Information on EC 5.3.1.3 - D-arabinose isomerase

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The expected taxonomic range for this enzyme is: Bacteria

EC NUMBER
COMMENTARY
5.3.1.3
-
RECOMMENDED NAME
GeneOntology No.
D-arabinose isomerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
D-Arabinose = D-ribulose
show the reaction diagram
-
-
-
-
D-Arabinose = D-ribulose
show the reaction diagram
protein environment suggests strongly that the reaction belongs to the ene-diol type
-
PATHWAY
KEGG Link
MetaCyc Link
D-arabinose degradation I
-
D-arabinose degradation II
-
SYSTEMATIC NAME
IUBMB Comments
D-arabinose aldose-ketose-isomerase
Requires a divalent metal ion (the enzyme from the bacterium Escherichia coli prefers Mn2+). 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 [3]. The enzyme catalyses the aldose-ketose isomerization of several sugars. Most enzymes also catalyse the reaction of EC 5.3.1.25, L-fucose isomerase [3]. The enzyme from the bacterium Falsibacillus pallidus also converts D-altrose to D-psicose [4]. cf. EC 5.3.1.4, L-arabinose isomerase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D-AI
Aeribacillus pallidus 14A
-
-
-
D-arabinose aldose-ketose-isomerase
-
-
D-arabinose aldose-ketose-isomerase
Klebsiella pneumoniae 40bXX
-
-
-
D-Arabinose isomerase
-
-
-
-
D-Arabinose isomerase
-
-
D-Arabinose isomerase
C0SSE7
L-fucose isomerase, bifunctional enzyme
D-Arabinose isomerase
Aeribacillus pallidus 14A
-
-
-
D-Arabinose isomerase
A4XJ56
L-fucose isomerase, bifunctional enzyme
D-Arabinose isomerase
-
D-AI
D-Arabinose isomerase
Klebsiella pneumoniae 40bXX
-
D-AI
-
D-arabinose ketol-isomerase
-
-
-
-
D-Arabinose(L-fucose) isomerase
-
-
-
-
EC 5.1.3.25
-
-
related
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Isomerase, arabinose
-
-
-
-
L-Fucose isomerase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9023-81-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 14A
-
-
Manually annotated by BRENDA team
Aeribacillus pallidus 14A
strain 14A
-
-
Manually annotated by BRENDA team
strain B/r; strain K-12
-
-
Manually annotated by BRENDA team
strain K-12; wild type and mutant strains which constitutively synthesize the enzyme
-
-
Manually annotated by BRENDA team
Escherichia coli B/r
strain B/r
-
-
Manually annotated by BRENDA team
mutants which are capable of utilizing D-arabinose as a sole source of carbon and energy for growth
-
-
Manually annotated by BRENDA team
strain PRL-R3
-
-
Manually annotated by BRENDA team
strain W70, wild type enzyme and constitutive mutants
-
-
Manually annotated by BRENDA team
wild type strain PRL-R3 and two constitutive mutants, 502 and 510
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae 40bXX
40bXX
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae M-7
strain M-7
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae PRL-R3
strain PRL-R3
-
-
Manually annotated by BRENDA team
Klebsiella pneumoniae W70
strain W70, wild type enzyme and constitutive mutants
-
-
Manually annotated by BRENDA team
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1823
-
D-arabinose
A4XJ56
-
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
10
-
7.0: sharp decrease in activity below, 8.0-10.0: maximal activity
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexamer
-
6 * 64976, crystallographic data
hexamer
-
x-ray crystallography
hexamer
Aeribacillus pallidus 14A
-
x-ray crystallography
-
homohexamer
C0SSE7
-
homotrimer
A4XJ56
3 * 68000 Da
tetramer
-
4 * 84600, Escherichia coli B/r, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea; 4 * 90900, Escherichia coli K-12, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea
tetramer
Escherichia coli B/r
-
4 * 84600, Escherichia coli B/r, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea; 4 * 90900, Escherichia coli K-12, high speed sedimentation of enzyme dissociated into subunits by protonation at pH 2 or dialysis against buffer containing 8 M urea
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli strain JM109
-
for over-expression in Escherichia coli JM109 cells
C0SSE7
into the vector pGEM-T Easy, and subsequently into the vector pET15b for expression in Escherichia coli ER2566 cells
A4XJ56
nucleotide sequence of the gene fucI
-
organization of the fuc regulon specifying L-fucose dissimilation as determined by gene cloning
-
overexpression in Escherichia coli
-