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Some amides can be reduced to aldehydes in the Sonn-Müller method, but most routes to aldehydes involve a well-chosen organometallic reductant. Lithium aluminum hydride reduces an excess of N,N-disubstituted amides to an aldehyde: [citation needed] R(CO)NRR' + LiAlH 4 → RCHO + HNRR' With further reduction the alcohol is obtained.
In enzymology, an amidase (EC 3.5.1.4, acylamidase, acylase (misleading), amidohydrolase (ambiguous), deaminase (ambiguous), fatty acylamidase, N-acetylaminohydrolase (ambiguous)) is an enzyme that catalyzes the hydrolysis of an amide. In this way, the two substrates of this enzyme are an amide and H 2 O, whereas its two products are ...
Fatty-acid amide hydrolase 1 (FAAH) [5] is a member of the serine hydrolase family of enzymes. It was first shown to break down anandamide (AEA), an N -acylethanolamine (NAE) in 1993. [ 6 ] In humans, it is encoded by the gene FAAH .
The enzyme is involved in the biosynthesis of many signaling peptides and some fatty acid amides. [6] In humans, the enzyme is encoded by the PAM gene. [7] [8] This transformation is achieved by conversion of a prohormone to the corresponding amide (C(=O)NH 2). This enzyme is the only known pathway for generating peptide amides.
Reductive amination (also known as reductive alkylation) is a form of amination that converts a carbonyl group to an amine via an intermediate imine. The carbonyl group is most commonly a ketone or an aldehyde. It is a common method to make amines and is widely used in green chemistry since it can be done catalytically in one-pot under
Because lysine's pK a is so high (pK a =11), a glutamate and several other residues act as the acid to stabilise its deprotonated state during the catalytic cycle. [33] [34] Threonine proteases use their N-terminal amide as the base, since steric crowding by the catalytic threonine's methyl prevents other residues from being close enough. [35] [36]
Enzymes are often highly specific and act on only certain substrates. Some enzymes are absolutely specific meaning that they act on only one substrate, while others show group specificity and can act on similar but not identical chemical groups such as the peptide bond in different molecules. Many enzymes have stereochemical specificity and act ...
-Enzymes exhibit extreme selectivity towards their substrates. Typically enzymes display three major types of selectivity: Chemoselectivity: Since the purpose of an enzyme is to act on a single type of functional group, other sensitive functionalities, which would normally react to a certain extent under chemical catalysis, survive. As a result ...