Cumulative Effect of Amino Acid Replacements Results in Enhanced Thermostability of Potato Type L α-Glucan Phosphorylase

The thermostability of potato type L α-glucan phosphorylase (EC 2.4.1.1) was enhanced by random and site-directed mutagenesis. We obtained three single-residue mutations—Phe39→Leu (F39L), Asn135→Ser (N135S), and Thr706→Ile (T706I)—by random mutagenesis. Although the wild-type enzyme was completely i...

Celý popis

Uloženo v:
Podrobná bibliografie
Hlavní autoři: Yanase, Michiyo, Takata, Hiroki, Fujii, Kazutoshi, Takaha, Takeshi, Kuriki, Takashi
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology 2005
Témata:
Enzymology and Protein Engineering
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC1214682/
https://ncbi.nlm.nih.gov/pubmed/16151135
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/AEM.71.9.5433-5439.2005
Tagy: Přidat tag
Žádné tagy, Buďte první, kdo otaguje tento záznam!

Podobné jednotky