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Article

Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site.

Protein science : a publication of the Protein Society - 1 Feb 2004

Kanai Ryuta, Haga Keiko, Akiba Toshihiko, Yamane Kunio, Harata Kazuaki

Abstract excerpt

Cyclodextrin glycosyltransferase (CGTase) belonging to the alpha-amylase family mainly catalyzes transglycosylation and produces cyclodextrins from starch and related alpha-1,4-glucans. The catalytic site of CGTase specifically conserves four aromatic residues, Phe183, Tyr195, Phe259, and Phe283, which are not found in alpha-amylase. To elucidate the structural role of Phe283, we determined the crystal structures...

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Identifiers

PMID: 14739329
DOI: 10.1110/ps.03408504
PMCID: PMC2286706

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Source receipt: pubmed, retrieved 7 Sept 2026.

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