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相关概念视频

Enzymes02:34

Enzymes

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Inside living organisms, enzymes act as catalysts for many biochemical reactions involved in cellular metabolism. The role of enzymes is to reduce the activation energies of biochemical reactions by forming complexes with its substrates. The lowering of activation energies favor an increase in the rates of biochemical reactions.
Enzyme deficiencies can often translate into life-threatening diseases. For example, a genetic abnormality resulting in the deficiency of the enzyme G6PD...
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Ligand Binding and Linkage00:49

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
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In animals, the mitochondrial F1F0 ATP synthase is the key protein that synthesizes ATP molecules through a complex catalytic mechanism. While the nuclear genome encodes the majority of ATP synthase subunits, the mitochondrial genome encodes some of the enzyme's most critical components. The formation of this multi-subunit enzyme is a complex multi-step process regulated at the level of transcription, translation, and assembly. Defects in one or more of these steps can result in decreased...
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Introduction to Mechanisms of Enzyme Catalysis01:13

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For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
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Binding sites linkages can regulate a protein's function.  For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
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相关实验视频

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Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues
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人体素甲基转移酶SET7/9的结构和催化机制

Bing Xiao1, Chun Jing, Jonathan R Wilson

  • 1Structural Biology Group, National Institute for Medical Research, Mill Hill, London NW7 1AA, UK.

Nature
|January 24, 2003
PubMed
概括

人类SET7/9是一种独特的单甲基酶,与其他SET蛋白不同. 它的晶体结构揭示了素标和辅因子的结合方式,解释了甲基化特异性和反应机制.

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科学领域:

  • 生物化学 生物化学
  • 分子生物学分子生物学
  • 表观遗传学 在表观遗传学中,表观遗传学是指表观遗传学.

背景情况:

  • 基因组的翻译后修改,包括乙化,酸化和甲基化,调节色素的结构和功能.
  • 希斯甲基化主要由SET (Su(var) 3-9,Enhancer-of-zeste,Trithorax) 域酶催化,大多数已知的酶甲基化特定的氨酸残留物.

研究的目的:

  • 通过人类SET7/9.9阐明组织素甲基化特异性的结构基础.
  • 了解SET7/9介导甲基化及其辅因子相互作用的机制.
  • 要将SET7/9描述为一种单甲基酶.

主要方法:

  • 一个涉及人类SET7/9的三元复合体的高分辨率晶体结构确定,其中包括一个组胺和辅因子S-adenosyl-l-methionine (AdoMet).
  • 溶液研究以确认酶活性和基质特异性.
  • 结构分析以确定酶活性部位内的关键相互作用和道.

主要成果:

  • 晶体结构显示,组织素基质和AdoMet辅因子与SET7/9.9的相反表面结合.
  • 酶内的狭窄通道有助于氨酸侧链进入活性部位和辅因子.
  • 证实SET7/9纯属单甲基酶,使其与其他SET蛋白区别开来.
  • 该结构为SET7/9对其基因组标的特异性的分子基础提供了洞察力.

结论:

  • SET7/9-希斯-AdoMet复合体的结构显示出一种独特的结合模式和道,用于基质访问.
  • SET7/9作为一种特定的单甲基酶起作用,其结构特征解释了基质识别和反应机制.
  • 这些发现有助于理解SET域蛋白在表观遗传调节中的多样性作用.