Abstract:
: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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Nambu Y,Ishii-Hyakutake M,Harada K,Mizuno S,Tsuge Tdoi
10.1002/1873-3468.13651subject
Has Abstractpub_date
2020-02-01 00:00:00pages
710-716issue
4eissn
0014-5793issn
1873-3468journal_volume
594pub_type
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