ribulose
the enzyme shows high substrate specificity
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-
r
L-arabinose
L-ribulose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
-
-
r
additional information
?
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no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview
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-
?
additional information
?
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-
no activity with L-ribose, L-xylose, D-galactose, D-mannose, and D-xylose. Wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview
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-
?
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
L-ribulose
L-arabinose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
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-
r
L-arabinose
L-ribulose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of Larabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
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-
r
L-arabinose
L-ribulose
L-arabinose isomerase is an intracellular enzyme that catalyzes the reversible isomerization of L-arabinose to L-ribulose, a component of the pentose phosphate or the phosphoketolase pathways
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM
additional information
-
the enzyme is not stimulated by Mg2+, Ca2+, Zn2+, Fe2+, or Ni2+ at 1 mM each, and is unaffected by EDTA at concentrations ranging from 1 to 10 mM
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
241.7
L-aldose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
241.7
L-ribulose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.02
L-aldose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
2.02
L-ribulose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 9
31%, 68%, 87%, and 48% of maximum activity at pH 6.0, pH 7.0, pH 8.0, and pH 9.0, respectively
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview
additional information
-
wild-type and mutant enzymes, homology modeling and substrate docking analysis, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene araA, DNA and amino acid sequence determination and analysis, His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
nutrition
there has been industrial interest in the end product D-tagatose as a low-calorie sugar-substituting sweetener
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
Sa-Nogueira, I.; Paveia, H.; De Lencastre, H.
Isolation of constitutive mutants for L-arabinose utilization in Bacillus subtilis
J. Bacteriol.
170
2855-2857
1988
Bacillus subtilis
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)
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