Information on EC 1.1.1.376 - L-arabinose 1-dehydrogenase [NAD(P)+]

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The expected taxonomic range for this enzyme is: Bacteria, Archaea

EC NUMBER
COMMENTARY hide
1.1.1.376
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RECOMMENDED NAME
GeneOntology No.
L-arabinose 1-dehydrogenase [NAD(P)+]
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arabinose + NAD(P)+ = L-arabinono-1,4-lactone + NAD(P)H + H+
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
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L-arabinose degradation III
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L-arabinose degradation IV
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degradation of pentoses
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SYSTEMATIC NAME
IUBMB Comments
L-arabinose:NAD(P)+ 1-oxidoreductase
The enzymes from the bacterium Azospirillum brasilense and the archaeon Haloferax volcanii are part of the L-arabinose degradation pathway and prefer NADP+ over NAD+. In vitro the enzyme from Azospirillum brasilense shows also high catalytic efficiency with D-galactose.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
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first enzyme in metabolism of L-arabinose
physiological function
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 + NAD+
?
show the reaction diagram
D-galactose + NADP+
?
show the reaction diagram
D-talose + NAD+
?
show the reaction diagram
low activity
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-
?
D-talose + NADP+
?
show the reaction diagram
low activity
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-
?
D-xylose + NAD+
?
show the reaction diagram
D-xylose + NADP+
?
show the reaction diagram
L-arabinose + NAD(P)+
L-arabinono-1,4-lactone + NAD(P)H + H+
show the reaction diagram
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
show the reaction diagram
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
show the reaction diagram
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
L-arabinose + NAD(P)+
L-arabinono-1,4-lactone + NAD(P)H + H+
show the reaction diagram
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
show the reaction diagram
Q53TZ2
first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl
NaCl
activity is dependent on KCl and NaCl. Maximal activities are obtained at 1.5 M KCl and 1 M NaCl
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
CoCl2
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10 mM, 54% inhibition
dithiothreitol
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1 mM, 10% inhibition
EDTA
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2.5 mM, 8% inhibition
FeSO4
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10 mM, 30% inhibition
MnCl2
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10 mM, 45% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.109 - 1.49
D-galactose
3.95 - 5.87
D-talose
2 - 72
D-xylose
0.075 - 42.5
L-arabinose
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
19.8 - 26
D-galactose
1.04 - 9.7
D-talose
4 - 12
D-xylose
0.1 - 33.3
L-arabinose
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.3 - 240
D-galactose
71
0.26 - 1.6
D-talose
2017
0.019 - 0.17
D-xylose
115
0.01 - 131
L-arabinose
206
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.042
pH 9.0, 30°C, L-arabinose + NAD+, mutant enzyme N172A
0.148
pH 9.0, 30°C, L-arabinose + NADP+, mutant enzyme N172A
1.7
pH 9.0, 30°C, D-talose + NAD+, enzyme purified from Azospirillum brasilense
2.6
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pH 9.0, 25°C, L-arabinose + NADP+
4.1
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pH 9.0, 25°C, L-arabinose + NAD+
5.3
pH 9.0, 30°C, D-xylose + NAD+, enzyme purified from Azospirillum brasilense
12.8
pH 9.0, 30°C, D-talose + NADP+, enzyme purified from Azospirillum brasilense
14.8
pH 9.0, 30°C, D-xylose + NADP+, enzyme purified from Azospirillum brasilense
14.9
pH 9.0, 30°C, L-arabinose + NAD+, recombinant wild-type enzyme
23.8
pH 9.0, 30°C, D-galactose + NAD+, enzyme purified from Azospirillum brasilense
25
pH 9.0, 30°C, L-arabinose + NAD+, enzyme purified from Azospirillum brasilense
32
pH 9.0, 30°C, L-arabinose + NADP+, recombinant wild-type enzyme
35.6
pH 9.0, 30°C, D-galactose + NADP+, enzyme purified from Azospirillum brasilense
44.9
pH 9.0, 30°C, L-arabinose + NADP+, enzyme purified from Azospirillum brasilense
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 10
50% of maximal activity is found at pH values of 6 and 10
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28000
4 * 28000, SDS-PAGE
33664
1 * 33664, calculated from sequence
39500
1 * 39500, SDS-PAGE
46400
gel filtration
130000
gel filtration
175000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homotetramer
monomer
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
55
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stable for 5 min
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
overexpression in Escherichia coli
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the gene is induced by L-arabinose but not by D-galactose
transcriptionally induced by both L-arabinose and D-xylose
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D168A
mutant shows no activity under standard assay conditions
N172A
kinetic analysis shows that the N172A mutant decreases by 4 orders of magnitude in kcat/Km values, compared with the wild-type enzyme
D168A
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mutant shows no activity under standard assay conditions
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N172A
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kinetic analysis shows that the N172A mutant decreases by 4 orders of magnitude in kcat/Km values, compared with the wild-type enzyme
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