1.1.1.12: L-arabinitol 4-dehydrogenase
This is an abbreviated version!
For detailed information about L-arabinitol 4-dehydrogenase, go to the full flat file.
Reaction
Synonyms
ADH, dehydrogenase, L-arabinitol, HjLAD, L-arabinitol dehydrogenase, L-arabitol dehydrogenase, LAD, Lad1, LADA, More, NAD(P)+-dependent arabitol dehydrogenase, pentitol-DPN dehydrogenase, XYL2
ECTree
Advanced search results
General Information
General Information on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
evolution
malfunction
metabolism
physiological function
additional information
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
evolution
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
evolution
-
the enzyme belongs to a medium-chain dehydrogenase/reductase (MDR) superfamily and a subfamily of polyol dehydrogenase, PDH
-
evolution
-
the enzyme belongs to the medium-chain dehydrogenase/reductase (MDR) superfamily and polyol dehydrogenase (PDH) subfamily. The enzyme contains the typical NAD+-binding motif GxGxxG of MDR family enzymes
-
H6WCP4, JQ079782
disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production. The xylanase overproducing phenotype is mainly caused by loss of ladA function, while improved xylanase production is mediated by XlnR
malfunction
H6WCP4, JQ079782
disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production. The xylanase overproducing phenotype is mainly caused by loss of ladA function, while improved xylanase production is mediated by XlnR. The ladA locus is the direct cause of the increased xylanase activity of 3M-43, a pyrA mutant of 3M-43
malfunction
-
disruption of the L-arabitol dehydrogenase encoding gene in Aspergillus tubingensis results in increased xylanase production. The xylanase overproducing phenotype is mainly caused by loss of ladA function, while improved xylanase production is mediated by XlnR
-
H6WCP4, JQ079782
the enzyme is involved in the L-arabinose catabolic pathway
metabolism
-
Yarrowia lipolytica strain ATCC MYA-2613 has endogenous enzymes for D-xylose assimilation, but inefficient xylitol dehydrogenase causes Yarrowia lipolytica to assimilate xylose poorly. L-Arabitol dehydrogenase is the rate-limiting step responsible for poor arabinose utilization in Yarrowia lipolytica. Functional roles of native sugar-specific transporters for activating the dormant pentose metabolism in Yarrowia lipolytica, cryptic pentose metabolism and native L-arabinose assimilation pathway, overview. TRP6Yli and TRP22Yli are xylose-specific transporters in Yarrowia lipolytica. L-Arabinose is first reduced into L-arabitol by NAD(P)H-dependent arabinose reductase (ARD), which is then converted into L-xylulose by NAD(P)+-dependent arabitol dehydrogenase (ADH). L-Xylulose is then converted to D-xylitol by NAD(P)H-dependent xylulose reductase (XLR), which is further assimilated to D-xylulose-5-phosphate, a precursor for the pentose-phosphate pathway (PPP)
metabolism
Yarrowia lipolytica ATCC MYA-2613
-
Yarrowia lipolytica strain ATCC MYA-2613 has endogenous enzymes for D-xylose assimilation, but inefficient xylitol dehydrogenase causes Yarrowia lipolytica to assimilate xylose poorly. L-Arabitol dehydrogenase is the rate-limiting step responsible for poor arabinose utilization in Yarrowia lipolytica. Functional roles of native sugar-specific transporters for activating the dormant pentose metabolism in Yarrowia lipolytica, cryptic pentose metabolism and native L-arabinose assimilation pathway, overview. TRP6Yli and TRP22Yli are xylose-specific transporters in Yarrowia lipolytica. L-Arabinose is first reduced into L-arabitol by NAD(P)H-dependent arabinose reductase (ARD), which is then converted into L-xylulose by NAD(P)+-dependent arabitol dehydrogenase (ADH). L-Xylulose is then converted to D-xylitol by NAD(P)H-dependent xylulose reductase (XLR), which is further assimilated to D-xylulose-5-phosphate, a precursor for the pentose-phosphate pathway (PPP)
-
metabolism
-
the enzyme is involved in the L-arabinose catabolic pathway
-
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
physiological function
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
physiological function
-
the organism catabolizes L-arabinose as well as D-glucose and D-xylose. The highest production amounts of ethanol from D-glucose, xylitol from D-xylose, and L-arabitol from L-arabinose were 0.45 g/g D-glucose, 0.60 g/g D-xylose, and 0.61 g/g L-arabinose with 21.7 g/l ethanol, 20.2 g/l xylitol, and 30.3 g/l L-arabitol, respectively. The enzyme has L-arabitol dehydrogenase (LAD) activity and also exhibits broad specificity to polyols, such as xylitol, D-sorbitol, ribitol, and L-arabitol. Xylitol is the preferred substrate
-
homology modeling and docking of L-arabinitol in the substrate-binding pocket of HjLAD suggesting routes of hydride transfer, where the key amino acid residues comprise the core region, molecular dynamics, overview
additional information
-
homology modeling and docking of L-arabinitol in the substrate-binding pocket of HjLAD suggesting routes of hydride transfer, where the key amino acid residues comprise the core region, molecular dynamics, overview
additional information
three-dimensional structure homology modelling, overview
additional information
-
three-dimensional structure homology modelling, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
-
xylitol production of wild-type and mutant strains, overview
additional information
xylitol production of wild-type and mutant strains, overview
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
xylitol production of wild-type and mutant strains, overview
-
additional information
-
three-dimensional structure homology modelling, overview
-
additional information
-
homology modeling and docking of L-arabinitol in the substrate-binding pocket of HjLAD suggesting routes of hydride transfer, where the key amino acid residues comprise the core region, molecular dynamics, overview
-