Indoleacetaldehyde Reductase of Cucumis sativus L: KINETIC PROPERTIES AND ROLE IN AUXIN BIOSYNTHESIS.

@article{Brown1980IndoleacetaldehydeRO,
  title={Indoleacetaldehyde Reductase of Cucumis sativus L: KINETIC PROPERTIES AND ROLE IN AUXIN BIOSYNTHESIS.},
  author={Hugh M. Brown and William K. Purves},
  journal={Plant physiology},
  year={1980},
  volume={65 1},
  pages={
          107-13
        }
}
Indoleacetaldehyde reductase catalyzes the conversion of indoleacetaldehyde to indole ethanol in extracts of Cucumis sativus L., with reduced pyridine nucleotide required as co-substrate. NADH and NADPH result in markedly different enzyme behavior, as reflected in reaction kinetics and in responses to inhibitors and activators. It is not yet clear whether there are two separate enzymes, one specific for NADH and the other for NADPH, or whether there is a single enzyme differentially influenced… 
INDOLE-3-ACETALDEHYDE REDUCTASE IN PHYCOMYCES BLAKESLEEANUS. CHARACTERIZATION OF THE ENZYME
TLDR
Changes in lAAJd reductase activity correlate with certain developmental stages of the fungus, and the formation of indole-3-ethanol (lEt) is dependent on the presence of NAD(P)H.
Proposed Enzymes of Auxin Biosynthesis and Their Regulation III. Some Properties of Pea Indolylacetaldehyde Oxidase
TLDR
The pea enzyme seems not to be a dismutase since indolylmethanol or indolylethanol were not formed as products and Pyridine nucleotide coenzymes did not activate the partially purified enzyme.
Identification of indole-3-acetaldehyde and indole-3-acetaldehyde reductase in Chinese cabbage.
TLDR
The enzyme reaction was inhibited at high NADPH concentrations (>200 μM) and modulated by IAA and indole-3-ethanol (IEt).
Indole-3-Ethanol Oxidase in Phycomyces blakesleeanus Bgff: Characterization of the Enzyme.
Indole-3-ethanol oxidase (IEt oxidase) from Phycomyces blakesleeanus Bgff.(P.b.) is a 56 kD polypeptide as determined by gel filtration. The reaction products are indole-3-acetaldehyde (IAAld) and,
Compartmentation of indole-3-acetic acid in Pisum sativum L.
Studies were initiated on the compartmentation of indole-3-acetic acid (IAA) in Pisum sativum cv. Meteor. Particular attention has been given to the biosynthesis and catabolism of IAA in isolated pea
Indole-3-acetic acid biosynthetic pathways in the basidiomycetous yeast Rhodosporidiumpaludigenum
TLDR
Investigation of IAA biosynthesis pathways in a basidiomycetous yeast concluded that R. paludigenum DMKU-RP301 produces IAA through an indole-3-pyruvic acid pathway.
Enzymes of auxin biosynthesis and their regulation I. Tryptophan and phenylalanine aminotransferase in pea plants
TLDR
Transamination of L-trp and L-phe was demonstrated by enzyme extracts from pea, maize and tomato, but was not detected in kohlrabi, and Indolylacetylaspartate and tryptophol were shown to be competitive inhibitors.
Indole‐3‐ethanol oxidase in Phycomyces blakesleeanus. Is indole‐3‐ethanol a “storage pool” for IAA?
TLDR
The observed variations in IEt content were strongly correlated with certain developmental stages of the fungus, and the decrease of IEt between 60 and 84 h of fungal development coincides with a high IEt oxidase activity.
Purification of NADPH‐specific indole‐3‐acetaldehyde reductase from Cucumis sativus by two‐dimensional native polyacrylamide gel electrophoresis
TLDR
NADPH-specific indole-3-acetaldehyde (IAAId) reductase from cucumber was purified by several purification steps to one spot on a two-dimensional polyacrylamide gel and was shown to be a cytoplasmic enzyme by differential centrifugation and subsequent marker enzyme analysis.
...
1
2
3
...

References

SHOWING 1-10 OF 12 REFERENCES
Indole-3-ethanol Oxidase: Kinetics, Inhibition, and Regulation by Auxins.
TLDR
The results may be interpreted as showing that IAA is a noncompetitive inhibitor which binds to that conformation of the enzyme which also binds indoleethanol, and the significance of these interactions for the regulation of IAA biosynthesis is discussed.
Cucumber seedling indoleacetaldehyde oxidase.
TLDR
2,4-Dichlorophenoxyacetic acid strongly inhibited the indoleacetaldehyde oxidase activity, and it is proposed that this enzyme may be subject in vivo to feedback inhibition by indole-3-acetic Acid.
Isolation of Indole-3-ethanol Oxidase from Cucumber Seedlings.
TLDR
An enzyme is isolating from cucumber seedlings which catalyzes the oxidation of IEt to indole-3-acetaldehyde (IAAld), which has nearly maximum activity from pH 8 to 11 and appears to be reduced to H(2)O(2).
Auxin biogenesis: subcellular compartmentation of indoleacetaldehyde reductases in cucumber seedlings.
TLDR
Results indicate a division of the terminal steps of auxin biogenesis into at least two subcellular compartments, and two of the enzymes in the auxin biosynthetic pathway were localized.
Occurrence of Indoleacetaldehyde and Tryptophol in the Extracts of Etiolated Shoots of Pisum and Helianthus Seedlings
Presence of a non-acidic, growth-promoting indole compound, identical in Rf and colour reaction and closely similar in UV spectrum to synthetic indoleacetaldehyde (IAAId) has been demonstrated in
Indoleacetaldehyde in cucumber seedlings.
The presence of indoleacetaldehyde in cucumber (Cucumis sativus L.) cotyledons was demonstrated by thin layer chromatographic R(F) values in three solvent systems, by the formation and hydrolysis of
Isolation and identification of indole-3-ethanol (tryptophol) from cucumber seedlings.
TLDR
Crude ether extracts of green shoots of Cucumis sativus L. promoted the elongation of cucumber hypocotyl segments and identified the growth promoter as indole-3-ethanol by mass spectrometry, thin layer and gas chromatography, and ultraviolet and visible spectroscopy.
The interpretation of non-hyperbolic rate curves for two-substrate enzymes. A possible mechanism for phosphofructokinase.
TLDR
It has now been shown that the phenomena of substrate inhibition and activation may occur simultaneously in the following ways.
...
1
2
...