Expanded amino acid sequence of the PhaC box in the active center of polyhydroxyalkanoate synthases

FEBS Letters

article

Yuka Nambu¹  Manami Ishii-Hyakutake¹  Ken Harada¹  Shoji Mizuno¹  Takeharu Tsuge¹ 

[1] Department of Materials Science and Engineering, School of Materials and Chemical Technology, Tokyo Institute of Technology;Bioplastic Research Team, RIKEN Center for Sustainable Resource Science

关键词: lipase box;    motif;    PHA synthase;    polyhydroxyalkanoate;   

DOI  :  10.1002/1873-3468.13651

来源: John Wiley & Sons Ltd.

【 摘 要 】

Polyhydroxyalkanoate (PHA) synthases catalyze the polymerization reaction of the acyl moiety of hydroxyacyl-coenzyme A into polyester. The catalytic subunit PhaC of PHA synthase has the PhaC box sequence at the active site that is typically described as G-X-C-X-G-G (X is an arbitrary amino acid), and cysteine is an active center. In this study, an amino acid replacement was introduced into the PhaC box of the PHA synthase derived from Ralstonia eutropha (PhaCRe) to investigate the importance of highly conserved residues in polymerizing activity. Point mutagenesis revealed that PhaCRe mutants with the expanded PhaC box sequence ([GAST]-X-C-X-[GASV]- [GA]) are functional PHA synthases. These findings highlight the low mutational robustness of the last glycine residue in the PhaC box as well as that of the active center cysteine.

【 授权许可】

Unknown