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Tytuł pozycji:

Structure-Function Relationship Study of a Secretory Amoebic Phosphatase: A Computational-Experimental Approach.

Tytuł:
Structure-Function Relationship Study of a Secretory Amoebic Phosphatase: A Computational-Experimental Approach.
Autorzy:
Terán-Ramírez C; Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.
Mares-Alejandre RE; Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.
Estrada-González AL; Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.
Muñoz-Muñoz PLA; Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.
Ramos-Ibarra MA; Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.
Źródło:
International journal of molecular sciences [Int J Mol Sci] 2021 Feb 22; Vol. 22 (4). Date of Electronic Publication: 2021 Feb 22.
Typ publikacji:
Journal Article
Język:
English
Imprint Name(s):
Original Publication: Basel, Switzerland : MDPI, [2000-
MeSH Terms:
Structure-Activity Relationship*
Entamoeba histolytica/*enzymology
Phosphoric Monoester Hydrolases/*chemistry
Phosphoric Monoester Hydrolases/*metabolism
6-Phytase/metabolism ; Binding Sites ; Catalytic Domain ; Diphosphates/metabolism ; Entamoeba histolytica/genetics ; Humans ; Molecular Docking Simulation ; Phosphoric Monoester Hydrolases/genetics ; Protein Conformation ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Recombinant Proteins/genetics ; Recombinant Proteins/metabolism
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Grant Information:
CB-2010/01-155714 Consejo Nacional de Ciencia y Tecnología; CB-2019/01-170715 Consejo Nacional de Ciencia y Tecnología; CPI/300/2/N/112/1 Universidad Autónoma de Baja California
Contributed Indexing:
Keywords: Entamoeba histolytica; HAP/phytase-like phosphatase; homology-based modeling; recombinant protein production; structure–function characterization
Substance Nomenclature:
0 (Diphosphates)
0 (Protozoan Proteins)
0 (Recombinant Proteins)
EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
EC 3.1.3.26 (6-Phytase)
O352864B8Z (sodium pyrophosphate)
Entry Date(s):
Date Created: 20210306 Date Completed: 20210527 Latest Revision: 20210527
Update Code:
20240104
PubMed Central ID:
PMC7926622
DOI:
10.3390/ijms22042164
PMID:
33671604
Czasopismo naukowe
Phosphatases are hydrolytic enzymes that cleave the phosphoester bond of numerous substrates containing phosphorylated residues. The typical classification divides them into acid or alkaline depending on the pH at which they have optimal activity. The histidine phosphatase (HP) superfamily is a large group of functionally diverse enzymes characterized by having an active-site His residue that becomes phosphorylated during catalysis. HP enzymes are relevant biomolecules due to their current and potential application in medicine and biotechnology. Entamoeba histolytica , the causative agent of human amoebiasis, contains a gene ( EHI_146950 ) that encodes a putative secretory acid phosphatase ( Eh HAPp49), exhibiting sequence similarity to histidine acid phosphatase (HAP)/phytase enzymes, i.e., branch-2 of HP superfamily. To assess whether it has the potential as a biocatalyst in removing phosphate groups from natural substrates, we studied the Eh HAPp49 structural and functional features using a computational-experimental approach. Although the combined outcome of computational analyses confirmed its structural similarity with HP branch-2 proteins, the experimental results showed that the recombinant enzyme (r Eh HAPp49) has negligible HAP/phytase activity. Nonetheless, results from supplementary activity evaluations revealed that r Eh HAPp49 exhibits Mg 2+ -dependent alkaline pyrophosphatase activity. To our knowledge, this study represents the first computational-experimental characterization of Eh HAPp49, which offers further insights into the structure-function relationship and the basis for future research.

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