Information on EC 5.3.1.4 - L-arabinose isomerase

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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
5.3.1.4
-
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RECOMMENDED NAME
GeneOntology No.
L-arabinose isomerase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-Arabinose = L-ribulose
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
intramolecular oxidoreduction
-
-
-
-
isomerization
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arabinose degradation I
-
-
degradation of pentoses
-
-
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-arabinose aldose-ketose-isomerase
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+) [2]. The enzyme binds the closed form of the sugar and catalyses ring opening to generate a form of open-chain conformation that facilitates the isomerization reaction, which proceeds via an ene-diol mechanism [5]. The enzyme can also convert D-galactose to D-tagatose with lower efficiency [4].
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-80-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 43068, gene araA
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene araA
Uniprot
Manually annotated by BRENDA team
gene araA
-
-
Manually annotated by BRENDA team
gene araA
-
-
Manually annotated by BRENDA team
Lactobacillus gayonii
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-Allose
?
show the reaction diagram
D-Allose
D-Psicose
show the reaction diagram
16%, relative activity compared to activity with D-galactose
-
-
?
D-Fucose
?
show the reaction diagram
D-fucose
D-fuculose
show the reaction diagram
221% activity compared to D-galactose
-
-
r
D-Galactose
?
show the reaction diagram
Lactobacillus gayonii
-
weak activity
-
-
-
D-galactose
D-tagatose
show the reaction diagram
D-glucose
?
show the reaction diagram
D-gulose
D-sorbose
show the reaction diagram
1.3%, relative activity compared to activity with D-galactose
-
-
?
D-rhamnose
?
show the reaction diagram
28% activity compared to D-galactose
-
-
?
D-Ribose
?
show the reaction diagram
D-ribulose
?
show the reaction diagram
12%, relative activity compared to activity with D-galactose
-
-
?
D-sorbose
?
show the reaction diagram
31% activity compared to D-galactose
-
-
?
D-tagatose
D-galactose
show the reaction diagram
-
-
-
-
r
D-xylose
-
show the reaction diagram
D-Xylose
?
show the reaction diagram
D-Xylose
D-Xylulose
show the reaction diagram
7.0%, relative activity compared to activity with D-galactose
-
-
?
L-Arabinose
?
show the reaction diagram
L-Arabinose
L-Ribulose
show the reaction diagram
L-Fucose
?
show the reaction diagram
L-Fucose
L-Fuculose
show the reaction diagram
-
only F279 mutant
-
-
?
L-ribulose
L-arabinose
show the reaction diagram
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
D-fucose
D-fuculose
show the reaction diagram
K7SW59
221% activity compared to D-galactose
-
-
r
D-galactose
D-tagatose
show the reaction diagram
L-Arabinose
?
show the reaction diagram
L-Arabinose
L-Ribulose
show the reaction diagram
L-ribulose
L-arabinose
show the reaction diagram
C7F8M0
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
?
-
Q65J10
other aldoses than L-arabinose including D-galactose are ineffective as substrate (1% or less, compared with L-arabinose)
-
-
-
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K+
Lactobacillus gayonii
-
slight activation
Sr2+
Lactobacillus gayonii
-
slight activation
additional information
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Dulcitol
erythritol
L-arabitol
Li+
about 90% residual activity at 1 mM
mannitol
weak inhibitor
Na+
about 90% residual activity at 1 mM
ribitol
xylitol
additional information
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Borate
iso-inositol
-
enhances activity to 108%
mannitol
-
enhances activity to 105%
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3 - 2564
D-galactose
11 - 114
D-tagatose
5.2 - 770
L-arabinose
173.6
L-fucose
-
F279Q mutant
5 - 18
L-ribulose
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.02 - 78.5
D-galactose
0.06 - 0.82
D-tagatose
241.7
L-aldose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
0.9 - 3657
L-arabinose
241.7
L-ribulose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0023 - 0.173
D-galactose
2.02
L-aldose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
0.01 - 1.08
L-arabinose
2.02
L-ribulose
pH 7.5, 23°C, recombinant His6-tagged wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7.9 - 36
L-arabitol
183
L-ribitol
-
at pH 7.0 and 50°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.004
D228N mutant, D-galactose as substrate
0.026
cell extract, at pH 7.5 and 52°C
0.029
R408V mutant, D-galactose as substrate
0.043
wild type, D-galactose as substrate
0.05
L408V mutant, D-galactose as substrate
0.055
recovered activity after immobilization of the enzyme
0.06
Q408V mutant, at pH 7.5, D-galactose as substrate; R408V mutant, at pH 7.5, D-galactose as substrate
0.062
Q408V mutant, D-galactose as substrate
0.103
activity determined from the cell extracts of Escherichia coli UP1110 3 h after the onset of IPTG induction
0.11
T393S mutant, D-galactose as substrate
0.122
-
after ammonium sulfate precipitation
0.14
-
wild type, D-galactose as substrate
0.163
-
after heat treatment
0.183
activity determined from the cell extracts of Lactobacillus plantarum BPT232 1h after the induction with the peptide SPPIP
0.232
after 8.9fold purification, at pH 7.5 and 52°C
0.25
-
cell-free extract, at pH 7.0 and 50°C
0.26
N428K mutant, D-galactose as substrate
0.27
V322M mutant, D-galactose as substrate
0.37
G408V mutant, D-galactose as substrate; Q475N mutant, D-galactose as substrate
0.38
R475N mutant, D-galactose as substrate
0.39
K475N mutant, D-galactose as substrate; K475N mutant found in GSAI152, D-galactose as substrate
0.48
A408V mutant, D-galactose as substrate; A475N mutant found in GSAI153, D-galactose as substrate
0.49
GSAI1 152, D-galactose as substrate
0.59
A408V/K475N mutant found in GSAI152 or GASI 153w D-galactose as substrate
0.74
GSAI1 153, D-galactose as substrate
0.84
-
in the absence of Mn2+, at pH 7.5 and 60°C
0.9
-
purified enzyme, in the absence of Mn2+, at pH 7.5 and 60°C
1
-
after Hi-trap Q ion exchange chromatography
1 - 2
-
mutant enzyme D299E, at pH 7.0 and 65°C
1.3
-
with D-galactose as substrate
1.72
-
after Biogel hydroxyapatite ion exchange chromatography
2.1
-
purified recombinant enzyme ion exchange chromatography
2.3
-
of the recombinant wild type enzyme after purification
2.5
-
purified enzyme, in the absence of Mn2+, at pH 7.5 and 60°C
3
purified recombinant mutant Y333A
4.03
-
in the presence of Mn2+, at pH 7.5 and 60°C
4.57
-
purified enzyme, at pH 7.5 and 60°C
4.6
-
mutant enzyme D268K/D299K, at pH 5.5-6.0 and 65°C
4.82
-
wild type, L-arabinose as substrate
5.3
-
mutant enzyme D268K, at pH 6.5-7.0 and 65°C
5.31
Lactobacillus gayonii
-
-
6.4
-
mutant enzyme D268E, at pH 6.5-7.0 and 65°C
6.8
-
mutant enzyme D268E, at pH 7.5 and 65°C
6.9
-
purified enzyme, in the presence of 1 mM Mn2+, at pH 7.5 and 60°C
7.1
-
mutant enzyme D268K/D269K, at pH 5.0 and 65°C
7.8
-
purified enzyme, in the presence of 1 mM Mn2+, at pH 7.5 and 60°C
8.9
-
with D-galactose as substrate
9
-
with D-galactose as substrate
9.2
-
mutant enzyme D269K/D299K, at pH 5.0 and 65°C
9.7
-
mutant enzyme D268R, at pH 5.5 and 65°C; mutant enzyme D269R, at pH 6.0 and 65°C
9.9
-
mutant enzyme D299K, at pH 5.0 and 65°C
11
-
wild type enzyme, at pH 6.5 and 65°C
12.7
-
mutant enzyme D268K/D269K/D299K, at pH 5.0 and 65°C
14.3
-
mutant enzyme D269K, at pH 5.0-5.5 and 65°C
17
-
wild-type with L-arabinose as substrate at pH 6 and 50°C
25.3
-
wild-type with L-arabinose as substrate at pH 7 and 50°C
25.8
-
mutant E268K with L-arabinose as substrate at pH 6 and 50°C
26.8
wild-type with L-arabinose as substrate at pH 8 and 65°C
27.6
mutant K269E with L-arabinose as substrate at pH 8 and 65°C
28
recombinant purified mutant Y333I
30.6
wild-type with L-arabinose as substrate at pH 7 and 65°C
31.7
-
mutant E268K with L-arabinose as substrate at pH 8 and 50°C
33.1
-
with L-arabinose as substrate
33.2
-
wild-type with L-arabinose as substrate at pH 8 and 50°C
35.3
-
mutant E268K with L-arabinose as substrate at pH 7 and 50°C
35.5
wild-type with L-arabinose as substrate at pH 6 and 65°C
36.5
-
with L-arabinose as substrate
39.9
mutant K269E with L-arabinose as substrate at pH 7 and 65°C
41.3
-
with L-arabinose as substrate
69
purified recombinant enzyme expressed in Bacillus subtilis, D-galactose isomerization
97
purified recombinant enzyme expressed in Bacillus subtilis, L-arabinose isomerization
105
purified recombinant wild-type enzyme
180
-
after 720fold purification, at pH 7.0 and 50°C
185
-
after purification with FPLC
253
after purification to homogeneity
262
purified recombinant enzyme
263.4
after purification to homogeneity
additional information
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