Information on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.12
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RECOMMENDED NAME
GeneOntology No.
L-arabinitol 4-dehydrogenase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-arabinitol + NAD+ = L-xylulose + NADH + H+
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-arabinose degradation II
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Metabolic pathways
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Pentose and glucuronate interconversions
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SYSTEMATIC NAME
IUBMB Comments
L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-19-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
strain PYCC 5603, analysis of L-arabinose catabolic pathway
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Manually annotated by BRENDA team
strain ATCC 28089 /DSM 1075 /Wisconsin 54-1255
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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induction of gene expression of the alpha-L-arabinofuranosidase encoding genes abf1, abf2, and abf3 and also bxl1, which encodes a beta-xylosidase with a separate alpha-L-arabinofuranosidase domain and activity, by L-arabinitol is strongly enhanced in a DELTAlad1 strain lacking L-arabinitol dehydrogenase activity and severely impaired in an aldose reductase DELTAxyl1 strain, suggesting a cross talk between L-arabinitol and the aldose reductase XYL1 in alpha-L-arabinofuranosidase gene expression
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
adonitol + NAD+
? + NADH
show the reaction diagram
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-
-
-
?
adonitol + NAD+
? + NADH + H+
show the reaction diagram
-
-
-
?
D-adonitol + NAD+
?
show the reaction diagram
-
-
-
-
?
D-allitol + NAD+
D-psicose + NADH
show the reaction diagram
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-
-
-
r
D-arabino-3-hexulose + NADH
D-talitol + NAD+
show the reaction diagram
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-
-
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r
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
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-
-
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r
D-psicose + NADH
D-allitol + NAD+
show the reaction diagram
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-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
show the reaction diagram
wild-type shows no activity on D-sorbitol, whereas mutant Y318F does
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?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbose + NADH
D-gulitol + NAD+
show the reaction diagram
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-
-
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?
galactitol + NAD+
L-xylo-3-hexulose + NADH
show the reaction diagram
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-
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r
L-arabinitol + NAD+
? + NADH
show the reaction diagram
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-
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?
L-arabinitol + NAD+
L-xylulose + NADH
show the reaction diagram
L-arabinitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
L-arabinitol + NADP+
L-xylulose + NADPH + H+
show the reaction diagram
no activity with cofactor NADP+ for wild-type
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?
L-arabitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
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?
L-iditol + NAD+
L-sorbose + NADH
show the reaction diagram
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-
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r
L-mannitol + NAD+
L-fructose + NADH
show the reaction diagram
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-
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r
L-sorbitol + NAD+
? + NADH
show the reaction diagram
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-
-
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?
L-tagatose + NADH
L-talitol + NAD+
show the reaction diagram
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-
-
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?
L-talitol + NAD+
D-arabino-3-hexulose + NADH
show the reaction diagram
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-
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r
L-xylo-3-hexulose + NADH
galactitol + NAD+
show the reaction diagram
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-
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r
ribitol + NAD+
?
show the reaction diagram
93% of the activity with L-arabinitol
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?
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + 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-arabinitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADP+
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very low yet detectable activity with NADP+, strong preference for NAD+
additional information
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
35
adonitol
-
pH 8.0, 25C
11.3
D-allitol
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pH 8.6, 25C
580
D-arabino-3-hexulose
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pH 8.6, 25C
96
D-fructose
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pH 8.6, 25C
81
D-psicose
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pH 8.6, 25C
0.868 - 483.5
D-sorbitol
115
D-sorbose
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pH 8.6, 25C
25
D-talitol
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pH 8.6, 25C
60
galactitol
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pH 8.6, 25C
0.056 - 57
L-arabinitol
0.056 - 0.078
L-arabitol
191
L-Iditol
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pH 8.6, 25C
37
L-mannitol
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pH 8.6, 25C
19
L-sorbitol
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pH 8.6, 25C
28
L-tagatose
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pH 8.6, 25C
81
L-xylo-3-hexulose
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pH 8.6, 25C
5
L-xylulose
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30C, pH 9.6
0.05 - 174
NAD+
0.008
NADH
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30C, pH 9.6
0.48 - 8
NADP+
0.218 - 290
xylitol
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
18
adonitol
Neurospora crassa
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pH 8.0, 25C
3.7 - 833
D-sorbitol
5.3 - 30
L-arabinitol
863 - 1800
L-arabitol
3.18 - 20.1
NAD+
8.23 - 20.16
NADP+
3.25 - 2208
xylitol
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
D-sorbitol
Rasamsonia emersonii
C5J3R8
pH 9, 30C
627
0.32 - 0.39
L-arabinitol
2564
0.88 - 79
NAD+
7
8.27 - 36.6
NADP+
10
0.14
xylitol
Rasamsonia emersonii
C5J3R8
pH 9, 30C
416
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.7
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pH 7.0, 22C
11.7
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pH 7.0, 22C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10.5
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more than 60% of maximal activity within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
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4 * 39000, SDS-PAGE, 4 * 39600, calculated
39600
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4 * 39000, SDS-PAGE, 4 * 39600, calculated
41000
x * 41000, calculated, x * 45000, SDS-PAGE
45000
x * 41000, calculated, x * 45000, SDS-PAGE
152000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 41000, calculated, x * 45000, SDS-PAGE
tetramer
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4 * 39000, SDS-PAGE, 4 * 39600, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
modelling of LadA on human SDH identifies residues M70 and Y318 in LadA, that may explain the absence of activity on D-sorbitol
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molecular replacement method using the coordinates of human sorbitol dehydrogenase, PDB ID 1PL8. Each monomer contains a bidomain architecture composed of a large catalytic domain of residues Ala5 through Val167, and residues Arg308 through Leu362, and a smaller cofactor-binding domain with residues Ala168 through Tyr307, with a large cleft separating the two domains
docking study with the substrate L-arabinitol, Zn2+ and NAD+ reveals a catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, and a cofactor NAD+ binding domain involving residues Gly202, ILeu204, Gly205, Cys273, Arg229 and Val298, with strong hydrogen bonding contacts with the substrate and cofactor
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
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4 h, more than 60% residual activity
50
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half-life 45 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable during storage for at least 2 years
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22C, stable for more than 1 month
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4C, stable during storage for months
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4C, stable for several months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant protein
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recombinant protein, expression in Escherichia coli
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recombinant proteins purified using Ni-agarose
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
derivatives of the expression vector pQE32 containing wild-type and mutated versions of ladA transformed to Escherichia coli M13 cells
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expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D213S/I214R
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significantly higher preference for NADP+ over NAD+
M70F
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almost complete loss of activity; results in a nearly complete enzyme inactivation
Y318F
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increased activity for L-arabinitol and xylitol, increased affinity for D-sorbitol; results in a significant increase in affinity for D-sorbitol, xylitol and L-arabitol
D211S
strong decrease in activity
D211S/I212R
strong decrease in activity, increase in activity with cofactor NADP+
D211S/I212R/D213N
strong decrease in activity, increase in activity with cofactor NADP+
D211S/I212R/S348T
strong decrease in activity, increase in activity with cofactor NADP+
D212S/I213R
D224S/I225R
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significantly altered cofactor specificity from NAD+ to NADP+
additional information
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gene disruption mutant, almost unable to grow on L-arabinose, extremely weak growth on L-arabinitol, D-talitol, galactitol
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate