142-92-7Relevant articles and documents
Chemical defense in the stink bug Cosmopepla bimaculata
Krall, Bryan S.,Bartelt, Robert J.,Lewis, Cara J.,Whitman, Douglas W.
, p. 2477 - 2494 (1999)
Adult Cosmopepla bimaculata discharge a volatile secretion from paired ventral metathoracic glands (MTG) when disturbed. Collected volatiles were similar in both sexes and consisted of n-tridecane (67%), (E)-2-decenal (12%), (E)-2-decenyl acetate (12%), (E)-2-hexenal (3%), hexyl acetate (2%), n-dodecane (2%), a tridecene isomer (1%), and n-undecane, n-tetradecane, and n-pentadecane (all 1%). In addition, undisturbed males produced a novel insect compound, (E)-8-heneicosene, whose function is unknown. The MTG secretion emerges as an enlarging droplet, which is held in place by a cuticular projection and a pleural scent area consisting of specialized rough cuticle surrounding the gland opening. Insects can selectively discharge from either the right or left gland or both glands simultaneously, can control the amount of fluid ejected, and can resorb the ejected secretion droplet back into the gland reservoir, in feeding trials, killdeer (Charadrius vociferus), starlings (Sturnus vulgaris), robins (Turdus migratorius), and anole lizards (Anolis carolinensis) rejected or demonstrated aversion to feeding on the bugs. Furthermore, bugs that lacked the secretion were more susceptible to predation than bugs with secretion, suggesting that the secretion functions in defense against predators.
Characterization of Alcohol Acyltransferase from Olive Fruit
Salas, Joaquin J.
, p. 3155 - 3158 (2004)
Alcohol acyltransferase catalyzes the esterification of volatile alcohols with acyl-CoA derivatives to produce volatile esters typically present in the aroma of some fruits. This enzyme was detected in extracts from the pericarp tissues of ripe olive fruits using hexanol and acetyl-CoA as the substrates. Alcohol acyltransferase showed a very low activity level in these fruits, with an optimum pH value at 7.5 and high Km values for hexanol and acetyl-CoA. The substrate specificity of this enzyme for various alcohols was also studied. The involvement of the studied enzyme in the biogenesis of the volatile esters present in the aroma of virgin olive oil was discussed.
Molybdenum-modified mesoporous SiO2as an efficient Lewis acid catalyst for the acetylation of alcohols
Hlatshwayo, Xolani S.,Ndolomingo, Matumuene Joe,Bingwa, Ndzondelelo,Meijboom, Reinout
, p. 16468 - 16477 (2021/05/19)
A suitable, expeditious and well-organized approach for the acetylation of alcohols with acetic anhydride in the presence of 5%MoO3-SiO2 as an optimum environmentally benign heterogeneous catalyst was developed. The high surface area obtained for 5%MoO3-SiO2, 101 m2 g-1 compared to other catalysts, 22, 23, and 44 m2 g-1 for 5%WO3-ZrO2, 5%WO3-SiO2, and 5%MoO3-ZrO2, respectively, appears to be the driving force for better catalytic activity. Amongst the two dopants used, molybdenum oxide is the better dopant compared to its tungsten oxide counterpart. High yields of up to 86% were obtained with MoO3 doping while WO3 containing catalysts did not show any activity. Other reaction parameters such as reactor stirring speed, and solvent variation were studied and revealed that the optimum stirring speed is 400 rpm and cyclohexane is the best solvent. Thus, the utilization of affordable and nontoxic materials, short reaction times, reusability, and producibility of excellent yields of the desired products are the advantages of this procedure.
Alkyl substituted 4-N-oxazadisilinane cations: A new family of Si protic ionic liquids and its application on esterification reactions
Alhaddad, Maha,Chakraborty, Priyanka,Hu, Jinsong,Huang, Kuo-Wei
supporting information, (2020/06/08)
A series of oxazadisilinane compounds were prepared and used as Br?nsted bases to form a series of 21 siloxane protic ionic liquids (Si-PILs) with four different acids. This new family of Si-PILs were well characterized and examined to catalyze esterification reactions.
Genome Mining of Oxidation Modules in trans-Acyltransferase Polyketide Synthases Reveals a Culturable Source for Lobatamides
Ueoka, Reiko,Meoded, Roy A.,Gran-Scheuch, Alejandro,Bhushan, Agneya,Fraaije, Marco W.,Piel, J?rn
supporting information, p. 7761 - 7765 (2020/03/25)
Bacterial trans-acyltransferase polyketide synthases (trans-AT PKSs) are multimodular megaenzymes that biosynthesize many bioactive natural products. They contain a remarkable range of domains and module types that introduce different substituents into growing polyketide chains. As one such modification, we recently reported Baeyer–Villiger-type oxygen insertion into nascent polyketide backbones, thereby generating malonyl thioester intermediates. In this work, genome mining focusing on architecturally diverse oxidation modules in trans-AT PKSs led us to the culturable plant symbiont Gynuella sunshinyii, which harbors two distinct modules in one orphan PKS. The PKS product was revealed to be lobatamide A, a potent cytotoxin previously only known from a marine tunicate. Biochemical studies show that one module generates glycolyl thioester intermediates, while the other is proposed to be involved in oxime formation. The data suggest varied roles of oxygenation modules in the biosynthesis of polyketide scaffolds and support the importance of trans-AT PKSs in the specialized metabolism of symbiotic bacteria.