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Related Concept Videos

Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
Nucleosome Remodeling02:54

Nucleosome Remodeling

Nucleosomes are the basic units of chromatin compaction. Each nucleosome consists of the DNA bound tightly around a histone core, which makes the DNA inaccessible to DNA binding proteins such as DNA polymerase and RNA polymerase. Hence, the fundamental problem is to ensure access to DNA when appropriate, despite the compact and protective chromatin structure.
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Ligand-Gated Ion Channel Receptor: Gating Mechanism01:30

Ligand-Gated Ion Channel Receptor: Gating Mechanism

Ligand-gated ion channels are transmembrane proteins that play a vital role in intercellular communication and functions of the nervous system. They allow the influx of ions across the membrane once the neurotransmitter binds, allowing the subsequent transmission of electrical excitation across the neurons. Other ligand-gated ion channels, like the γ-aminobutyric acid (GABA) receptor, permit anions like chloride into the cells on the binding of the GABA molecule. Their entry into the cell...
Covalently Linked Protein Regulators02:04

Covalently Linked Protein Regulators

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.
These groups modify specific amino acids in a protein.

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Related Experiment Video

Updated: Jun 20, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

Methyltransferase "Gating Loop" Reengineering: Reshaping Catalytic Performance through Tunnel Dynamics and Structural

Ming-Xin Sun1, Cui Zhang1, Zhi-Han Gong1

  • 1The Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800# Lihu Road, WuXi 214122, People's Republic of China.

Journal of Agricultural and Food Chemistry
|June 19, 2026
PubMed
Summary
This summary is machine-generated.

Engineered methyltransferase M5 enhances L-hypaphorine production from L-tryptophan. This enzyme modification optimizes the substrate tunnel for improved methylation, offering a new method for enzyme functional modification.

Keywords:
Gating loopL-HypaphorineMethyltransferaseSubstrate retentionTunnel engineering

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Last Updated: Jun 20, 2026

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
09:42

Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes

Published on: January 16, 2016

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08:34

An Engineered Split-TET2 Enzyme for Chemical-inducible DNA Hydroxymethylation and Epigenetic Remodeling

Published on: December 18, 2017

Area of Science:

  • Biochemistry
  • Enzyme Engineering
  • Medicinal Chemistry

Background:

  • The methyltransferase EgtD from Mycobacterium smegmatis is crucial for producing L-hypaphorine, a valuable indole alkaloid.
  • Understanding the structural basis of EgtD's activity is key to enhancing its catalytic efficiency.

Purpose of the Study:

  • To engineer a double mutant MsE of EgtD for improved N-terminal trimethylation of L-tryptophan.
  • To investigate the structural determinants of MsE activity and substrate binding.
  • To enhance the enzyme's conversion rate and relative activity.

Main Methods:

  • Site-directed mutagenesis (alanine scanning, saturation mutagenesis) targeting critical loops (Loop34-39, Loop163-168).
  • Enzyme activity assays to compare wild-type, MsE, and M5 mutant.
  • Molecular dynamics simulations, CAVER tunnel analysis, and ligand dissociation pathway studies.

Main Results:

  • Identified Loop34-39 and Loop163-168 as critical for MsE activity and substrate binding.
  • Developed mutant M5 (P35C/K36R/F38L/T163G/T168F) with a 7.11-fold increase in relative activity and 58.93% conversion rate.
  • M5 remodels the active site and substrate access tunnel, creating a "capture-release" microcompartment for methylation.

Conclusions:

  • Loop optimization is an effective strategy for enzyme functional modification.
  • Mutant M5 demonstrates significantly enhanced catalytic performance for L-hypaphorine production.
  • The study provides a foundation for further enzyme engineering and the development of biocatalysts.