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

ABSTRACT: 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 (EhHAPp49), exhibiting sequence similarity to histidine acid phosphatase (HAP)/phyt

SUBMITTER: Teran-Ramirez C 

PROVIDER: S-EPMC7926622 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature