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Cited by 290Protease and Inhibitor MechanismsEnzyme Production and CharacterizationEnzyme Structure and Function

The DOI matches its Crossref record; 75 of the 77 references it cites were found in a registry or an index.

Research Applications of Proteolytic Enzymes in Molecular Biology

Open access
Mótyán, János, Tóth, Ferenc, Tőzsér, József·2013·Biomolecules
DOI 10.3390/biom3040923PMC PMC4030975
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Abstract

Proteolytic enzymes (also termed peptidases, proteases and proteinases) are capable of hydrolyzing peptide bonds in proteins. They can be found in all living organisms, from viruses to animals and humans. Proteolytic enzymes have great medical and pharmaceutical importance due to their key role in biological processes and in the life-cycle of many pathogens. Proteases are extensively applied enzymes in several sectors of industry and biotechnology, furthermore, numerous research applications require their use, including production of Klenow fragments, peptide synthesis, digestion of unwanted proteins during nucleic acid purification, cell culturing and tissue dissociation, preparation of recombinant antibody fragments for research, diagnostics and therapy, exploration of the structure-function relationships by structural studies, removal of affinity tags from fusion proteins in recombinant protein techniques, peptide sequencing and proteolytic digestion of proteins in proteomics. The aim of this paper is to review the molecular biological aspects of proteolytic enzymes and summarize their applications in the life sciences.

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Crossref · 10.3390/biom3040923

Cites

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Figures

Figure 1 Action of aminopeptidases and carboxypeptidases removing the terminal amino acid residues as well as endopeptidases on a polypeptide substrate (having n residues). Red arrows show the peptide bonds to be cleaved.
Figure 1 Action of aminopeptidases and carboxypeptidases removing the terminal amino acid residues as well as endopeptidases on a polypeptide substrate (having n residues). Red arrows show the peptide bonds to be cleaved.CC BY · PubMed Central
Figure 2 Kinetically-controlled synthesis of Z-d-Leu-l-Leu-NH2 dipeptide. After the formation of enzyme-substrate complex (K1) a covalent enzyme-substrate intermediate is formed (K2). The intermediate is subjected to the attack from H2O or other nucleophiles (Nu). KH is the equilibrium constant of hydrolysis, KT is the equilibrium constant of the transferase reaction.
Figure 2 Kinetically-controlled synthesis of Z-d-Leu-l-Leu-NH2 dipeptide. After the formation of enzyme-substrate complex (K1) a covalent enzyme-substrate intermediate is formed (K2). The intermediate is subjected to the attack from H2O or other nucleophiles (Nu). KH is the equilibrium constant of hydrolysis, KT is the equilibrium constant of the transferase reaction.CC BY · PubMed Central
Figure 3 Structure of IgG antibody molecules (A) and fragments released after proteolytic digestion using papain (B), pepsin (C) or ficin (D).
Figure 3 Structure of IgG antibody molecules (A) and fragments released after proteolytic digestion using papain (B), pepsin (C) or ficin (D).CC BY · PubMed Central
Figure 4 Steps of proteomic analysis using mass-spectrometry after separation and in-gel digestion of proteins of interest.
Figure 4 Steps of proteomic analysis using mass-spectrometry after separation and in-gel digestion of proteins of interest.CC BY · PubMed Central

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Show all 77 references

Research works printed but not linked: 4

  1. Rani, 2012, Review on latest overview of proteases, Int. J. Curr. Life Sci., 2, 12
  2. Bhalla, 1999, Thermophilic bacterial proteases, J. Punjab Acad. Sci., 1, 77
  3. Ragnurrson, U. (, 1985). Use of Proteolytic Enzymes for the Synthesis of Fragments of Mouse Epidermal Growth Factor. Proceedings of Peptides 1984, Almquist, Stockholm.
  4. Adamczak, 2004, Enzyme for efficient biocatalysis, Food Technol. Biotechnol., 42, 251

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Metadata

Authors
Mótyán, J., Tóth, F., & Tőzsér, J.
Affiliations
University of Debrecen (HU)
Corresponding author
Tőzsér, József
ORCID
Venue
Biomolecules
Publisher
MDPI AG
Published
2013-11-08
Volume
3
Issue
4
Pages
923-942
ISSN
2218-273X (ISSN-L)
DOI
10.3390/biom3040923
PMC
PMC4030975
OpenAlex
W2130109271
Cited by
267
References
77
Citations by year
2026: 14 · 2025: 24 · 2024: 34 · 2023: 38 · 2022: 29 · 2021: 32 · 2020: 26 · 2019: 31 · 2018: 11 · 2017: 7 · 2016: 9 · 2015: 5 · 2014: 5
FWCI
2.23
Type
journal article
Language
en
Open access
Licence
Locations
  • Biomolecules (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion)
  • University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion)
Funders
  • European Regional Development Fund
  • European Social Fund
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
Keywords
proteolytic enzymes, Klenow fragment, peptide synthesis, nucleic acid purification, tissue dissociation, recombinant antibody fragments, proteomics, peptide sequencing, structure-function relationship, protease inhibitors

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