Bacterial and algal orthologs of prostaglandin H2synthase: novel insights into the evolution of an integral membrane protein.
Biochim Biophys Acta
; 1848(1 Pt A): 83-94, 2015 Jan.
Article
em En
| MEDLINE
| ID: mdl-25281773
ABSTRACT
Prostaglandin H2synthase (PGHS; EC 1.14.99.1), a bi-functional heme enzyme that contains cyclooxygenase and peroxidase activities, plays a central role in the inflammatory response, pain, and blood clotting in higher eukaryotes. In this review, we discuss the progenitors of the mammalian enzyme by using modern bioinformatics and homology modeling to draw comparisons between this well-studied system and its orthologs from algae and bacterial sources. A clade of bacterial and algal orthologs is described that have salient structural features distinct from eukaryotic counterparts, including the lack of a dimerization and EGF-like domains, the absence of gene duplicates, and minimal membrane-binding domains. The functional implications of shared and variant features are discussed.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Bactérias
/
Prostaglandina-Endoperóxido Sintases
/
Proteínas de Algas
/
Proteínas de Membrana
Limite:
Animals
/
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article