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Names | |
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Preferred IUPAC name Butane-1,4-diamine | |
Other names 1,4-Diaminobutane, 1,4-Butanediamine | |
Identifiers | |
3D model (JSmol) | |
3DMet | |
605282 | |
ChEBI | |
ChEMBL | |
ChemSpider | |
DrugBank | |
ECHA InfoCard | 100.003.440 |
EC Number |
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1715 | |
KEGG | |
MeSH | Putrescine |
PubChem CID | |
RTECS number |
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UNII | |
UN number | 2928 |
CompTox Dashboard (EPA) | |
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Properties | |
C4H12N2 | |
Molar mass | 88.154 g·mol−1 |
Appearance | Colourless crystals |
Odor | fishy-ammoniacal, pungent |
Density | 0.877 g/mL |
Melting point | 27.5 °C (81.5 °F; 300.6 K) |
Boiling point | 158.6 °C; 317.4 °F; 431.7 K |
Miscible | |
log P | −0.466 |
Vapor pressure | 2.33 mm Hg at 25 deg C (est) |
Henry's law constant (kH) | 3.54x10−10 atm-cu m/mol at 25 deg C (est) |
Refractive index (nD) | 1.457 |
Hazards | |
GHS labelling: | |
Danger | |
H228, H302, H312, H314, H331 | |
P210, P261, P280, P305+P351+P338, P310 | |
Flash point | 51 °C (124 °F; 324 K) |
Explosive limits | 0.98–9.08% |
Lethal dose or concentration (LD, LC): | |
LD50 (median dose) |
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Related compounds | |
Related alkanamines | |
Related compounds | |
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa). |
Putrescine is an organic compound with the formula (CH2)4(NH2)2. It is a colorless solid that melts near room temperature. It is classified as a diamine. [3] Together with cadaverine, it is largely responsible for the foul odor of putrefying flesh, but also contributes to other unpleasant odors.
Putrescine is produced on an industrial scale by the hydrogenation of succinonitrile. [3]
Biotechnological production of putrescine from a renewable feedstock has been investigated. A metabolically engineered strain of Escherichia coli that produces putrescine at high concentrations in glucose mineral salts medium has been described. [4]
Spermidine synthase uses putrescine and S-adenosylmethioninamine (decarboxylated S-adenosyl methionine) to produce spermidine. Spermidine in turn is combined with another S-adenosylmethioninamine and gets converted to spermine.
Putrescine is synthesized in small quantities by healthy living cells by the action of ornithine decarboxylase.
Putrescine is synthesized biologically via two different pathways, both starting from arginine.
Putrescine is found in all organisms. [6] Putrescine is widely found in plant tissues, [6] often being the most common polyamine present within the organism. It's role in development is well documented, but recent studies have suggested that putrescine also plays a role in stress responses in plants, both to biotic and abiotic stressors. [7] The absence of putrescine in plants is associated with an increase in both parasite and fungal population in plants.
Putrescine serves an important role in a multitude of ways, which include: a cation substitute, an osmolyte, or a transport protein. [6] It also serves as an important regulator in a variety of surface proteins, both on the cell surface and on organelles, such as the mitochondria and chloroplasts. A recorded increase of ATP production has been found in mitochondria and ATP synthesis by chloroplasts with an increase in mitochondrial and chloroplastic putrescine, but putrescine has also been shown to function as a developmental inhibitor in some plants, which can be seen as dwarfism and late flowering in Arabiadopsis plants. [6]
Putrescine production in plants can also be promoted by fungi in the soil. [8] Piriformospora indica (P. indica) is one such fungus, found to promote putrescine production in Arabidopsis and common garden tomato plants. In a 2022 study it was shown that the presence of this fungus had a promotional effect on the growth of the root structure of plants. After gas chromatography testing, putrescine was found in higher amounts in these root structures. [9]
Plants that had been inoculated with P. indica had presented an excess of arginine decarboxylase. [9] This is used in the process of making putrescine in plant cells. One of the downstream effects of putrescine in root cells is the production of auxin. That same study found that putrescine added as a fertilizer showed the same results as if it was inoculated with the fungus, which was also shown in Arabidopsis and barley. The evolutionary foundations of this connection and putrescine are still unclear.
Putrescine is a component of bad breath and bacterial vaginosis. [10] It is also found in semen and some microalgae, together with spermine and spermidine.
Putrescine reacts with adipic acid to yield the polyamide nylon 46, which is marketed by DSM under the trade name Stanyl. [11]
Application of putrescine, along with other polyamines, can be used to extend the shelf life of fruits by delaying the ripening process. [12] Pre-harvest application of putrescine has been shown to increase plant resistance to high temperatures and drought. [13] Both of these effects seem to result from lowered ethylene production following exogenous putrescine exposure. [14]
Due to its role in putrification, putrescine has also been proposed as a biochemical marker for determining how long a corpse has been decomposing. [15]
Putrescine and cadaverine were first described in 1885 by the Berlin physician Ludwig Brieger (1849–1919). [16] [17] [18]
In rats, putrescine has a low acute oral toxicity of 2000 mg/kg body weight, with no-observed-adverse-effect level of 2000 ppm (180 mg/kg body weight/day). [19]
Cadaverine is an organic compound with the formula (CH2)5(NH2)2. Classified as diamine, it is a colorless liquid with an unpleasant odor. It is present in small quantities in living organisms but is often associated with the putrefaction of animal tissue.
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the l-arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid.
Ornithine is a non-proteinogenic amino acid that plays a role in the urea cycle. Ornithine is abnormally accumulated in the body in ornithine transcarbamylase deficiency. The radical is ornithyl.
The enzyme ornithine decarboxylase catalyzes the decarboxylation of ornithine to form putrescine. This reaction is the committed step in polyamine synthesis. In humans, this protein has 461 amino acids and forms a homodimer.
Agmatine, also known as 4-aminobutyl-guanidine, was discovered in 1910 by Albrecht Kossel. It is a chemical substance which is naturally created from the amino acid arginine. Agmatine has been shown to exert modulatory action at multiple molecular targets, notably: neurotransmitter systems, ion channels, nitric oxide (NO) synthesis and polyamine metabolism and this provides bases for further research into potential applications.
Eflornithine, sold under the brand name Vaniqa among others, is a medication used to treat African trypanosomiasis and excessive hair growth on the face in women. Specifically it is used for the 2nd stage of sleeping sickness caused by T. b. gambiense and may be used with nifurtimox. It is taken intravenously or topically. It has also been given orally on at least some rare occasions for the treatment of African trypanosomiasis.
Spermine is a polyamine involved in cellular metabolism that is found in all eukaryotic cells. The precursor for synthesis of spermine is the amino acid ornithine. It is an essential growth factor in some bacteria as well. It is found as a polycation at physiological pH. Spermine is associated with nucleic acids and is thought to stabilize helical structure, particularly in viruses. It functions as an intracellular free radical scavenger to protect DNA from free radical attack. Spermine is the chemical primarily responsible for the characteristic odor of semen.
Spermidine is a polyamine compound found in ribosomes and living tissues and having various metabolic functions within organisms. It was originally isolated from semen.
Spermidine synthase is an enzyme that catalyzes the transfer of the propylamine group from S-adenosylmethioninamine to putrescine in the biosynthesis of spermidine. The systematic name is S-adenosyl 3-(methylthio)propylamine:putrescine 3-aminopropyltransferase and it belongs to the group of aminopropyl transferases. It does not need any cofactors. Most spermidine synthases exist in solution as dimers.
SpeF is a putative cis-acting element identified in several gram negative alpha proteobacteria. It is proposed to be involved in regulating expression of genes involved in polyamide biosynthesis.
The enzyme adenosylmethionine decarboxylase catalyzes the conversion of S-adenosyl methionine to S-adenosylmethioninamine. Polyamines such as spermidine and spermine are essential for cellular growth under most conditions, being implicated in many cellular processes including DNA, RNA and protein synthesis. S-adenosylmethionine decarboxylase (AdoMetDC) plays an essential regulatory role in the polyamine biosynthetic pathway by generating the n-propylamine residue required for the synthesis of spermidine and spermine from putrescein. Unlike many amino acid decarboxylases AdoMetDC uses a covalently bound pyruvate residue as a cofactor rather than the more common pyridoxal 5'-phosphate. These proteins can be divided into two main groups which show little sequence similarity either to each other, or to other pyruvoyl-dependent amino acid decarboxylases: class I enzymes found in bacteria and archaea, and class II enzymes found in eukaryotes. In both groups the active enzyme is generated by the post-translational autocatalytic cleavage of a precursor protein. This cleavage generates the pyruvate precursor from an internal serine residue and results in the formation of two non-identical subunits termed alpha and beta which form the active enzyme.
The enzyme Acid-Induced Arginine Decarboxylase (AdiA), also commonly referred to as arginine decarboxylase, catalyzes the conversion of L-arginine into agmatine and carbon dioxide. The process consumes a proton in the decarboxylation and employs a pyridoxal-5'-phosphate (PLP) cofactor, similar to other enzymes involved in amino acid metabolism, such as ornithine decarboxylase and glutamine decarboxylase. It is found in bacteria and virus, though most research has so far focused on forms of the enzyme in bacteria. During the AdiA catalyzed decarboxylation of arginine, the necessary proton is consumed from the cell cytoplasm which helps to prevent the over-accumulation of protons inside the cell and serves to increase the intracellular pH. Arginine decarboxylase is part of an enzymatic system in Escherichia coli, Salmonella Typhimurium, and methane-producing bacteria Methanococcus jannaschii that makes these organisms acid resistant and allows them to survive under highly acidic medium.
Antizyme inhibitor 2 (AzI2) also erroneously known as arginine decarboxylase (ADC) is a protein that in humans is encoded by the AZIN2 gene. In contrast to initial suggestions, Antizyme inhibitor 2 does not act as arginine decarboxylase (ADC) in mammalian cells
A ureohydrolase is a type of hydrolase enzyme. The ureohydrolase superfamily includes arginase, agmatinase, formiminoglutamase and proclavaminate amidinohydrolase. These enzymes share a 3-layer alpha-beta-alpha structure, and play important roles in arginine/agmatine metabolism, the urea cycle, histidine degradation, and other pathways.
The biosynthesis of cocaine has long attracted the attention of biochemists and organic chemists. This interest is partly motivated by the strong physiological effects of cocaine, but a further incentive was the unusual bicyclic structure of the molecule. The biosynthesis can be viewed as occurring in two phases, one phase leading to the N-methylpyrrolinium ring, which is preserved in the final product. The second phase incorporates a C4 unit with formation of the bicyclic tropane core.
A polyamine is an organic compound having more than two amino groups. Alkyl polyamines occur naturally, but some are synthetic. Alkylpolyamines are colorless, hygroscopic, and water soluble. Near neutral pH, they exist as the ammonium derivatives. Most aromatic polyamines are crystalline solids at room temperature.
Polyamines (PAs) are small, positively charged, organic molecules that are ubiquitous in all living organisms. These are considered as one of the oldest group of substances known in biochemistry. There are three common types of polyamines, putrescine, spermidine, hermospermine according to structure, universal distribution in all cellular compartments, and presumed involvement in physiological activities. Polyamine is found in all cellular compartments and physiological activities due to their simple structures. The function of polyamine is very diverse in that it performs a key macromolecule to cellular membrane. Because of their essential roles in plant, mutation of polyamines can cause critical damage on plants. Furthermore, some polyamines like putrescine inhibit biosynthetic activities in plants. The activity of polyamines can be categorized to some parts due to its signalling and growing activity.
The ldcC RNA motif is a conserved RNA structure that was discovered by bioinformatics. ldcC motif RNAs are found in Bacillota and two species of Spirochaetota.
Beverly Marie Guirard was a microbiologist who worked on the biochemistry of microbial growth, especially with respect to vitamin B6. She is also known for her work defining the components of coenzyme A which was a part of the research that led to a Nobel Prize for Fritz Albert Lipmann.
BpsA is a single-module non-ribosomal peptide synthase (NRPS) located in the cytoplasm responsible for the process of creating branched-chain polyamines, and producing spermidine and spermine. It has a singular ligand in its structure involved with Fe3+ and PLIP interactions. As seen by its EC number, it is a transferase (2) that transfers an alkyl or aryl group other than methyl groups (5) (2.5.1). BpsA was first discovered in the archaea Methanococcus jannaschii and thermophile Thermococcus kodakarensis and since then has been used in a variety of applications such as being used as a reporter, researching phosphopantetheinyl transferase (PPTase), and for NRPS domain recombination experiments it can be used as a model. Both (hyper)thermophilic bacteria and euryarchaeotal archaea seem to conserve BpsA and orthologs as branches chains polyamines are crucial for survival. There is also a second type of BpsA also known as Blue-pigment indigoidine synthetase that produces the pigment indigoidine and is found in organisms like Erwinia chrysanthemi. However, not much seems to be known about this variant except that it is a synthase, and it does not yet appear to be classified under an EC number.