Entamoeba histolytica Phosphoserine aminotransferase (EhPSAT): insights into the structure-function relationship.

ABSTRACT:

Background

Presence of phosphorylated Serine biosynthesis pathway upstream to the de novo cysteine biosynthesis pathway makes PSAT a crucial enzyme. Besides this, phoshoserine produced by the enzyme can also be taken up directly by cysteine synthase as a substrate. PSAT is a PLP dependent enzyme where the cofactor serves as an epicenter for functional catalysis with the active site architecture playing crucial role in optimum function of the enzyme.

Findings

EhPSAT is a homodimer of molecular mass 86 kDa. To understand the structural modulations associated with pH dependent changes in functional activity of EhPSAT detailed biophysical studies were carried out. pH alterations had no significant effect on the secondary structure, cofactor orientation and oligomeric configurati

SUBMITTER: Mishra V 

PROVIDER: S-EPMC2850911 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature