Characterization and expression patterns of a membrane-bound trehalase from Spodoptera exigua.

ABSTRACT:

Background

The chitin biosynthesis pathway starts with trehalose in insects and the main functions of trehalases are hydrolysis of trehalose to glucose. Although insects possess two types, soluble trehalase (Tre-1) and membrane-bound trehalase (Tre-2), very little is known about Tre-2 and the difference in function between Tre-1 and Tre-2.

Results

To gain an insight into trehalase functions in insects, we investigated a putative membrane-bound trehalase from Spodoptera exigua (SeTre-2) cloned from the fat body. The deduced amino acid sequence of SeTre-2 contains 645 residues and has a predicted molecular weight of approximately 74 kDa and pI of 6.01. Alignment of SeTre-2 with other insect trehalases showed that it contains two trehalase signature motifs and a putative transm

SUBMITTER: Tang B 

PROVIDER: S-EPMC2424068 | biostudies-literature | 2008 May

REPOSITORIES: biostudies-literature