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Information on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase and Organism(s) Neurospora crassa and UniProt Accession Q7SI09

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Neurospora crassa
UNIPROT: Q7SI09 not found.
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Word Map
The taxonomic range for the selected organisms is: Neurospora crassa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
l-arabitol dehydrogenase, l-arabinitol 4-dehydrogenase, hjlad, l-arabinitol dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dehydrogenase, L-arabinitol
-
-
-
-
L-arabitol dehydrogenase
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-
-
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pentitol-DPN dehydrogenase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
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-
-
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reduction
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-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9028-19-7
-
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 + H+
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
-
-
?
xylitol + NAD+
D-xylulose + NADH + H+
show the reaction diagram
-
-
-
?
adonitol + NAD+
? + NADH
show the reaction diagram
-
-
-
-
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
show the reaction diagram
-
-
-
-
?
Xylitol + NAD+
?
show the reaction diagram
-
-
-
-
?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
electron density corresponding to the bound NAD+ cofactor is observed within the smaller nucleotide-binding domain, along a crevice between the two domains. The adenine ring is nestled in a shallow pocket created by numerous hydrophobic residues, including Ile212, Val232, Thr260, and Val262. The nicotinamide is adjacent to the catalytic zinc ion, where it is poised for hydride transfer to the C2 atom of the substrate
NAD+
-
strong preference for NAD+
NADP+
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very low yet detectable activity with NADP+, strong preference for NAD+
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
a structural zinc ion is situated at a loop region located adjacent to the catalytic domain, where it is ligated by enzyme residues Cys108, Cys111, Cys114, and Cys122. The catalytically requisite zinc ion constitutes the second metal found in each monomer of LAD. This metal is coordinated by residues Cys53, His78, and Glu79, with a water molecule completing a near-tetrahedral coordination sphere
Zn2+
-
two ions per subunit
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.14 - 5
NAD+
0.48 - 8
NADP+
35
adonitol
-
pH 8.0, 25°C
18
L-arabinitol
-
pH 8.0, 25°C
174
NAD+
-
pH 8.0, 25°C
290
xylitol
-
pH 8.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.18 - 10.83
NAD+
8.23 - 20.16
NADP+
18
adonitol
-
pH 8.0, 25°C
20.2
L-arabinitol
-
pH 8.0, 25°C
20.1
NAD+
-
pH 8.0, 25°C
15
xylitol
-
pH 8.0, 25°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.88 - 79
NAD+
8.27 - 36.6
NADP+
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
152000
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gel filtration
39000
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4 * 39000, SDS-PAGE, 4 * 39600, calculated
39600
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4 * 39000, SDS-PAGE, 4 * 39600, calculated
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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4 * 39000, SDS-PAGE, 4 * 39600, calculated
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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+
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
4 h, more than 60% residual activity
50
-
half-life 45 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
22°C, stable for more than 1 month
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4°C, stable for several months
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant protein
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
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enzymatic cycling assay for nicotinic acid adenine dinucleotide phosphate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sullivan, R.; Zhao, H.
Cloning, characterization, and mutational analysis of a highly active and stable L-arabinitol 4-dehydrogenase from Neurospora crassa
Appl. Microbiol. Biotechnol.
77
845-852
2007
Neurospora crassa
Manually annotated by BRENDA team
Bae, B.; Sullivan, R.P.; Zhao, H.; Nair, S.K.
Structure and engineering of L-arabinitol 4-dehydrogenase from Neurospora crassa
J. Mol. Biol.
402
230-240
2010
Neurospora crassa (Q7SI09), Neurospora crassa
Manually annotated by BRENDA team