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Biomolecules
Special Issues
Feature Papers in Enzymology—2nd Edition
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Feature Papers in Enzymology—2nd Edition

A special issue of Biomolecules (ISSN 2218-273X). This special issue belongs to the section "Enzymology".

Deadline for manuscript submissions: 28 February 2025 | Viewed by 876

Special Issue Editor

Prof. Dr. Piero Crespo

E-Mail Website
Guest Editor
CSIC Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC), Santander, Spain
Interests: Ras-ERK pathway spatial regulation; scaffold proteins; protein-protein interactions as therapeutic targets
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Based on the success of the first Special Issue, this second Special Issue of “Feature Papers in Enzymology” aims to collect high-quality research articles, review articles, and communications on all aspects of enzymology. It is dedicated to recent advances in the broad research area of enzymology and is inclusive of papers focused on the structure, function, and properties of enzymes, as well as catalytic and inhibition mechanisms of enzymes, mechanisms of drug action, and related advances in enzymes. This Special Issue will highlight advances in all types of enzymes, including hydrolases, oxidoreductases, lyases, transferases, ligases, and isomerases. Research related to cofactors (prosthetic groups, coenzymes, and metal ions) will also be of interest to this collection. It will be composed of a selection of exclusive papers from the Editorial Board Members (EBMs) of the Enzymology Section, as well as invited papers from relevant experts. We also welcome senior experts in the field to make contributions to this Special Issue. We aim to represent our section as an attractive open-access publishing platform for the enzymology research field.

Prof. Dr. Piero Crespo
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Biomolecules is an international peer-reviewed open access monthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • structure and function
  • enzyme catalysis
  • enzyme inhibition
  • enzyme mechanisms
  • computational enzymology
  • biophysical characterization
  • structure determination
  • drug action
  • biochemical mechanisms
  • molecular forces
  • allosterism
  • orthosterism

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Published Papers (1 paper)

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Research

17 pages, 4441 KiB  
Article
Functional Characterization of the SHIP1-Domains Regarding Their Contribution to Inositol 5-Phosphatase Activity
by Spike Murphy Müller, Nina Nelson and Manfred Jücker
Biomolecules 2025, 15(1), 105; https://doi.org/10.3390/biom15010105 - 10 Jan 2025
Viewed by 715
Abstract
The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is a multidomain protein consisting of two protein–protein interaction domains, the Src homology 2 (SH2) domain, and the proline-rich region (PRR), as well as three phosphoinositide-binding domains, the pleckstrin homology-like (PHL) domain, the 5-phosphatase [...] Read more.
The Src homology 2 domain-containing inositol 5-phosphatase 1 (SHIP1) is a multidomain protein consisting of two protein–protein interaction domains, the Src homology 2 (SH2) domain, and the proline-rich region (PRR), as well as three phosphoinositide-binding domains, the pleckstrin homology-like (PHL) domain, the 5-phosphatase (5PPase) domain, and the C2 domain. SHIP1 is commonly known for its involvement in the regulation of the PI3K/AKT signaling pathway by dephosphorylation of phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) at the D5 position of the inositol ring. However, the functional role of each domain of SHIP1 for the regulation of its enzymatic activity is not well understood. To determine the contribution of the individual domains to catalytic activity, the full-length protein was compared with truncated constructs lacking one or more domain(s), regarding the substrate turnover (kcat) and catalytic efficiency (kcat/Km) towards ci8-PtdIns(3,4,5)P3. With this approach, it was possible to verify the allosteric activation of SHIP1 mediated by the C2 domain as described previously, while the PHL domain seemed instead to have a negative effect regarding catalytic efficiency. The full-length SHIP1 clearly displayed the highest turnover and the second-highest catalytic efficiency, showing the role of the SH2 domain and PRR not only in protein–protein interactions but also in catalysis. The SH2 domain increased substrate turnover but negatively affected catalytic efficiency. The linker between the SH2 and the PHL domains decreased the turnover number but positively influenced the catalytic efficiency. The PRR increased both the substrate turnover and the protein’s catalytic efficiency. The regression analysis of the Michaelis–Menten graph revealed SHIP1 to be an allosteric enzyme, with the PRR and the linker being the most involved domains in that regard. In summary, our data indicate a complex regulation of the enzymatic activity of SHIP1 by its individual domains. While the C2 domain and PRR at the carboxy-terminus have a positive effect on enzymatic activity, the SH2 and PHL domain at the amino-terminus inhibit catalytic efficiency. Full article
(This article belongs to the Special Issue Feature Papers in Enzymology—2nd Edition)
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