Structural elements to convert Escherichia coli alpha-xylosidase (YicI) into alpha-glucosidase

FEBS Letters
Masayuki OkuyamaAtsuo Kimura

Abstract

Escherichia coli YicI, a member of glycoside hydrolase family (GH) 31, is an alpha-xylosidase, although its amino-acid sequence displays approximately 30% identity with alpha-glucosidases. By comparing the amino-acid sequence of GH 31 enzymes and through structural comparison of the (beta/alpha)(8) barrels of GH 27 and GH 31 enzymes, the amino acids Phe277, Cys307, Phe308, Trp345, Lys414, and beta-->alpha loop 1 of (beta/alpha)(8) barrel of YicI have been identified as elements that might be important for YicI substrate specificity. In attempt to convert YicI into an alpha-glucosidase these elements have been targeted by site-directed mutagenesis. Two mutated YicI, short loop1-enzyme and C307I/F308D, showed higher alpha-glucosidase activity than wild-type YicI. C307I/F308D, which lost alpha-xylosidase activity, was converted into alpha-glucosidase.

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Citations

Dec 8, 2011·Bioscience, Biotechnology, and Biochemistry·Masayuki Okuyama
Apr 15, 2016·Journal of Bioscience and Bioengineering·Tomohiko MatsuzawaKatsuro Yaoi
Aug 2, 2013·The Journal of Biological Chemistry·Henriëtte J RozeboomBauke W Dijkstra
Sep 4, 2015·The Journal of Biological Chemistry·Yuka OkazawaTakashi Tonozuka
Jan 1, 2022·Applied Microbiology and Biotechnology·Tomohiko MatsuzawaKatsuro Yaoi

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