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Article

Mutation effects of a conserved alanine (Ala510) in type I polyhydroxyalkanoate synthase from Ralstonia eutropha on polyester biosynthesis.

Macromolecular bioscience - 20 Oct 2004

Tsuge Takeharu, Saito Yu, Narike Masaharu, Muneta Koho, Normi Yahaya M, Kikkawa Yoshihiro, Hiraishi Tomohiro, Doi Yoshiharu

Abstract excerpt

Type I polyhydroxyalkanoate (PHA) synthases, as represented by Ralstonia eutropha enzyme (PhaC(Re)), have narrow substrate specificity toward (R)-3-hydroxyacyl-coenzyme A with acyl chain length of C3-C5 to yield PHA polyesters. In this study, saturation point mutagenesis of a highly conserved alanine at position 510 (A510) in PhaC(Re) was carried out to investigate the effects on the polymerization activity and...

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Identifiers

PMID: 15508175
DOI: 10.1002/mabi.200400075

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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