Cargando…

A COMPARATIVE ANALYSIS OF THREE CLASSES OF BACTERIAL NON-SPECIFIC ACID PHOSPHATASES AND ARCHAEAL PHOSPHOESTERASES: EVOLUTIONARY PERSPECTIVE

INTRODUCTION: Bacterial nonspecific acid phosphohydrolases (NSAPs) or phosphatases are group of enzymes secreted as soluble periplasmic proteins or retained as membrane bound lipoproteins that are usually able to dephosphorylate a broad array of structurally unrelated organic phosphoesters (nucleoti...

Descripción completa

Detalles Bibliográficos
Autores principales: U. Gandhi, Neha, B. Chandra, Sathees
Formato: Online Artículo Texto
Lenguaje:English
Publicado: AVICENA, d.o.o., Sarajevo 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3508851/
https://www.ncbi.nlm.nih.gov/pubmed/23322973
http://dx.doi.org/10.5455/aim.2012.20.167-173
Descripción
Sumario:INTRODUCTION: Bacterial nonspecific acid phosphohydrolases (NSAPs) or phosphatases are group of enzymes secreted as soluble periplasmic proteins or retained as membrane bound lipoproteins that are usually able to dephosphorylate a broad array of structurally unrelated organic phosphoesters (nucleotides, sugar phosphates, phytic acid etc.) to acquire inorganic phosphate (Pi) and organic byproducts. They exhibit optimal catalytic activity at acidic to neutral pH values. On the basis of amino acid sequence relatedness, phosphatase are grouped into different molecular families namely Class A, Class B and Class C acid phosphatase respectively. RESULTS AND DISCUSSION: In this article out of thirty three sequences, twenty six belonging to each of the three classes of bacterial acid phosphatase and seven belonging to archaeal phosphoesterases were analyzed using various tools of bioinformatics. Phylogenetic analysis, dot plot comparisons and motif analysis were done to identify a number of similarities and differences between three classes of bacterial acid phosphatases and archaeal phosphoesterases. In this research we have attempted to decipher evolutionary relationship between three classes of bacterial acid phosphatase and archaeal phosphoesterases using bioinformatics approach.