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Biology
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Research on Enzyme Activities and New Advances on Their Regulation
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Research on Enzyme Activities and New Advances on Their Regulation

A special issue of Biology (ISSN 2079-7737).

Deadline for manuscript submissions: closed (15 May 2022) | Viewed by 8673

Special Issue Editor

Dr. Roberta Moschini

E-Mail Website
Guest Editor
Department of Biology, University of Pisa, Via S. Zeno 51, 56127 Pisa, Italy
Interests: enzyme kinetic; enzyme inhibition assays; nutraceuticals; natural or synthetic bioactive compounds; proteins purification; oxidative stress; antioxidants; cellular biochemistry
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

enzymes are unique for cell life and their study represent a relevant aspect in modern biology going from the clarification of their role in both cellular metabolism and diseases to their biotechnological applications. The study of the regulation and modulation of enzyme activities has a key role in different biological aspects, not only for pharmacological applications but also for a better knowledge of the role of enzymes in the main cellular metabolic pathways.  Thus, structural and functional characterization of enzymes is fundamental in order to define the most efficient molecules for the modulation of enzyme activity.

 Aim of the issue is to present reviews or research articles addressed to broaden the knowledge of enzymes in both structural and functional terms. The articles will focus on various aspects of enzyme study, from enzyme kinetics to their structural characterization and their application in both pharmacological and biotechnological fields.

Dr. Roberta Moschini
Guest Editor

Manuscript Submission Information

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Keywords

  • Keywords: enzyme structure
  • catalytic mechanism
  • enzyme inhibition
  • natural or synthetic bioactive compounds
  • enzyme regulation
  • protein engineering
  • molecular pathology
  • drug design
  • molecular disease

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Published Papers (2 papers)

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Research

11 pages, 1882 KiB  
Article
Biostimulatory Effects of Amino Acids on Phenylalanine Ammonia Lyase, Capsaicin Synthase, and Peroxidase Activities in Capsicum baccatum L.
by Tilen Zamljen, Aljaz Medic, Metka Hudina, Robert Veberic and Ana Slatnar
Biology 2022, 11(5), 674; https://doi.org/10.3390/biology11050674 - 27 Apr 2022
Cited by 9 | Viewed by 2435
Abstract
Biostimulants are widely used in agriculture because they can improve fruit quality and quantity. Less is known about how biostimulants act over time in plants, in our case peppers, and how they affect the enzyme activity of important enzymes for capsaicinoid synthesis. The [...] Read more.
Biostimulants are widely used in agriculture because they can improve fruit quality and quantity. Less is known about how biostimulants act over time in plants, in our case peppers, and how they affect the enzyme activity of important enzymes for capsaicinoid synthesis. The biostimulatory effects of amino acids on the activities of phenylalanine ammonia lyase (PAL), capsaicin synthase (CS), and peroxidase (POX) were investigated in the pericarp and placenta of the chili pepper Capsicum baccatum L. cv. “Bishop Crown” over 72 h of application. The PAL and CS activities significantly increased in the placenta after 1 h of biostimulant application, with significant increases of 130% and 16%, respectively. The POX activity remained unchanged over the full 72 h in the placenta but significantly increased after 48 h in the pericarp (+53%). Total capsaicinoids increased in the first hour of biostimulant application, by 4.30 g/kg FW in the placenta (19%) and by 0.94 g/kg FW in the pericarp (+56%). Biostimulant application also increased total and individual capsaicinoids after 48 h in the chili placenta and pericarp. With improved methods for enzymatic determination, we gained new insights into the responses of chilies to biostimulant amino acids. Full article
(This article belongs to the Special Issue Research on Enzyme Activities and New Advances on Their Regulation)
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16 pages, 17594 KiB  
Article
Effects of A6E Mutation on Protein Expression and Supramolecular Assembly of Yeast Asparagine Synthetase
by Thunyarat Surasiang and Chalongrat Noree
Biology 2021, 10(4), 294; https://doi.org/10.3390/biology10040294 - 3 Apr 2021
Cited by 1 | Viewed by 3828
Abstract
Asparagine synthetase deficiency (ASD) has been found to be caused by certain mutations in the gene encoding human asparagine synthetase (ASNS). Among reported mutations, A6E mutation showed the greatest reduction in ASNS abundance. However, the effect of A6E mutation has not yet been [...] Read more.
Asparagine synthetase deficiency (ASD) has been found to be caused by certain mutations in the gene encoding human asparagine synthetase (ASNS). Among reported mutations, A6E mutation showed the greatest reduction in ASNS abundance. However, the effect of A6E mutation has not yet been tested with yeast asparagine synthetase (Asn1/2p). Here, we constructed a yeast strain by deleting ASN2 from its genome, introducing the A6E mutation codon to ASN1, along with GFP downstream of ASN1. Our mutant yeast construct showed a noticeable decrease of Asn1p(A6E)-GFP levels as compared to the control yeast expressing Asn1p(WT)-GFP. At the stationary phase, the A6E mutation also markedly lowered the assembly frequency of the enzyme. In contrast to Asn1p(WT)-GFP, Asn1p(A6E)-GFP was insensitive to changes in the intracellular energy levels upon treatment with sodium azide during the log phase or fresh glucose at the stationary phase. Our study has confirmed that the effect of A6E mutation on protein expression levels of asparagine synthetase is common in both unicellular and multicellular eukaryotes, suggesting that yeast could be a model of ASD. Furthermore, A6E mutation could be introduced to the ASNS gene of acute lymphoblastic leukemia patients to inhibit the upregulation of ASNS by cancer cells, reducing the risk of developing resistance to the asparaginase treatment. Full article
(This article belongs to the Special Issue Research on Enzyme Activities and New Advances on Their Regulation)
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