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
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Engineering
Engineering on EC 1.1.1.12 - L-arabinitol 4-dehydrogenase
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M70F
Y318F
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+
H91A
additional information
results in a significant increase in affinity for D-sorbitol, xylitol and L-arabitol
Y318F
increased activity for L-arabinitol and xylitol, increased affinity for D-sorbitol
D212S/I213R
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no activity with NAD+, slight activity with NADP+
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construction of deletion mutants of ladA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
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construction of deletion mutants of ladA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
additional information
construction of deletion mutants of ladA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant ladA2-1 displays the reduced xylitol productivity
additional information
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construction of deletion mutants of ladA and ladA-xdhA, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Genomic DNA from Aspergillus oryzae strain KBN616 is used as the template for amplification of the three xdhA and ladA inserts. Activities of xylitol dehydrogenase and xylose reductase in the mutant strains, phenotype, overview
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additional information
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construction of deletion mutants of ladA by homologous transformation, to generate mutants with decreased dehydrogenase activities and increased xylitol production. Gene pyrG is used as a selectable marker. Consumption of D-xylose for xdhA2-1 and ladA2-1 is similar to that of KBN616. Mutant ladA2-1 displays the reduced xylitol productivity
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additional information
gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
additional information
JQ079782
gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
additional information
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gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
additional information
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gene disruption of the L-arabitol dehydrogenase encoding gene resulting in increased xylanase production. Complementation with constitutively expressed ladA confirms that the xylanase overproducing phenotype is mainly caused by loss of ladA function, while a knockout of xlnR in the UV mutant demonstrates that improved xylanase production is mediated by XlnR
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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
additional information
all tested wild-type and mutant enzymes have a similar secondary structure and the global folding of mutant and wild-type HjLAD is similar
additional information
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all tested wild-type and mutant enzymes have a similar secondary structure and the global folding of mutant and wild-type HjLAD is similar
additional information
preparation of a metal-protein hybrid nanoflower system for efficient immobilization of the recombinant enzyme L-arabinitol 4-dehydrogenase from Hypocrea jecorina (HjLAD). Synthesis of enzyme-Cu(PO4)2 x 3H2O hybrid nanoflowers and encapsulation of His-tagged enzyme, FESEM images, overview. Compared with the free enzyme, the synthesized hybrid nanoflower exhibit enhanced enzymatic activity of 246% for HjLAD. The immobilized enzyme retains high catalytic activity and shows improved he tolerance towards pH and temperature changes. Synthesized nanoflowers also retain high storage stability and reusability. In addition, the immobilized enzyme exhibits significantly enhanced L-xylulose production under cofactor regeneration conditions compared to the free enzyme combination
additional information
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all tested wild-type and mutant enzymes have a similar secondary structure and the global folding of mutant and wild-type HjLAD is similar
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additional information
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overexpression of native pentose-specific transporters together with the rate-limiting D-xylitol and L-arabitol dehydrogenases, the dormant pentose metabolism of Yarrowia lipolytica is activated, overview. Recombinant overexpression of a heterologous L-arabitol dehydrogenase of Aspergillus oryzae (ADHAoz), in Yarrowia lipolytica strain YlSR157 using the constitutive TEF promoter, ADHAoz is chosen because it exhibits higher activity toward L-arabitol (39.2 mU/mg protein) than D-xylitol (6.54 mU/mg protein). Unlike strain YlSR102, strain YlSR157 grows faster and consumes more sugars when growing on both single arabinose and mixed pentose sugars
additional information
Yarrowia lipolytica ATCC MYA-2613
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overexpression of native pentose-specific transporters together with the rate-limiting D-xylitol and L-arabitol dehydrogenases, the dormant pentose metabolism of Yarrowia lipolytica is activated, overview. Recombinant overexpression of a heterologous L-arabitol dehydrogenase of Aspergillus oryzae (ADHAoz), in Yarrowia lipolytica strain YlSR157 using the constitutive TEF promoter, ADHAoz is chosen because it exhibits higher activity toward L-arabitol (39.2 mU/mg protein) than D-xylitol (6.54 mU/mg protein). Unlike strain YlSR102, strain YlSR157 grows faster and consumes more sugars when growing on both single arabinose and mixed pentose sugars
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