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100910-66-5

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100910-66-5 Usage

General Description

5-Methylpyridine-3-carboxaldehyde is a chemical compound with the molecular formula C7H7NO. It is an aldehyde derivative of 5-methylpyridine and is commonly used as a synthetic intermediate in the production of pharmaceuticals and agrochemicals. The compound is also known for its use as a flavoring agent, especially in the food and beverage industry. 5-Methylpyridine-3-carboxaldehyde is a clear, colorless liquid with a strong, pungent odor. It is also known to be a skin and eye irritant, and should be handled with caution.

Check Digit Verification of cas no

The CAS Registry Mumber 100910-66-5 includes 9 digits separated into 3 groups by hyphens. The first part of the number,starting from the left, has 6 digits, 1,0,0,9,1 and 0 respectively; the second part has 2 digits, 6 and 6 respectively.
Calculate Digit Verification of CAS Registry Number 100910-66:
(8*1)+(7*0)+(6*0)+(5*9)+(4*1)+(3*0)+(2*6)+(1*6)=75
75 % 10 = 5
So 100910-66-5 is a valid CAS Registry Number.
InChI:InChI=1/C7H7NO/c1-6-2-7(5-9)4-8-3-6/h2-5H,1H3

100910-66-5SDS

SAFETY DATA SHEETS

According to Globally Harmonized System of Classification and Labelling of Chemicals (GHS) - Sixth revised edition

Version: 1.0

Creation Date: Aug 10, 2017

Revision Date: Aug 10, 2017

1.Identification

1.1 GHS Product identifier

Product name 5-Methylnicotinaldehyde

1.2 Other means of identification

Product number -
Other names 5-methylpyridine-3-carbaldehyde

1.3 Recommended use of the chemical and restrictions on use

Identified uses For industry use only.
Uses advised against no data available

1.4 Supplier's details

1.5 Emergency phone number

Emergency phone number -
Service hours Monday to Friday, 9am-5pm (Standard time zone: UTC/GMT +8 hours).

More Details:100910-66-5 SDS

100910-66-5Relevant articles and documents

Characterization of nicotinamidases: Steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism

French, Jarrod B.,Cen, Yana,Vrablik, Tracy L.,Xu, Ping,Allen, Eleanor,Hanna-Rose, Wendy,Sauve, Anthony A.

, p. 10421 - 10439 (2010)

Nicotinamidases are metabolic enzymes that hydrolyze nicotinamide to nicotinic acid. These enzymes are widely distributed across biology, with examples found encoded in the genomes of Mycobacteria, Archaea, Eubacteria, Protozoa, yeast, and invertebrates, but there are none found in mammals. Although recent structural work has improved our understanding of these enzymes, their catalytic mechanism is still not well understood. Recent data show that nicotinamidases are required for the growth and virulence of several pathogenic microbes. The enzymes of Saccharomyces cerevisiae, Drosophila melanogaster, and Caenorhabditis elegans regulate life span in their respective organisms, consistent with proposed roles in the regulation of NAD+ metabolism and organismal aging. In this work, the steady state kinetic parameters of nicotinamidase enzymes from C. elegans, Sa. cerevisiae, Streptococcus pneumoniae (a pathogen responsible for human pneumonia), Borrelia burgdorferi (the pathogen that causes Lyme disease), and Plasmodium falciparum (responsible for most human malaria) are reported. Nicotinamidases are generally efficient catalysts with steady state kcat values typically exceeding 1 s -1. The Km values for nicotinamide are low and in the range of 2 -110 μM. Nicotinaldehyde was determined to be a potent competitive inhibitor of these enzymes, binding in the low micromolar to low nanomolar range for all nicotinamidases tested. A variety of nicotinaldehyde derivatives were synthesized and evaluated as inhibitors in kinetic assays. Inhibitions are consistent with reaction of the universally conserved catalytic Cys on each enzyme with the aldehyde carbonyl carbon to form a thiohemiacetal complex that is stabilized by a conserved oxyanion hole. The S. pneumoniae nicotinamidase can catalyze exchange of 18O into the carboxy oxygens of nicotinic acid with H218O. The collected data, along with kinetic analysis of several mutants, allowed us to propose a catalytic mechanism that explains nicotinamidase and nicotinic acid 18O exchange chemistry for the S. pneumoniae enzyme involving key catalytic residues, a catalytic transition metal ion, and the intermediacy of a thioester intermediate.

HETEROCYCLIC AMIDES AS KINASE INHIBITORS

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Page/Page column 74, (2016/12/07)

Disclosed are compounds having the formula: (I) wherein R1, R2, and R3 are as defined herein, and methods of making and using the same.

Manganese oxide promoted liquid-phase aerobic oxidative amidation of methylarenes to monoamides using ammonia surrogates

Wang, Ye,Yamaguchi, Kazuya,Mizuno, Noritaka

supporting information; experimental part, p. 7250 - 7253 (2012/08/28)

In the presence of amorphous MnO2, various methylarenes (even with two or more methyl groups) could be selectively converted into the corresponding primary monoamides in moderate to high yields. The observed catalysis was truly heterogeneous, and the retrieved amorphous MnO2 catalyst could be reused without an appreciable loss of its catalytic performance. Copyright

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