生物活性天然产品中的脱氨酸残留物
Shan Wang1, Kewen Wu2, Ya-Jie Tang1
1State Key Laboratory of Microbial Technology, Shandong University, Qingdao 266237, China. shan.wang@sdu.edu.cn.
Natural product reports
|November 9, 2023
概括
本综述探讨了脱氨基酸 (dhAAs),它们的合成灵活性,以及在折叠体和生物对角化学中的作用. 它强调了理解自然产品中不寻常的dhAA残留物的生物合成的进展.
科学领域:
- 生物化学和有机化学
- 自然产品生物合成 自然产品生物合成
- 类化学和折叠分子
背景情况:
- α,β-脱氨基酸 (dhAAs) 是不和的非蛋白质原性氨基酸,在细菌代谢物和其他自然产品中普遍存在.
- 该α,β-不和赋予显著的合成灵活性和在生物对等应用中的实用性.
- 含有dhAA的是折叠体研究中的关键组成部分,形成了像2.05螺旋体这样的定义良好的构造.
研究的目的:
- 审查含有不寻常的脱氨酸残留物的类天然产品生物合成的最新进展.
- 讨论这些不太了解的dhAA残留物的形成途径.
- 突出dhAAs在折叠材料和点击化学中的合成灵活性和应用.
主要方法:
- 关于天然产品生物合成的文献综述,重点关注2000年至2023年的脱氨基酸.
- 对含有不寻常和神秘的dhAA残留物的类天然产品提出的生物合成途径的分析.
- 讨论dHA的化学特性和应用,包括迈克尔添加,交叉合和生物对角化学.
主要成果:
- 脱氨酸 (Dha) 和脱氨酸 (Dhb) 是最丰富的dhAAs,通常在核糖体合成和翻译后修饰的 (RiPPs) 中发现.
- 在RiPPs中Dha和Dhb的生物合成已经得到了充分的研究,而其他dHAA的途径仍然不太了解.
- 含有dhAA残留的基折叠体具有独特的构造和聚合性质,其中一些通过光依赖性异构化进行调制.
结论:
- 在了解Dha和Dhb等常见的dhAAs的生物合成方面取得了重大进展.
- 需要进行进一步的研究,以阐明自然产品中不太常见和神秘的dhAA残留物的形成.
- dhAAs在合成化学,折叠体设计和生物对角应用中提供了广泛的潜力.
更多相关视频
08:01LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
Published on: April 9, 2017
8.2K
10:31Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
Published on: February 3, 2022
3.0K
相关概念视频
Amino acids
89.0K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
89.0K
Amino Acid Biosynthetic Pathways
17
Amino acid biosynthesis is essential for cell growth, protein synthesis, and metabolic regulation. Cells generate essential and non-essential amino acids from metabolic intermediates to sustain vital biological functions. These intermediates originate from key metabolic pathways: glycolysis, the tricarboxylic acid (TCA) cycle, and the pentose phosphate pathway. Important precursors include α-ketoglutarate, pyruvate, oxaloacetate, phosphoenolpyruvate, and erythrose-4-phosphate, which...
17
What are Proteins?
14.6K
Proteins are polymers of amino acids linked together by peptide bonds. Proteins and polypeptides are interchangeably used to refer to long chains of amino acids. However, polypeptides have a molecular weight of fewer than 10,000 daltons, while proteins have greater molecular weight. Polypeptides with less than 20 amino acids are called oligopeptides or simply peptides. Interactions among the constituent amino acid side chains of proteins help them fold into a stable 3-dimensional...
14.6K
Amides to Carboxylic Acids: Hydrolysis
3.2K
Amides can undergo either acid-catalyzed hydrolysis or base-promoted hydrolysis through a typical nucleophilic acyl substitution. Each hydrolysis requires severe conditions.
Acid-catalyzed hydrolysis:
Hydrolysis of amides under acidic conditions yields carboxylic acids. Since the reaction occurs slowly, hydrolysis requires the conditions of heat.
The mechanism begins with the protonation of the carbonyl oxygen by the acid catalyst. The protonation makes the amide carbonyl carbon more...
Acid-catalyzed hydrolysis:
Hydrolysis of amides under acidic conditions yields carboxylic acids. Since the reaction occurs slowly, hydrolysis requires the conditions of heat.
The mechanism begins with the protonation of the carbonyl oxygen by the acid catalyst. The protonation makes the amide carbonyl carbon more...
3.2K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
NMR Spectroscopy Of Amines
8.9K
In proton NMR spectroscopy, primary amines and secondary amines showcase their N–H protons as a broad signal in the chemical shift range between δ 0.5 and 5 ppm. The exact position in this range depends on several factors, including sample concentration, hydrogen bonding, and the type of solvent used. Since amine protons undergo fast proton exchange in solution, the protons are labile and therefore do not participate in any splitting with adjacent protons. Thus, the observed peak is...
8.9K
