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

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 Lett

journal_title

FEBS letters

authors

Nambu Y,Ishii-Hyakutake M,Harada K,Mizuno S,Tsuge T

doi

10.1002/1873-3468.13651

subject

Has Abstract

pub_date

2020-02-01 00:00:00

pages

710-716

issue

4

eissn

0014-5793

issn

1873-3468

journal_volume

594

pub_type

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