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Related Concept Videos

Phase II Reactions: Acetylation Reactions01:24

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
The substrates for acetylation are typically drugs or their metabolites with an amino, sulfonamide, or hydrazine functional group. Acetylation can occur at several points in the drug molecule, including primary, secondary, and...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Allosteric Proteins-ATCase01:19

Allosteric Proteins-ATCase

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.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to  N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...
The Citric Acid Cycle: Output01:28

The Citric Acid Cycle: Output

The citric acid cycle is termed an amphibolic pathway as it operates both anabolically and catabolically. The cyclic reactions balance the flux of the substrates to provide an optimal concentration of NADH and ATP to the cell.
Regulation of Citric Acid Cycle
The citric acid cycle is regulated in several ways, including feedback inhibition, regulation of enzyme activities, and associated anaplerotic or cataplerotic pathways.
The primary substrate of the TCA cycle—acetyl CoA—is produced by the...
The Citric Acid Cycle02:36

The Citric Acid Cycle

The citric acid cycle, also known as the Krebs cycle or TCA cycle, consists of several energy-generating reactions that yield one ATP molecule, three NADH molecules, one FADH2 molecule, and two CO2 molecules.
Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.

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Related Experiment Video

Updated: Jun 3, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
05:51

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase

Published on: December 19, 2011

Acetate kinase and phosphotransacetylase.

James G Ferry1

  • 1Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania, USA.

Methods in Enzymology
|March 16, 2011
PubMed
Summary

Key enzymes phosphotransacetylase and acetate kinase are central to methane production from acetate in anaerobic microbes. Their characterization in Methanosarcina species reveals ancient origins and common catalytic mechanisms with bacterial enzymes.

Area of Science:

  • Biochemistry
  • Microbiology
  • Enzymology

Background:

  • Methane is primarily produced from acetate by anaerobic microbes.
  • Acetate is converted to acetyl-CoA by phosphotransacetylase and acetate kinase.
  • These enzymes play a crucial role in the anaerobic digestion of organic matter.

Purpose of the Study:

  • To characterize phosphotransacetylase and acetate kinase from Methanosarcina thermophila.
  • To elucidate the catalytic mechanisms and evolutionary origins of these enzymes.
  • To investigate their role in methane biosynthesis.

Main Methods:

  • Purification and biochemical characterization of enzymes from Methanosarcina thermophila.
  • Recombinant expression of enzymes in Escherichia coli.

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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity

Published on: January 5, 2016

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Last Updated: Jun 3, 2026

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase
05:51

Direct Detection of the Acetate-forming Activity of the Enzyme Acetate Kinase

Published on: December 19, 2011

Liquid Chromatography Coupled to Refractive Index or Mass Spectrometric Detection for Metabolite Profiling in Lysate-based Cell-free Systems
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Liquid Chromatography Coupled to Refractive Index or Mass Spectrometric Detection for Metabolite Profiling in Lysate-based Cell-free Systems

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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity
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In Vitro Assay to Measure Phosphatidylethanolamine Methyltransferase Activity

Published on: January 5, 2016

  • X-ray crystallography for structural analysis.
  • Kinetic and biochemical studies of wild-type and variant enzymes.

    • Main Results:

    • Both phosphotransacetylase and acetate kinase were purified and characterized.
    • Enzymes were successfully expressed in E. coli, enabling structural and mechanistic studies.
    • Crystal structures and kinetic analyses provided insights into catalytic mechanisms.
    • High sequence identity to bacterial homologs suggests ancient origins.

    Conclusions:

    • Phosphotransacetylase and acetate kinase are essential for methane formation from acetate in Methanosarcina.
    • Structural and biochemical data offer detailed mechanistic proposals.
    • The enzymes' ancient origins and conserved mechanisms highlight fundamental biological processes.