110-60-1 Usage
Overview
Putrescine is a low-molecular-weight nitrogenous base with the systematic name 1,4-diaminobutane. It is an aliphatic diamine belonging to the group of biogenic amines (Bas). Two basic amino groups are present, which at the physiological pH of 7.4 carry a positive charge that makes them suitable for a wide range of functions in different cell types. According to some authors, putrescine also belongs, together with cadaverine, spermine, and spermidine, to polyamines (molecules containing two?or more amino groups in the molecule)[1,2]. Polyamines are found in all cell types and their presence in various kinds of foodstuffs is partly due to their endogenous origin. In humans, there are 3 common sources of putrescine: the first one is endogenous biosynthesis within their own cells, the second one includes foodstuffs (alimentary intake), and the last one is the production of putrescine by bacteria of the intestinal microflora. The largest amount of putrescine in humans is taken from food[2]. If none of the 3 sources of putrescine becomes excessive, putrescine is used for its physiological functions and the excess is excreted by normal metabolism. However, increased intake of putrescine in food can lead to serious toxicological consequences.
Figure 1 The chemical structure of putrescine
Biosynthesis
l ,4-Diaminobutane (putrescine), spermidine, spermine, and closely related derivatives are found in a wide variety of animals, bacteria, yeasts, and plants. It is generally accepted that polyamine biosynthesis is intimately interrelated with the synthesis of nucleic acids and proteins[3]. Polyamines are ubiquitous in biological materials, although the relative amounts of 1,4-diaminobutane, spermidine, and spermine differ markedly in different cells[4, 5]. In general, prokaryotes have a higher concentration of 1,4-diaminobutane than spermidine and lack spermine. Eukaryotes usually have little 1,4-diaminobutane, and have spermine as well as spermidine.
The pathway for the biosynthesis of 1,4-diaminobutane and spermidine was first established in microorganisms and was later found to be very similar in animal cells. In bacteria, 1,4-diaminobutane may be formed either by ornithine decarboxylase or by arginine decarboxylase via agmatine[6-8]. Both biosynthetic enzymes are normally present in Escherichia coli, although ornithine decarboxylation is usually the major pathway[8]. Both decarboxylases have been purified from E. coli and have been shown to require pyridoxal phosphate[9-11]. These enzymes are subject to feedback inhibition and repression by 1,4-diaminobutane or spermidine[12, 13]. In animal tissues amines are derived by decarboxylation of ornithine, rather than by decarboxylation of arginine[14, 15]. Purification of ornithine decarboxylase has been hindered by the very low enzyme activity normally present. However, as discussed in the section on the role of polyamines in growth, ornithine decarboxylase levels increase dramatically after a variety of stimuli, and the enzyme has been purified to apparent homogeneity from regenerating liver[17] and from the livers of rats treated with thioacetamide[18]. Pyridoxal phosphate appears to be a required cofactor[16, 19].
Physiological function
Putrescine fulfills important physiological functions in a wide variety of living cells. This BA shows many physiological functions and it is a precursor in the synthesis of other polyamines (spermine and spermidine). Putrescine is classified as a physiologic amine. Physiological functions of putrescine and other polyamines are related to their polycationic nature, which determines interactions with negatively charged molecules such as DNA, RNA, proteins, phospholipids[20]. Newer studies show that putrescine, along with other polyamines and phosphate ions, forms nuclear aggregates of polyamines in the cell nuclei, which are responsible for the abovementioned interactions and affect the 3-dimensional structure of DNA[21]. These interactions are related to the regulation of the structure of nucleic acids and protein synthesis[22, 23].
Putrescine, along with other polyamines, binds to membrane structures such as phospholipids, mainly in erythrocytes. This polyamine may lead to a decrease in membrane fluidity but also to increased resistance to fragmentation due to stabilization of the membrane skeleton[24, 25]. It has also been found that apart from the membrane stabilization and the effect on the synthesis of nucleic acids and proteins, polyamines are involved in the removal of free radicals[26]. In many mammals, they play an important role as luminal growth factors for intestinal maturation and growth[27, 28] and can play a significant role in the prevention of food allergies[29]. In mammals, polyamines have direct effects on several ion channels and receptors, resulting in the regulation of Ca2+, Na+, and K+ homeostasis[30, 31].
Applications
Putrescine is used as a precursor in many biological systems and synthon for amido-ureas. It is involved in the synthesis of nylon 46 by reacting with adipic acid[32].
Toxicity
With respect to important physiological functions, it is clear that disruption of the normal balance due to increased intake of putrescine from food can have serious toxicological consequences. Although the toxic effects of putrescine are significantly lower than that of histamine or tyramine, there are many serious secondary effects. Diamines such as putrescine have a very important role in alimentary poisoning as they can enhance and potentiate the toxic effect of histamine, tyramine, and phenylethylamine by interacting with enzymes that metabolize these BAs[33]. For example, experiments on guinea pigs and rats revealed that putrescine potentiates histamine toxicity up to 10 times[34, 35]. Putrescine enhances histamine toxicity by inhibiting enzymes oxidizing histamine diaminooxidase(DAO; EC 1.4.3.6)?and histamine N-methyltransferase (NMT; EC 2.1.1.8)[36-38]. Moreover, from a toxicological point of view, a serious aspect of putrescine occurrence in foodstuffs is the possibility of forming carcinogenic nitrosamines. Putrescine can form carcinogenic nitrosamines by the reaction with nitrites[39, 40].
The effect of putrescine on food quality
In addition to the toxic effects, the occurrence of putrescine in foodstuffs leads to undesirable organoleptic properties and adversely affects the taste and aroma of food[41], for example, in shrimps, it is perceptible at concentrations of 3 mg/kg[42]. Increased occurrence of putrescine indicates food spoilage caused by microbial activity and it is also the main BA that indicates spoiled meat. The amount of putrescine, histamine, and cadaverine shows the freshness of meat and is defined as biogenic amines index (BAI)[43].
Reference
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Bard′ocz S, Duguid TJ, Brown DS, Grant G, Pusztai A, White A, Ralph A. 1995. The importance of dietary polyamines in cell regeneration and growth. Br J Nutr 73[6]:819–28.
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Tabor, H., Tabor, C. W. 1964. Pharmacal. Rev. 1 6:245-300
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Morris, D. R., Koffron, K. L. 1969. J. Bio. Chem. 244:6094-99
Applebaum, D. 1972. Purification and characterization of induced and biosynthetic ornithine decarboxylases of Escherichia coli. PhD thesis. Univ. Washington. Seattle. 157 pp. Univ. Microfilms #73-1 3789
Wu, W. H., Morris, D. R. 1973. J. Bio. Chem. 248: 1687-95, 1696-99
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Morris, D. R., Wu, W. H., Applebaum, D., Kofi'ron, K. L. 1970. See Ref. 8, pp. 968-76
Russell, D. H., cd. 1973. Polyamines in Normal and Neoplastic Growth, New York: Raven. 429 pp.
Herbst, E. J., Bachrach, U.,cds. 1970. Ann. NY Acad. Sci. 171:693-1009
Pegg. A. E . . Williams-Ashman. H. G. 1968. Biochem. J 108: 533-39
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Raina, A., Jiinne, J. 1968. Acta Chem. Scand. 22 :2375-77
Igarashi K, Kashiwagi K. 2010. Modulation of cellular function by polyamines. Intl J Biochem Cell Biol 42[1]:39–51.
Di Luccia A, Picariello G, Iacomino G, Formisano A, Paduano L, D’Agostino L. 2009. The in vitro nuclear aggregates of polyamines. FEBS J 276[8]:2324–35.
Silla Santos MH. 1996. Biogenic amines: their importance in foods. Intl J Food Microbiol 29[2–3]:213–31.
Hou MH, Lin SB, Yuann JM, Lin WC, Wang AH, Kan Ls L. 2001. Effects of polyamines on the thermal stability and formation kinetics of DNA duplexes with abnormal structure. Nucleic Acids Res 29[24]:5121–8.
Til HP, Falke HE, Prinsen MK, Willems MI. 1997. Acute and subacute toxicity of tyramine, spermidine, spermine, putrescine and cadaverine in rats. Food Chem Toxicol 35[3–4]:337–48.
Largue E, Sabater-Molina M, Zamora S. 2007. Biological significance of dietary polyamines. Nutrition 23[1]:87–95.
Kaur-Sawhney R, Tiburcio AF, Altabella T, Galston AW. 2003. Polyamines in plants: an overview. J Cell Mol Biol 2:1–12.
Dufour C, Dandrifosse G, Forget P, Vermesse F, Romain N, Lepoint P. 1988. Spermine and spermidine induce intestinal maturation in the rat. Gastroenterology 95[1]:112–6.
L¨oser C. 2000. Polyamines in human and animal milk. Br J Nutr 84[Suppl1]:S55–8 Dandrifosse G, Peulen O, El Khefif N, Deloyer P, Dandrifosse AC, Grandfils C. 2000. Are milk polyamines preventive agents against food allergy? Proc Nutr Soc 59[1]:81–6.
Dandrifosse G, Peulen O, El Khefif N, Deloyer P, Dandrifosse AC, Grandfils C. 2000. Are milk polyamines preventive agents against food allergy? Proc Nutr Soc 59[1]:81–6.
Johnson TD. 1996. Modulation of channel function by polyamines. Trends Pharmacol Sci 17[1]:22–7.
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https://www.alfa.com/zh-cn/catalog/B21316/
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Lehane L, Olley J. 2000. Histamine fish poisoning revisited. Intl J Food Microbiol 58[1–2]:1–37.
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Hern′andez-Jover T, Izquierdo-Pulido M, Veciana-Nogues MT, Marine-Font A, Vidal-Carou MC. 1997. Biogenic amine and polyamine contents in meat and meat products. J Agric Food Chem 45[6]:2098–102.
Emborg J, Dalgaard P. 2006. Formation of histamine and biogenic amines in cold-smoked tuna: an investigation of psychrotolerant bacteria from samples implicated in cases of histamine fish poisoning. J Food Prot 69[4]:897–906.
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Lehane L, Olley J. 2000. Histamine fish poisoning revisited. Intl J Food Microbiol 58[1–2]:1–37.
Benner Jr RA, Staruszkiewicz WF, Rogers PL, Otwelle WS. 2003. Evaluation of putrescine, cadaverine, and indole as chemical indicators of decomposition in penaeid shrimp. J Food Sci 68[7]:2178–85.
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Chemical Properties
colourless liquid
Uses
Different sources of media describe the Uses of 110-60-1 differently. You can refer to the following data:
1. A GABA precursor in many biological systems.
2. 1,4-Diaminobutane is used as a precursor in many biological systems and synthon for amido-ureas. It is involved in the synthesis of nylon 46 by reacting with adipic acid.
3. GABA precursor in many biological systems and synthon for amido-ureas.
Definition
ChEBI: A four-carbon alkane-alpha,omega-diamine. It is obtained by the breakdown of amino acids and is responsible for the foul odour of putrefying flesh.
Safety Profile
Poison by
subcutaneous, intravenous, and rectal
routes. Moderately toxic by ingestion. An
experimental teratogen. Human mutation
data reported. When heated to
decomposition it emits toxic fumes of NOx.
See also 1,3-BUTANEDIAMINE and
AMINES.
Check Digit Verification of cas no
The CAS Registry Mumber 110-60-1 includes 6 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 3 digits, 1,1 and 0 respectively; the second part has 2 digits, 6 and 0 respectively.
Calculate Digit Verification of CAS Registry Number 110-60:
(5*1)+(4*1)+(3*0)+(2*6)+(1*0)=21
21 % 10 = 1
So 110-60-1 is a valid CAS Registry Number.
InChI:InChI=1/C4H12N2/c5-3-1-2-4-6/h1-6H2
110-60-1Relevant articles and documents
Occurrence of agmatine pathway for putrescine synthesis in Selenomonas ruminatium
Liao, Shaofu,Poonpairoj, Phuntip,Ko, Kyong-Cheol,Takatuska, Yumiko,Yamaguchi, Yoshihiro,Abe, Naoki,Kaneko, Jun,Kamio, Yoshiyuki
, p. 445 - 455 (2008)
Selenomonas ruminantium synthesizes cadaverine and putrescine from L-lysine and L-ornithine as the essential constituents of its peptidoglycan by a constitutive lysine/ornithine decarboxylase (LDC/ODC). S. ruminantium grew normally in the presence of the specific inhibitor for LDC/ODC, DL-α-difluoromethylornithine, when arginine was supplied in the medium. In this study, we discovered the presence of arginine decarboxylase (ADC), the key enzyme in agmatine pathway for putrescine synthesis, in S. ruminantium. We purified and characterized ADC and cloned its gene (adc) from S. ruminantium chromosomal DNA. ADC showed more than 60% identity with those of LDC/ODC/ADCs from Gram-positive bacteria, but no similarity to that from Gram-negative bacteria. In this study, we also cloned the aguA and aguB genes, encoding agmatine deiminase (AguA) and N-carbamoyl-putrescine amidohydrolase (AguB), both of which are involved in conversion from agmatine into putrescine. AguA and AguB were expressed in S. ruminantium. Hence, we concluded that S. ruminantium has both ornithine and agmatine pathways for the synthesis of putrescine.
Turtschamide, a cytotoxic putrescine bisamide from Corydalis turtschaninovii
Kim, Ki Hyun,Choi, Sang Un,Lee, Kang Ro
, p. 1490 - 1492 (2012)
A putrescine bisamide with a unique cyclic structure derived from l-tyrosine, turtschamide (1), was isolated from the tubers of Corydalis turtschaninovii. The structure of 1 was established by extensive spectroscopic study, and its absolute configuration was determined by a combination of NOE experiment and application of the Marfey's method. Turtschamide (1) exhibited cytotoxicity against the A549, SK-OV-3, SK-MEL-2, and HCT-15 cells.
Nickel and nickel-magnesia catalysts active in the hydrogenation of 1,4-butanedinitrile
Serra, Marc,Salagre, Pilar,Cesteros, Yolanda,Medina, Francisco,Sueiras, Jesus E.
, p. 210 - 219 (2001)
Several NiO-MgO systems were synthesized to be studied as nickel catalysts for the hydrogenation of 1,4-butanedinitrile in the gas phase and compared with a bulk NiO of controlled morphology. All samples were characterized by XRD, BET, TPR, TPD, SEM, and H2 chemisorption techniques. The Ni-MgO systems had higher activities than the Ni bulk catalyst. The most active catalyst at all reaction temperatures was type R4CB which had homogeneous particles of about 1000 A, the highest metal surface area, and the highest coverage with weakly bound hydrogen. The presence of basic magnesia suppresses the condensation reactions and consequently favors the elimination of amines, and prevents catalyst deactivation. The selectivity toward the different products not only depends on the catalytic properties but can also be modified by controlling the hydrogen/dinitrile ratio. The highest selectivity to 4-aminobutanenitrile was achieved by catalyst R4CB, with 85% at 100% conversion and working at a space velocity of 13,000 h-1 and 343 K. This selectivity could be increased by lowering the hydrogen/butanedinitrile ratio.
CHENGES IN POLYAMINES AND RELATED ENZYMES WITH LOSS OF VIABILITY IN RICE SEEDS.
Mukhopadhyay, A.,Choudhuri, M. M.,Sen, K.,Ghosh, B.
, p. 1547 - 1552 (1983)
Putrescine, spermidine and spermine of high vigour, low vigour and non viable (classes 1, 2 and 3 respectively) seeds of Oryza sativa increased with loss of viability.The largest concentration of spermine was found in non-viable embryos.Spermine was absent in the husks of all the three categories of seeds.Arginine decarboxylase was greatest in high vigoured seeds and its activity gradually declined with loss of viability.However, diamine oxidase and polyamine oxidase activities gradually increased with the loss of viability of the seeds while DNA, RNA and protein contents decreased.The total content of polyamines increased on kinetin treatment but declined on ABA treatment.DNA, RNA and protein followed the same trend as polyamines.The polyamine contents increased by ca 3- and 4-fold, respectively, in high vigoured and low vigoured seeds on 1E-4 M kinetin treatment.The activity of ADC followed the same change as that of the polyamines in both cases, but the reverse was observed for the activities of diamine and polyamine oxidases.Key Word Index - Oryza sativa; Gramineae; rice; spermine; spermidine; putrescine; arginine; arginine decarboxylase; polyamine oxidase.
-
Schultz
, p. 2666 (1948)
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STUDIES ON POLYAMINES. II. METABOLISM OF SPERMIDINE AND SPERMINE BY
UNEMOTO
, p. 1255 - 1264 (1963)
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Imprinted Apportionment of Functional Groups in Multivariate Metal-Organic Frameworks
Feng, Liang,Wang, Kun-Yu,Lv, Xiu-Liang,Powell, Joshua A.,Yan, Tian-Hao,Willman, Jeremy,Zhou, Hong-Cai
supporting information, p. 14524 - 14529 (2019/10/02)
Sophisticated chemical processes widely observed in biological cells require precise apportionment regulation of building units, which inspires researchers to develop tailorable architectures with controllable heterogeneity for replication, recognition and information storage. However, it remains a substantial challenge to endow multivariate materials with internal sequences and controllable apportionments. Herein, we introduce a novel strategy to manipulate the apportionment of functional groups in multivariate metal-organic frameworks (MTV-MOFs) by preincorporating interlocked linkers into framework materials. As a proof of concept, the imprinted apportionment of functional groups within ZIF-8 was achieved by exchanging imine-based linker templates with original linkers initially. The removal of linker fragments by hydrolysis can be achieved via postsynthetic labilization, leading to the formation of architectures with controlled heterogeneity. The distributions of functional groups in the resulting imprinted MOFs can be tuned by judicious control of the interlocked chain length, which was further analyzed by computational methods. This work provides synthetic tools for precise control of pore environment and functionality sequences inside multicomponent materials.
Method for preparing polyamine by direct ammoniation of polyhydroxy compound
-
Paragraph 0046; 0047, (2016/10/24)
A method for preparing polyamine by direct ammoniation of a polyhydroxy compound is disclosed. By using a polyhydroxy compound, ammonia gas or liquefied ammonia as a raw material and using a carrier-loaded liquid-phase reduced transition metal as a catalyst, an ammoniation reaction of the polyhydroxy compound under mild conditions is realized. The catalyst has high selectivity of polyamine. The catalyst can be recovered and recycled.