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Information on EC 1.1.1.376 - L-arabinose 1-dehydrogenase [NAD(P)+] and Organism(s) Azospirillum brasilense and UniProt Accession Q53TZ2
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1.1.1.376 L-arabinose 1-dehydrogenase [NAD(P)+]IUBMB Comments
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. The enzyme is specific for alpha-L-arabinopyranose [3,4].
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The taxonomic range for the selected organisms is: Azospirillum brasilense
The expected taxonomic range for this enzyme is: Bacteria, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
hvo_b0032, nad(p)-dependent l-arabinose 1-dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-arabinose 1-dehydrogenase
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
alpha-L-arabinopyranose: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. The enzyme is specific for alpha-L-arabinopyranose [3,4].
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
D-galactose + NAD+
?
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
D-galactose + NADP+
?
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
additional information
?
-
no activity with D-arabinose, D-glucose, D-ribose, L-xylose, L-mannose, L-lyxose, and D-fructose (less than 1% of the activity with L-arabinose)
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
L-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
the enzyme shows high catalytic efficiency for both L-arabinose and D-galactose. The enzyme prefers NADP+ over NAD+
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
-
-
?
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-arabinose + NAD+
L-arabinono-1,4-lactone + NADH + H+
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
-
-
-
?
L-arabinose + NADP+
L-arabinono-1,4-lactone + NADPH + H+
first step of L-arabinose metabolism. The enzyme is involved in the metabolism of L-arabinose but not D-galactose
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
570fold higher affinity with NADP+ (Km: 0.0028 mM) than NAD (Km: 1.586) when L-arabinose is used as a substrate. kcat value for NADP+ is 62.3/s, which is slightly smaller than that for NAD+ (105.9/s)
NAD+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
NAD+
preference of NADP+ over NAD+, wild-type enzyme. Mutant enzyme S37D/R38A shows a complete reversal of coenzyme specificity
NADP+
570fold higher affinity with NADP+ (Km: 0.0028 mM) than NAD (Km: 1.586) when L-arabinose is used as a substrate. kcat value for NADP+ is 62.3/s, which is slightly smaller than that for NAD+ (105.9/s)
NADP+
preference of NADP+ over NAD+ is significantly subjected by a pair of Ser37 and Arg38
NADP+
preference of NADP+ over NAD+, wild-type enzyme. Mutant enzyme S37D/R38A shows a complete reversal of coenzyme specificity
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
no significant increase in activity in the presence of MgCl2, MnCl2, ZnCl2, CoCl2, NiCl2, or CaCl2 at final concentrations of 1 mM
additional information
-
no enhancement of activity in presence of divalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.109
D-galactose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
1.49
D-galactose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
3.95
D-talose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
5.87
D-talose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
2 - 10
D-xylose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
72
D-xylose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.255
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.26
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
0.785
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
1.41
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
28.9
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
42.5
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19.8
D-galactose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
26
D-galactose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
1.04
D-talose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
9.7
D-talose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
4
D-xylose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
12
D-xylose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.1
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A
0.3
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
6.1
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
16.5
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
19
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
33.3
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.3
D-galactose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
240
D-galactose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
0.26
D-talose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
1.6
D-talose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
0.019
D-xylose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
0.17
D-xylose
pH 9.0, 30°C, cofactor: NADP*, enzyme purified from Azospirillum brasilense
0.01
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, mutant enzyme N172A
0.03
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, mutant enzyme N172A
7.78
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, recombinant wild-type enzyme
13.4
L-arabinose
pH 9.0, 30°C, cofactor: NAD+, enzyme purified from Azospirillum brasilense
63.5
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, recombinant wild-type enzyme
131
L-arabinose
pH 9.0, 30°C, cofactor: NADP+, enzyme purified from Azospirillum brasilense
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.7
pH 9.0, 30°C, D-talose + 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
5.3
pH 9.0, 30°C, D-xylose + NAD+, enzyme purified from Azospirillum brasilense
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a disruptant of the L-arabinose 1-dehydrogenase gene does not grow on L-arabinose but grows on D-galactose at the same growth rate as the wild-type strain
metabolism
the enzyme is responsible for the first step of the non-phosphorylative L-arabinose pathway from bacteria
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapor diffusion method at 20°C, crystal structures of apo- and NADP-bound AraDH at 1.5 and 2.2 A resolutions
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D168A
mutant shows no activity under standard assay conditions
H119N
N172A
kinetic analysis shows that the N172A mutant decreases by 4 orders of magnitude in kcat/Km values, compared with the wild-type enzyme
N173A
N173G
N173Q
N173S
N173V
S37D
7.3fold increase in Km-value for NADP+ and 6.5fold decrease in KM-value for NAD+
S37D/R38A
mutant enzyme shows a complete reversal of coenzyme specificity. The kcat/Km value for NADP+ decreases further by 20fold from that of the S37D mutant, and the ratio of NADP+ to NAD+ is about 0.07
W152A
W152F
W152H
W152Y
W231A
H119N
kcat/KM for L-arabinose is 8088fold lower than the wild-type value
H119N
mutant emzyme is significantly active, Km value is markedly higher (4450fold) than that of wild-type
N173A
kcat/KM for L-arabinose is 6111fold lower than the wild-type value
N173G
kcat/KM for L-arabinose is 3427fold lower than the wild-type value
N173Q
kcat/KM for L-arabinose is 9735fold lower than the wild-type value
N173S
kcat/KM for L-arabinose is 7051fold lower than the wild-type value
N173V
kcat/KM for L-arabinose is 1874fold lower than the wild-type value
W152A
kcat/KM for L-arabinose is 106fold lower than the wild-type value
W152A
the kcat/Km value by 2 orders of magnitude from wild-type enzyme
W152F
kcat/KM for L-arabinose is 28.4fold lower than the wild-type value
W152F
mutant shows an 14fold higher Km value than the W152Y mutant
W152H
kcat/KM for L-arabinose is 2.8fold lower than the wild-type value
W152Y
kcat/KM for L-arabinose is 1.7fold lower than the wild-type value
W152Y
mutant shows an 14fold higher Km value than the W152Y mutant
W231A
kcat/KM for L-arabinose is 33.2fold lower than the wild-type value
W231A
the kcat/Km value by 2 orders of magnitude from wild-type enzyme
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene with a N-terminal (His)6-tag is expressed in Escherichia coli BL21(DE3) cells
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Novick, N.J.; Tyler, M.E.
Partial purification and properties of an L-arabinose dehydrogenase from Azospirillium brasilense
Can. J. Microbiol.
29
242-246
1983
Azospirillum brasilense
-
Watanabe, S.; Kodaki, T.; Kodak, T.; Makino, K.
Cloning, expression, and characterization of bacterial L-arabinose 1-dehydrogenase involved in an alternative pathway of L-arabinose metabolism
J. Biol. Chem.
281
2612-2623
2006
Azospirillum brasilense (Q53TZ2), Azospirillum brasilense DSM 1690 (Q53TZ2)
Yoshiwara, K.; Watanabe, S.; Watanabe, Y.
Crystal structure of bacterial L-arabinose 1-dehydrogenase in complex with L-arabinose and NADP
Biochem. Biophys. Res. Commun.
530
203-208
2020
Azospirillum brasilense (Q53TZ2), Azospirillum brasilense ATCC 29145 (Q53TZ2)
Watanabe, Y.; Iga, C.; Watanabe, Y.; Watanabe, S.
Structural insights into the catalytic and substrate recognition mechanisms of bacterial L-arabinose 1-dehydrogenase
FEBS Lett.
593
1257-1266
2019
Azospirillum brasilense (Q53TZ2), Azospirillum brasilense, Azospirillum brasilense ATCC29145 (Q53TZ2)
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