87-51-4 Usage
Description
Indole-3-acetic acid, also known as IAA, is an organic compound and a naturally occurring auxin, a type of plant hormone. It plays a crucial role in the regulation of plant growth and development by promoting cell elongation and division. IAA is found in various plant species and is involved in various physiological processes, including root initiation, fruit development, and leaf abscission.
Used in Plant Growth Regulation:
Indole-3-acetic acid is used as a plant growth hormone for promoting plant growth and development. It acts as an inducer of plant cell elongation and division, leading to increased plant size and improved crop yields.
Used in Agriculture:
Indole-3-acetic acid is used as a plant growth regulator in agriculture to enhance crop productivity. It helps in promoting root growth, improving fruit set, and increasing overall plant vigor. By optimizing the application of IAA, farmers can achieve better crop yields and improved plant health.
Used in Plant Tissue Culture:
Indole-3-acetic acid is used as a growth factor in plant tissue culture, a technique used for plant propagation and genetic manipulation. It is added to the culture medium to stimulate cell division and elongation, enabling the growth and development of plantlets from explants or callus tissue.
Used in Plant Bioassays:
Indole-3-acetic acid is used in plant bioassays to study the effects of various factors on plant growth and development. It serves as a standard for comparing the activity of other plant growth regulators and helps researchers understand the mechanisms of action of different plant hormones.
Used in Pharmaceutical Industry:
Indole-3-acetic acid has potential applications in the pharmaceutical industry as a precursor for the synthesis of various drugs and pharmaceutical compounds. Its unique chemical properties and biological activity make it a valuable starting material for the development of new therapeutic agents.
Biosynthesis
3-Indolylacetic acid is biosynthesised in plants from tryptophan by two pathways, the indolylpyruvic acid pathway being quantitatively the more important. Experiments with tomato shoots have shown the existence of a tryptophan transaminase, which catalyses the formation of indolylpyruvic acid, and a tryptophan decarboxylase, which catalyses the formation of tryptamine. The decarboxylation of indolylpyruvic acid is catalysed by indolylpyruvate decarboxylase, while indolylacetaldehyde dehydrogenase catalyses the oxidation of indolylacetaldehyde to indolylacetic acid.
The biosynthesis of 3-indolylacetic acid
Biological Functions
3-Indolylacetic acid (indole-3-acetic acid, IAA) is one of the auxins, which together with the gibberellins and abscisic acid, cyto- kinins and ethylene are hormones regulating the growth and development of plants. IAA is a ubiquitous constituent of higher plants and the most important auxin. Some other, non-indolic compounds, including phenyl- acetic acid biosynthesised in plants from phenylalanine, have similar properties and synthetic auxins have also been prepared.
In the plant, IAA conjugates with many compounds, including glucose and other sugars, and with aspartic and glutamic acids. This is probably a way of storing the hormone for future use.
IAA initiates many growth effects in plants, including geotropism and phototropism, development of the ovary, division of cells, enlargement in callus tissue, root formation and apical dominance. When fed to plants, the hormone causes growth up to a maximum, which depends on the type of tissue being fed, and thereafter inhibits further growth, probably through the formation of ethylene, which is growth-inhibitory. Stern tissues tolerate the highest levels of IAA and root tissues the lowest. In the plant, the most active sites of IAA synthesis are the young, expanding leaves.
Purification Methods
Recrystallise heteroauxin from EtOH/water [James & Ware J Phys Chem 89 5450 1985]. [Beilstein 22 III/IV 65.] Alternatively recrystallise 30g of the acid with 10g of charcoal in 1L of hot water, filter and cool when 22g of colourless acid separate. Dry it and store it in a dark bottle away from direct sunlight [Johnson & Jacoby Org Synth Coll Vol V 654 1973]. The picrate has m 178-180o. [Beilstein 22 H 66, 22 I 508, 22 II 50, 22 III/IV 1088.] It is a plant growth substance.
Check Digit Verification of cas no
The CAS Registry Mumber 87-51-4 includes 5 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 2 digits, 8 and 7 respectively; the second part has 2 digits, 5 and 1 respectively.
Calculate Digit Verification of CAS Registry Number 87-51:
(4*8)+(3*7)+(2*5)+(1*1)=64
64 % 10 = 4
So 87-51-4 is a valid CAS Registry Number.
InChI:InChI=1/C10H9NO2/c12-10(13)5-7-6-11-9-4-2-1-3-8(7)9/h1-4,6,11H,5H2,(H,12,13)/p-1
87-51-4Relevant articles and documents
A study of the kinetics and mechanism of oxidation of L-tryptophan by diperiodatonickelate(IV) in aqueous alkaline medium
Chimatadar,Basavaraj,Nandibewoor
, p. 1046 - 1053 (2007)
The kinetics of oxidation of L-tryptophan by diperiodatonickelate(IV) (DPN) in an aqueous alkaline medium at a constant ionic strength of 0.30 mol dm -3 was studied spectrophotometrically. The reaction was first order in diperiodatonickelate(IV) and less than first order in tryptophan and the OH- ion. The addition of periodate had no effect on the reaction, and nickel(II) produced did not influence the reaction rate significantly. An increase in ionic strength and decrease in medium permittivity did not affect the reaction rate. A mechanism involving the formation of a complex between L-tryptophan and reactive DPN species was proposed. The constants characterizing the mechanism were evaluated. The activation parameters for the slow reaction step were computed and discussed.
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Sielo et al.
, p. 397,400 (1969)
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HETEROCYCLIC COMPOUND, APPLICATION THEREOF, AND COMPOSITION CONTAINING SAME
-
, (2022/03/07)
A heterocyclic compound represented by formula XI, a pharmaceutically acceptable salt, a solvate, or a solvate of a pharmaceutically acceptable salt thereof, use thereof, and a composition containing the same. The compound is novel in structure and has good STAT5 inhibitory activity.
Oxidation of Primary Alcohols and Aldehydes to Carboxylic Acids via Hydrogen Atom Transfer
Tan, Wen-Yun,Lu, Yi,Zhao, Jing-Feng,Chen, Wen,Zhang, Hongbin
supporting information, p. 6648 - 6653 (2021/09/08)
The oxidation of primary alcohols and aldehydes to the corresponding carboxylic acids is a fundamental reaction in organic synthesis. In this paper, we report a new chemoselective process for the oxidation of primary alcohols and aldehydes. This metal-free reaction features a new oxidant, an easy to handle procedure, high isolated yields, and good to excellent functional group tolerance even in the presence of vulnerable secondary alcohols and tert-butanesulfinamides.
The plant pathogen enzyme AldC is a long-chain aliphatic aldehyde dehydrogenase
Lee, Soon Goo,Harline, Kate,Abar, Orchid,Akadri, Sakirat O.,Bastian, Alexander G.,Chen, Hui-Yuan S.,Duan, Michael,Focht, Caroline M.,Groziak, Amanda R.,Kao, Jesse,Kottapalli, Jagdeesh S.,Leong, Matthew C.,Lin, Joy J.,Liu, Regina,Luo, Joanna E.,Meyer, Christine M.,Mo, Albert F.,Pahng, Seong Ho,Penna, Vinay,Raciti, Chris D.,Srinath, Abhinav,Sudhakar, Shwetha,Tang, Joseph D.,Cox, Brian R.,Holland, Cynthia K.,Cascella, Barrie,Cruz, Wilhelm,McClerkin, Sheri A.,Kunkel, Barbara N.,Jez, Joseph M.
, p. 13914 - 13926 (2020/12/09)
Aldehyde dehydrogenases are versatile enzymes that serve a range of biochemical functions. Although traditionally considered metabolic housekeeping enzymes because of their ability to detoxify reactive aldehydes, like those generated from lipid peroxidation damage, the contributions of these enzymes to other biological processes are widespread. For example, the plant pathogen Pseudomonas syringae strain PtoDC3000 uses an indole-3-acetaldehyde dehydrogenase to synthesize the phytohormone indole-3-acetic acid to elude host responses. Here we investigate the biochemical function of AldC from PtoDC3000. Analysis of the substrate profile of AldC suggests that this enzyme functions as a long-chain aliphatic aldehyde dehydrogenase. The 2.5 ? resolution X-ray crystal of the AldC C291A mutant in a dead-end complex with octanal and NAD1 reveals an apolar binding site primed for aliphatic aldehyde substrate recognition. Functional characterization of site-directed mutants targeting the substrate- and NAD(H)-binding sites identifies key residues in the active site for ligand interactions, including those in the “aromatic box” that define the aldehyde-binding site. Overall, this study provides molecular insight for understanding the evolution of the prokaryotic aldehyde dehydrogenase superfamily and their diversity of function.