𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Combination of N149S and D171G mutations in Aeromonas caviae polyhydroxyalkanoate synthase and impact on polyhydroxyalkanoate biosynthesis

✍ Scribed by Takeharu Tsuge; Shinko Watanabe; Daisuke Shimada; Hideki Abe; Yoshiharu Doi; Seiichi Taguchi


Book ID
109329983
Publisher
John Wiley and Sons
Year
2007
Tongue
English
Weight
109 KB
Volume
277
Category
Article
ISSN
0378-1097

No coin nor oath required. For personal study only.


πŸ“œ SIMILAR VOLUMES


Variation in Copolymer Composition and M
✍ Takeharu Tsuge; Shinko Watanabe; Shun Sato; Tomohiro Hiraishi; Hideki Abe; Yoshi πŸ“‚ Article πŸ“… 2007 πŸ› John Wiley and Sons 🌐 English βš– 175 KB

## Abstract Amino acid substitutions at two residues downstream from the active‐site histidine of polyhydroxyalkanoate (PHA) synthases are effective for changing the composition and the molecular weight of PHA. In this study, saturation mutagenesis at the position Ala505 was applied to PHA synthase

Mutation Effects of a Conserved Alanine
✍ Takeharu Tsuge; Yu Saito; Masaharu Narike; Koho Muneta; Yahaya M. Normi; Yoshihi πŸ“‚ Article πŸ“… 2004 πŸ› John Wiley and Sons 🌐 English βš– 256 KB

## Abstract Summary: 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 mutagenesi