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Information on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase
for references in articles please use BRENDA:EC1.1.1.12
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.12 L-arabinitol 4-dehydrogenase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
showSynonyms
l-arabitol dehydrogenase, l-arabinitol 4-dehydrogenase, hjlad, l-arabinitol dehydrogenase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ADH
dehydrogenase, L-arabinitol
-
-
-
-
HjLAD
L-arabinitol dehydrogenase
L-arabitol dehydrogenase
LAD
Lad1
LADA
NAD(P)+-dependent arabitol dehydrogenase
pentitol-DPN dehydrogenase
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-
-
-
XYL2
L-arabitol dehydrogenase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-arabinitol + NAD+ = L-xylulose + NADH + H+
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
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redox reaction
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-
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-
reduction
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-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
L-arabinose degradation II
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SYSTEMATIC NAME
IUBMB Comments
L-arabinitol:NAD+ 4-oxidoreductase (L-xylulose-forming)
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CAS REGISTRY NUMBER
COMMENTARY
9028-19-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-arabino-3-hexulose + NADH
D-talitol + NAD+
-
Substrates: -
Products: -
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D-sorbitol + NAD+
? + NADH + H+
Substrates: wild-type shows no activity on D-sorbitol, whereas mutant Y318F does
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?
L-arabinitol + NADP+
L-xylulose + NADPH + H+
Substrates: no activity with cofactor NADP+ for wild-type
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?
L-talitol + NAD+
D-arabino-3-hexulose + NADH
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Substrates: -
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ribitol + NAD+
?
Substrates: 93% of the activity with L-arabinitol
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?
ribitol + NAD+
D-ribulose + NADH + H+
Substrates: -
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r
xylitol + NADP+
D-xylulose + NADPH + H+
Substrates: very low activity with NADP+
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D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
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?
D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
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D-sorbitol + NAD+
D-fructose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
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L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
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Substrates: enzyme of the L-arabinose catabolic pathway
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L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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L-arabinitol + NAD+
L-xylulose + NADH + H+
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Substrates: -
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L-arabinitol + NAD+
L-xylulose + NADH + H+
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Substrates: L-arabitol consumption rate by resting cells is of the same order of magnitude as the LAD activity determined for crude cell extracts. The strong accumulation of L-arabitol (intracellular concentration of up to 0.4 M) during aerobic L-arabinose metabolism indicates the existence of a bottleneck at the level of LAD
Products: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
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Substrates: L-arabitol consumption rate by resting cells is of the same order of magnitude as the LAD activity determined for crude cell extracts. The strong accumulation of L-arabitol (intracellular concentration of up to 0.4 M) during aerobic L-arabinose metabolism indicates the existence of a bottleneck at the level of LAD
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
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Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
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L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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r
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
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L-arabinitol + NAD+
L-xylulose + NADH + H+
[Candida] arabinofermentans PYCC 5603
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Substrates: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
[Candida] arabinofermentans PYCC 5603T
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Substrates: -
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?
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: -
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?
L-arabitol + NAD+
L-xylulose + NADH + H+
Substrates: about 20% activity compared to xylitol
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L-arabitol + NAD+
L-xylulose + NADH + H+
Yarrowia lipolytica ATCC MYA-2613
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Substrates: -
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Xylitol + NAD+
?
Substrates: 17% of the activity with L-arabinitol
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?
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
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r
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: preferred substrates, reaction of EC 1.1.1.9
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xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
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?
additional information
?
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Substrates: Y318 of LadA contributes significantly to the substrate specificity difference between LAD and xylitol dehydrogenase/D-sorbitol dehydrogenase
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?
additional information
?
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Substrates: Y318 of LadA contributes significantly to the substrate specificity difference between LAD and xylitol dehydrogenase/D-sorbitol dehydrogenase
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?
additional information
?
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Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
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additional information
?
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Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
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?
additional information
?
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Substrates: the enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, and ribitol. Xylitol is the preferred substrate (EC 1.1.1.9)
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additional information
?
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Substrates: the enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, and ribitol. Xylitol is the preferred substrate (EC 1.1.1.9)
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additional information
?
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Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
Products: -
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?
additional information
?
-
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Substrates: the enzyme exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol (cf. EC 1.1.1.56), and L-arabitol. Xylitol is the preferred substrate, but native and recombinant enzyme McXDH exhibits relative activities toward L-arabinitol of approximately 20% that toward xylitol
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?
additional information
?
-
-
Substrates: no substrate: D-mannitol, D-arabinitol, D-sorbitol
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?
additional information
?
-
Substrates: no substrate: D-arabinitol. The promiscuity of LAD towards different substrates is restricted to five-carbon sugars, and no activity is observed towards either D-sorbitol or D-mannitol
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?
additional information
?
-
-
Substrates: no substrate: D-arabinitol. The promiscuity of LAD towards different substrates is restricted to five-carbon sugars, and no activity is observed towards either D-sorbitol or D-mannitol
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?
additional information
?
-
-
Substrates: enzyme contributes to 30% of total xylitol dehydrogenase activity, enzyme can partially compensate for loss of xylitol dehydrogenase function
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
xylitol + NAD+
D-xylulose + NADH + H+
Substrates: -
Products: -
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r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
Products: -
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r
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: enzyme of the L-arabinose catabolic pathway
Products: -
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r
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
Products: -
?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
Products: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
-
Substrates: -
Products: -
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r
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
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?
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
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r
L-arabinitol + NAD+
L-xylulose + NADH + H+
Substrates: -
Products: -
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?
L-arabitol + NAD+
L-xylulose + NADH + H+
Yarrowia lipolytica ATCC MYA-2613
-
Substrates: -
Products: -
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r
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
cofactor NAD+ binding domain involving residues Gly202, ILeu204, Gly205, Cys273, Arg229 and Val298, molecular docking studies
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
NADP+
-
very low yet detectable activity with NADP+, strong preference for NAD+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
additional information
Zn2+
required, the zinc ADH signature and conserved coenzyme binding motif are observed in the amino acid sequence of McXDH at positions 65-76 and 183-188 and are completely conserved among McXDH and XDHs from other yeasts and filamentous fungi
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+
structure analysis indicates that enzyme belongs to the family of Zn2+-containing, medium-chain alcohol dehydrogenases. Residues involved in Zn2+ binding are C55, H80, and E165. Thereis a second zinc-binding site C110, C113, C116, and C124
Zn2+
catalytic Zn2+ binding domain involving residues Cys66, His91, Glu92 and Glu176, molecular docking studies
Zn2+
the Cys66, His91, Glu92, and Glu176 residues are involved in coordination of catalytic Zn2+ along with a water molecule
additional information
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
additional information
-
after incubation with ZnSO4, ZnCl2, FeCl2, and CuCl2, 40, 37, 30, and 25%, respectively, of the activity of the metal-free enzyme is restored. Poorer effects by Fe3+, Cd2+, and Ca2+, while Ni2+, Mn2+, Co2+, Mg2+, K+, and Na+ do not exert restorative effects
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
21.3
L-arabinitol
pH 8.0, 25°C, immobilzed recombinant enzyme in nanoflowers
31.1