701-44-0Relevant academic research and scientific papers
Novel nicotinamide analog as inhibitor of nicotinamide N-methyltransferase
Ruf, Sven,Hallur, Mahanandeesha Siddappa,Anchan, Nisha K.,Swamy, Indu N.,Murugesan, Karthikai Raj,Sarkar, Sayantani,Narasimhulu, Lokesh Kananti,Putta, V.P. Rama Kishore,Shaik, Shama,Chandrasekar, Devaraj Venkatapura,Mane, Vishal Subhash,Kadnur, Sanjay Venkatachalapathi,Suresh, Juluri,Bhamidipati, Ravi Kanth,Singh, Manvi,Burri, Raghunadha Reddy,Kristam, Rajendra,Schreuder, Herman,Czech, Joerg,Rudolph, Christine,Marker, Alexander,Langer, Thomas,Mullangi, Ramesh,Yura, Takeshi,Gosu, Ramachandraiah,Kannt, Aimo,Dhakshinamoorthy, Saravanakumar,Rajagopal, Sridharan
supporting information, p. 922 - 925 (2018/02/14)
Nicotinamide N-methyltransferase (NNMT) has been linked to obesity and diabetes. We have identified a novel nicotinamide (NA) analog, compound 12 that inhibited NNMT enzymatic activity and reduced the formation of 1-methyl-nicotinamide (MNA), the primary metabolite of NA by ~80% at 2 h when dosed in mice orally at 50 mg/kg.
Direct comparison of the enzymatic characteristics and superoxide production of the four aldehyde oxidase enzymes present in mouse
Kücükg?ze, G?khan,Terao, Mineko,Garattini, Enrico,Leimkühler, Silke
, p. 947 - 955 (2017/07/22)
Aldehyde oxidases (AOXs) are molybdoflavoenzymes with an important role in the metabolism and detoxification of heterocyclic compounds and aliphatic as well as aromatic aldehydes. The enzymes use oxygen as the terminal electron acceptor and produce reduced oxygen species during turnover. Four different enzymes, mAOX1, mAOX3, mAOX4, and mAOX2, which are the products of distinct genes, are present in the mouse. A direct and simultaneous comparison of the enzymatic properties and characteristics of the four enzymes has never been performed. In this report, the four catalytically active mAOX enzymes were purified after heterologous expression in Escherichia coli. The kinetic parameters of the four mouse AOX enzymes were determined and compared with the use of six predicted substrates of physiologic and toxicological interest, i.e., retinaldehyde, N1-methylnicotinamide, pyridoxal, vanillin, 4-(dimethylamino)cinnamaldehyde (p-DMAC), and salicylaldehyde. While retinaldehyde, vanillin, p-DMAC, and salycilaldehyde are efficient substrates for the four mouse AOX enzymes, N1-methylnicotinamide is not a substrate of mAOX1 or mAOX4, and pyridoxal is not metabolized by any of the purified enzymes. Overall, mAOX1, mAOX2, mAOX3, and mAOX4 are characterized by significantly different KM and kcat values for the active substrates. The four mouse AOXs are also characterized by quantitative differences in their ability to produce superoxide radicals. With respect to this last point, mAOX2 is the enzyme generating the largest rate of superoxide radicals of around 40% in relation to moles of substrate converted, and mAOX1, the homolog to the human enzyme, produces a rate of approximately 30% of superoxide radicals with the same substrate.
HETEROCYCLIC CGRP RECEPTOR ANTAGONISTS
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Page/Page column 73, (2015/11/09)
The present invention is directed to heterocyclic compounds which are antagonists of CGRP receptors and useful in the treatment or prevention of diseases in which CGRP is involved, such as migraine. The invention is also directed to pharmaceutical composi
IMINATION OF PYRIDINIUM AND QUINOLINIUM SALTS
Plas, H. C. van der,Buurman, D. J.
, p. 3763 - 3764 (2007/10/02)
A new method for imination of N-alkyl pyridinium- and quinolinium salts is described.It involves a low temperature oxidation of a solution of appropriate substrates in liquid ammonia with potassium permanganate.
The use of immobilized enzymes in organic synthesis. Part 6. Oxidation of 1-alkyl-3-carbamoylpyridinium chlorides by rabbit liver aldehyde oxidase
Angelino, S.A.G.F.,Buurman, D.J.,Plas, H.C. van der,Mueller, F.
, p. 342 - 346 (2007/10/02)
A method is described for the oxidation of some 1-alkyl-3-carbamoylpyridinium chlorides by reaction with immobilized rabbit liver aldehyde oxydase.With the 1-methyl-, 1-ethyl- and 1-n-propyl derivatives, only the 1-alkyl-1,6-dihydro-6-oxo-3-pyridinecarboxamides have been obtained, but with the t-Bu analogue the corresponding 4-oxo compound was found as single product.The i-Pr derivative gave rise to a mixture of the corresponding 4- and 6-oxo compounds.From the kinetic data some information has been acquired with respect to the enzyme active-site environment and the binding of the substrates to the enzyme.
