Enzyme-Based Organic Synthesis. Cheanyeh Cheng
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Название: Enzyme-Based Organic Synthesis
Автор: Cheanyeh Cheng
Издательство: John Wiley & Sons Limited
Жанр: Химия
isbn: 9781118995150
isbn:
Instead of small molecules acetylation, reversible protein acetylation by corresponding acetyltransferase is a ubiquitous means for the rapid control of diverse cellular processes [59, 60]. The acetyl group on acetyl‐CoA is transferred to the ε‐amino group of lysine residues of the acceptor protein by acetyltransferase. This is just the case for the acetylation of histones by histone acetyltransferases (HATs) that has an important role in transcriptional regulation by remodeling chromatin structure. The acetylation of histones may result in altering interactions between protein–protein and protein–DNA complexes due to the neutralization of positive charged lysine in the amino termini of histone proteins [61, 62]. In higher organisms, aberrant acetylation of lysine residues in histone tails correlates with diseases such as cancers and developmental disorders and may contribute to modulation of cell life span [63, 64]. In mammalian mitochondrial matrix, endoplasmic reticulum lumen, and peroxisomes, carnitine acetyltransferase (CrAT) catalyzes the reversible transfer of acetyl groups between acetyl‐CoA and l‐carnitine (β‐hydroxy‐γ‐trimethylammonium butyrate). The main function of carnitine is the transfer of long‐chain fatty acids to mitochondria for subsequent β‐oxidation. CrAT is homologous to other carnitine acyltransferases, particularly, to carnitine palmitoyltransferase 1 (CPT I) that serves the regulation of long‐chain fatty acid metabolism. Therefore, the reversibly catalyzed reaction between acetyl‐CoA and carnitine by CrAT makes CrAT a regulator for the cellular pool of CoA that, in turn, plays a role as a carrier of activated acetyl groups in the oxidation of energy metabolism substrates and in the synthesis of fatty acids and lipids. It is also known that the accumulation of fatty acyl‐CoAs in heart may induce apoptosis and inflammation and acetyl‐carnitine improves cognition in the brain [65–67].
Scheme 3.15 Protein acetylation with CRTase and DAMC without involving acetyl‐CoA.
Source: Arora et al. [71].
The model acetoxy‐coumarins (AC), 7,8‐diacetoxy‐4‐methylcoumarin (DAMC), was shown to possess radical scavenger property by interacting with free radical to remove its acetyl group and give the acetyl cation (CH3CO+) and the phenoxyl radical [68]. The antioxidant action of DAMC is independent on the formation of parent 7,8‐dihydroxy‐4‐methylcoumarin (DHMC). Calreticulin (CR) catalyzes the transfer of acetyl groups from AC to certain proteins [69, 70]; thus, CR was termed calreticulin transacetylase (CRTase). The enzymatic acetylation of protein by CRTase is unique and characterized as without involving acetyl‐CoA. CRTase of rat tracheal smooth muscle cells (TSMC) was characterized the specificity of DAMC for acetylating and activating nitric oxide synthase (NOS) as illustrated by Scheme 3.15 [71]. Since the activated TSMC NOS will enhance NO in airway cells, and NO is believed to ameliorate the exacerbation of airway diseases such as asthma and coronary obstructive pulmonary diseases (COPD), AC may be expected to find therapeutic applications in respiratory diseases [71, 72].
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