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Information on EC 5.3.1.4 - L-arabinose isomerase and Organism(s) Acidothermus cellulolyticus and UniProt Accession A0LT86

for references in articles please use BRENDA:EC5.3.1.4
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IUBMB 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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This record set is specific for:
Acidothermus cellulolyticus
UNIPROT: A0LT86
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Word Map
The taxonomic range for the selected organisms is: Acidothermus cellulolyticus
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Isomerase, L-arabinose
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L-arabinose ketol-isomerase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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intramolecular oxidoreduction
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PATHWAY SOURCE
PATHWAYS
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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 hide
9023-80-7
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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-galactose
D-tagatose
show the reaction diagram
conversion yield over 50% after 12 h under optimal conditions
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?
L-arabinose
L-ribulose
show the reaction diagram
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-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-arabinose
L-ribulose
show the reaction diagram
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
activates and increase thermostability of the enzyme
Mn2+
activates and increase thermostability of the enzyme
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Cu2+
30% inhibition at 1 mM
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
over 90% of maximal activity at pH 6.0, maximal activity at pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.63
sequence calculation
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 43068, gene araA
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54768
x * 54768, sequence calculation, x * 55000, recombinant enzyme, SDS-PAGE
55000
x * 54768, sequence calculation, x * 55000, recombinant enzyme, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 54768, sequence calculation, x * 55000, recombinant enzyme, SDS-PAGE
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
25°C, purified recombinant enzyme, 80% activity remaining after 12 h, 70% after 24 h
701868
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
65
purified recombinant enzyme, completely stable for 2 h
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme from Escherichia coli strain BL21(DE3) by heat treatment, ion exchange chromatography, and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene araA, DNA and amino acid sequence determination and analysis, expression in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Cheng, L.; Mu, W.; Zhang, T.; Jiang, B.
An L-arabinose isomerase from Acidothermus cellulolytics ATCC 43068: cloning, expression, purification, and characterization
Appl. Microbiol. Biotechnol.
86
1089-1097
2010
Acidothermus cellulolyticus (A0LT86), Acidothermus cellulolyticus
Manually annotated by BRENDA team