Information on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase

Word Map on EC 1.1.1.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.12
-
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
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Pentose and glucuronate interconversions
-
-
Metabolic pathways
-
-
L-arabinose degradation II
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)
-
CAS REGISTRY NUMBER
COMMENTARY hide
9028-19-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
and uracil auxotroph derivative strain P4
SwissProt
Manually annotated by BRENDA team
a DELTApyrG strain developed from strain KBN616
SwissProt
Manually annotated by BRENDA team
ladA from strain 1M-7
UniProt
Manually annotated by BRENDA team
strain PYCC 5603, analysis of L-arabinose catabolic pathway
-
-
Manually annotated by BRENDA team
pentose-fermenting strain isolated from an alcohol fermentation starter in Thailand
UniProt
Manually annotated by BRENDA team
pentose-fermenting strain isolated from an alcohol fermentation starter in Thailand
UniProt
Manually annotated by BRENDA team
strain ATCC 28089 /DSM 1075 /Wisconsin 54-1255
UniProt
Manually annotated by BRENDA team
i.e Trichoderma reesei
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
-
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
additional information
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
-
-
-
-
?
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
-
-
-
-
r
D-arabino-3-hexulose + NADH
D-talitol + NAD+
show the reaction diagram
-
-
-
-
r
D-fructose + NADH + H+
D-sorbitol + NAD+
show the reaction diagram
-
-
-
-
r
D-psicose + NADH
D-allitol + NAD+
show the reaction diagram
-
-
-
-
?
D-sorbitol + NAD+
? + NADH + H+
show the reaction diagram
wild-type shows no activity on D-sorbitol, whereas mutant Y318F does
-
-
?
D-sorbitol + NAD+
D-fructose + NADH + H+
show the reaction diagram
D-sorbose + NADH
D-gulitol + NAD+
show the reaction diagram
-
-
-
-
?
galactitol + NAD+
L-xylo-3-hexulose + NADH
show the reaction diagram
-
-
-
-
r
L-arabinitol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
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
-
-
?
L-arabitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
L-iditol + NAD+
L-sorbose + NADH
show the reaction diagram
-
-
-
-
r
L-mannitol + NAD+
L-fructose + NADH
show the reaction diagram
-
-
-
-
r
L-sorbitol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
L-tagatose + NADH
L-talitol + NAD+
show the reaction diagram
-
-
-
-
?
L-talitol + NAD+
D-arabino-3-hexulose + NADH
show the reaction diagram
-
-
-
-
r
L-xylo-3-hexulose + NADH
galactitol + NAD+
show the reaction diagram
-
-
-
-
r
ribitol + NAD+
?
show the reaction diagram
93% of the activity with L-arabinitol
-
-
?
Xylitol + NAD+
?
show the reaction diagram
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
additional information
?
-
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+
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
-
pH 8.6, 25C
580
D-arabino-3-hexulose
-
pH 8.6, 25C
96
D-fructose
-
pH 8.6, 25C
81
D-psicose
-
pH 8.6, 25C
0.868 - 483.5
D-sorbitol
115
D-sorbose
-
pH 8.6, 25C
25
D-talitol
-
pH 8.6, 25C
60
galactitol
-
pH 8.6, 25C
0.056 - 57
L-arabinitol
0.056 - 0.078
L-arabitol
191
L-Iditol
-
pH 8.6, 25C
37
L-mannitol
-
pH 8.6, 25C
19
L-sorbitol
-
pH 8.6, 25C
28
L-tagatose
-
pH 8.6, 25C
81
L-xylo-3-hexulose
-
pH 8.6, 25C
5
L-xylulose
-
30C, pH 9.6
0.05 - 174
NAD+
0.008
NADH
-
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
-
pH 8.0, 25C
3.7 - 833
D-sorbitol
0.108 - 70
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
pH 9, 30C
0.32 - 4.83
L-arabinitol
0.88 - 79
NAD+
8.27 - 36.6
NADP+
0.14
xylitol
pH 9, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.9
purified native enzyme, pH 7.0, 40C, substrates L-arabinitol and NAD+
8.7
-
pH 7.0, 22C
11.7
-
pH 7.0, 22C
24
-
purified recombinant His-tagged enzyme, pH 7.0, 25C
44
-
purified recombinant His-tagged enzyme, pH 8.0, 25C
105
-
purified recombinant His-tagged enzyme, pH 9.5, 25C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.6
H6WCP4, JQ079782
assay at; assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 11
activity range, inactive above or below
6 - 10
-
activity range of both free and immobilized enzymes
7 - 9.5
-
pH-profile, overview
8 - 10.5
-
more than 60% of maximal activity within
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
H6WCP4, JQ079782
assay at; assay at
65
-
both free and immobilized enzyme HjLAD
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 55
activity range, inactive at 60C
25 - 70
-
activity range of both free and immobilized enzymes
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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
-
4 * 39000, SDS-PAGE, 4 * 39600, calculated
39600
-
4 * 39000, SDS-PAGE, 4 * 39600, calculated
41000
x * 41000, calculated, x * 45000, SDS-PAGE
45000
x * 41000, calculated, x * 45000, SDS-PAGE
152000
-
gel filtration
195000
native enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homopentamer
tetramer
-
4 * 39000, SDS-PAGE, 4 * 39600, calculated
additional information
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
-
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
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
half-life of free enzyme is 190 min, of immobilized enzyme 31.5 h
30
-
half-life of free enzyme is 165 min, of immobilized enzyme 24.5 h
40
-
half-life of free enzyme is 26 min, of immobilized enzyme 4.25 h
45
-
4 h, more than 60% residual activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, stable during storage for at least 2 years
-
22C, stable for more than 1 month
-
4C, stable during storage for months
-
4C, stable for several months
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
native enzyme by ammonium sulfate fractionation, anion exchange chromatography, hydrophobic interation chromatography, and another different step of anion exchange chromatography, followed by gel filtration. Recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity and anion exchange chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3)
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3)
-
recombinant protein
-
recombinant protein, expression in Escherichia coli
-
recombinant proteins purified using Ni-agarose
-
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
-
expression in Escherichia coli
gene lad1, overexpression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3)
-
gene lad1, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene ladA, DNA and amino acid sequence determination and analysis; gene ladA, DNA and amino acid sequence determination and analysis, construction of strain 3M-43/pyrA, a pyrA mutant of strain 3M-43, in which an intact copy of ladA is inserted under control of the Aspergillus nidulans gpdA promoter. Complementation of the 3M-43 pyrA strain with pGpd:ladA
H6WCP4, JQ079782
gene xyl2, DNA and amino acid sequence determination and analysis, cloning in Escherichia coli strain JM109, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3)
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D213S/I214R
-
significantly higher preference for NADP+ over NAD+
M70F
-
almost complete loss of activity; results in a nearly complete enzyme inactivation
Y318F
-
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
-
significantly altered cofactor specificity from NAD+ to NADP+
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate
synthesis
additional information