Structure reveals regulatory mechanisms of a MaoC-like hydratase from Phytophthora capsici involved in biosynthesis of polyhydroxyalkanoates (PHAs).

ABSTRACT:

Background

Polyhydroxyalkanoates (PHAs) have attracted increasing attention as "green plastic" due to their biodegradable, biocompatible, thermoplastic, and mechanical properties, and considerable research has been undertaken to develop low cost/high efficiency processes for the production of PHAs. MaoC-like hydratase (MaoC), which belongs to (R)-hydratase involved in linking the β-oxidation and the PHA biosynthetic pathways, has been identified recently. Understanding the regulatory mechanisms of (R)-hydratase catalysis is critical for efficient production of PHAs that promise synthesis an environment-friendly plastic.

Methodology/principal findings

We have determined the crystal structure of a new MaoC recognized from Phytophthora capsici. The crystal structure of the enzy

SUBMITTER: Wang H 

PROVIDER: S-EPMC3823801 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature