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SYSTEMATIC NAME
IUBMB Comments
n-alkanal:NADP+ 2-oxidoreductase
Shows highest activity with 1-nitrocyclohexene but also has significant activity with 2-methylpentenal and trans-cinnamaldehyde [3]. Involved in the detoxication of alpha,beta-unsaturated aldehydes and ketones. Has very low activity with NAD as reductant (cf. EC 1.3.1.74, 2-alkenal reductase [NAD(P)+]).
the amino acid sequences of the deduced allyl-ADHs are different in four amino acid residues, allyl-ADH2 has the following mutations compared to ADH1: T17A, V30A, L345P,R278H
tyrosine at position 56 of PaDBR2 is highly conserved among oxidoreductases, and is proposed to be involved in binding with NADPH. In isozyme PaDBR1, this position is occupied by a cysteine residue; tyrosine at position 56 of PaDBR2 is highly conserved among oxidoreductases, and is proposed to be involved in binding with NADPH. In isozyme PaDBR1, this position is occupied by a Cystein residue
suppression of chloroplastic alkenal/one oxidoreductase represses the carbon catabolic pathway in Arabidopsis leaves during night. Phosphoenolpyruvate carboxylase activity decreases and starch degradation during the night is suppressed in aor (RNAi). In contrast, the phenotype of aor (RNAi) is rescued when aor (RNAi) plants are grown under constant light conditions. The smaller plant sizes observed in aor mutants grown under day/night cycle conditions are attributable to the decrease in carbon utilization during the night. The acrolein reducing activity decreases to about 60% and 75%in aor-1 and aor-4 mutant lines, respectively, compared with the wild-type. Lack of AtAOR in chloroplasts induces oxidative stress. Phenotype analysis, detailed overview
lipid-derived reactive carbonyl species (RCS) possess electrophilic moieties and cause oxidative stress by reacting with cellular components. Arabidopsis thaliana has a chloroplast-localized alkenal/one oxidoreductase (AtAOR) for the detoxification of lipid-derived RCS, especially alpha,beta-unsaturated carbonyls. The detoxification of lipid-derived RCS by AtAOR in chloroplasts contributes to the protection of dark respiration and supports plant growth during the night
the aluminium-induced increase in root expression level of gene encoding 2-alkenal reductase (NADP+-dependent) might contribute to plant Al-tolerance by the detoxification of reactive carbonyls
recombinant NtRed-1 does not catalyze dehydrogenation of (2S,4S)-carveol, indicating that the recombinant NtRed-1 lacks the catalytic function as allyl-alcohol dehydrogenase, although the recombinant NtRed-1 is designed from the nucleotide sequence of allyl-ADH
results indicate that the enzyme catalyzes specifically the dehydrogenation of the secondary alcohols adjacent to the C-C double bond, no oxidation of saturated alcohols
the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
docking of the ligand and substrate into the active cavity, overview. The catalytic efficiency of isozyme PaDBR1 is substantially less than that of PaDBR2, especially towards cinnamyl aldehydes carrying a methoxy group (coniferyl, 5-hydroxyconiferyl and sinapyl aldehydes). No activity with sinapyl aldehyde, cinnamyl aldehyde, 4-coumaric acid, caffeic acid, 4-coumaryl alcohol, caffeyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
docking of the ligand and substrate into the active cavity, overview. The catalytic efficiency of isozyme PaDBR1 is substantially less than that of PaDBR2, especially towards cinnamyl aldehydes carrying a methoxy group (coniferyl, 5-hydroxyconiferyl and sinapyl aldehydes). No activity with sinapyl aldehyde, cinnamyl aldehyde, 4-coumaric acid, caffeic acid, 4-coumaryl alcohol, caffeyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
docking of the ligand and substrate into the active cavity, overview. The catalytic efficiency of isozyme PaDBR1 is substantially less than that of PaDBR2, especially towards cinnamyl aldehydes carrying a methoxy group (coniferyl, 5-hydroxyconiferyl and sinapyl aldehydes). No activity with sinapyl aldehyde, cinnamyl aldehyde, 4-coumaric acid, caffeic acid, 4-coumaryl alcohol, caffeyl alcohol, coniferyl alcohol, 5-hydroxyconiferyl alcohol, and sinapyl alcohol
the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
the recombinant isozyme PaDBR2 has a higher catalytic activity than isozyme PaDBR1 with respect to the reduction of the double bond present in hydroxycinnamyl aldehydes
the Km-values for the (S)-alcohols are one order of magnitude lower than those for the (R)-alcohols, indicating that the enzyme has a higher affinity for the S-configuration than for the R-configuration
pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate 5-hydroxyconiferyl aldeyde; pH and temperature not specified in the publication, purified recombinant isozyme PaDBR1 mutant C56V, substrate coniferyl aldeyde
each monomer is composed of two domains, a substrate binding or catalytic domain (residues 1-135 and 304-343) and a nucleotide-binding domain (residues 136-303)
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
determination of the X-ray crystal structures of holo-, binary (NADP(H)-bound), and ternary (NADP+ and 4-hydroxy-3-methoxycinnamaldehyde-bound) NtDBR complexes
recombinant His-tagged isozyme PaDBR1 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration; recombinant His-tagged isozyme PaDBR2 from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged isozyme PaDBR1 in Escherichia coli strain BL21(DE3); DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of N-terminally His-tagged isozyme PaDBR2 in Escherichia coli strain BL21(DE3)
gene cloned into pET21b (Novagen), without a stop codon, to incorporate a C-terminal His6-tag and transformed Escherichia coli strain BL21(DE3)pLysS (Stratagene)
site-directed mutagenesis, the mutation turns the substrate selectivity and catalytic efficiency of isozyme PaDBR1 indistinguishable from those of isozyme PaDBR2, Docking arrangement of PaDBR1C56Y with NADP+/p-coumaryl aldehyde, overview. Increased activity compared to wild-type enzyme
generation of AtAOR (aor) mutants, including a transfer DNA knockout, aor (T-DNA), and RNA interference knockdown, aor (RNAi), lines. Both aor mutants show smaller plant sizes than wild-type plants when they are grown under day/night cycle conditions
generation of AtAOR (aor) mutants, including a transfer DNA knockout, aor (T-DNA), and RNA interference knockdown, aor (RNAi), lines. Both aor mutants show smaller plant sizes than wild-type plants when they are grown under day/night cycle conditions