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Related Concept Videos

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.
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Bacterial Protein Maturation01:26

Bacterial Protein Maturation

Bacterial protein maturation is a tightly regulated process that ensures newly synthesized polypeptides achieve correct functional conformations. This maturation involves a series of modifications, folding events, and quality control steps, often assisted by specialized chaperone proteins.N-Terminal ModificationsThe maturation of bacterial polypeptides begins cotranslationally as the polypeptide exits the ribosome. The first amino acid, N-formylmethionine (fMet), is typically modified at the...
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...
Protein Folding01:22

Protein Folding

Overview
Protein Folding01:25

Protein Folding

Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...

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Updated: May 12, 2026

Enzymatic Modification and Flow Cytometry Assessment of Yeast Surface Displayed Proteins
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Published on: May 30, 2025

Effect of posttranslational modifications on enzyme function and assembly.

Helena Ryšlavá1, Veronika Doubnerová, Daniel Kavan

  • 1Department of Biochemistry, Faculty of Science, Charles University in Prague, Hlavova 8, CZ-12840 Prague 2, Czech Republic.

Journal of Proteomics
|April 23, 2013
PubMed
Summary

Researchers are uncovering hundreds of distinct post-translational modifications (PTMs) on enzymes. Understanding these PTMs is crucial for enzyme regulation and systems biology approaches.

Keywords:
ABRFAGEALEAMLAPC/CAssociation for Biomolecular Resource FacilitiesCCTCDKCHOCOS-1CSCCV-1 in Origin carrying SV40 genetic material (cell line)Catalytic activityCellular localizationChinese hamster ovaryECECDEGFER-associated protein degradationERADEnzymeGFPHECTHEKIP3MDMMMPMRMPosttranslational modificationRAGERINGRNSS-adenosyl-l-homocysteineS-adenosyl-l-methionineSAHSAMSILStabilityStructureTASTCP-1acute myeloid leukemiaadvanced glycosylation endproductadvanced lipooxidation endproductanaphase-promoting complex/cyclosomecell surface capture technologychaperone containing TCP-1cyclin-dependent kinaseelectron capture dissociationenzyme commission of IUPACepidermal growth factorgreen fluorescent proteinhomologous to the E6-AP carboxyl terminushuman embryonic kidneyinositoltrisphosphatematrix metalloproteinasemultiple reaction monitoringmurine double minutereactive nitrogen speciesreally interesting new genereceptor for advanced glycosylation end productsstable isotope labelingtagging via substrate approachtailless complex polypeptide-1

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Area of Science:

  • Biochemistry
  • Proteomics
  • Systems Biology

Background:

  • Hundreds of distinct post-translational modifications (PTMs) are identified on enzyme molecules using advanced techniques.
  • Global proteomics analyses reveal widespread distribution of PTMs across key enzymes in all cellular compartments.
  • PTMs play a critical role in regulating enzyme catalytic activity through complex interplays.

Purpose of the Study:

  • To provide a holistic understanding of enzyme function by evaluating patterns of multiple PTMs.
  • To explore the integration of proteomics with other 'omics' fields for systems biology strategies.
  • To highlight the need for detailed structural investigations and future high-throughput analytical techniques for PTM detection.

Main Methods:

  • Mass spectrometry and other techniques for detailed examination of enzyme molecules.
  • Contemporary proteomics for global analyses of enzyme PTMs.
  • Integration of proteomics with molecular genetics and transcriptomics for systems biology.

Main Results:

  • Identification of hundreds of distinct PTMs on enzymes.
  • Widespread distribution of PTMs on key enzymes across cellular compartments.
  • Functional evaluation of multiple enzymatic and nonenzymatic PTMs within single enzymes.

Conclusions:

  • Multiple PTMs and their interplays are critical for enzyme catalytic activity regulation.
  • Systems biology strategies integrating proteomics offer functional interrogation of enzymatic networks.
  • Future high-throughput techniques are envisioned for global PTM detection at the proteome level.