Exploring the Biocatalytic Scope of Alditol Oxidase from Streptomyces coelicolor

van Hellemond, EW; Vermote, L; Koolen, W; Sonke, T; Zandvoort, E; Heuts, DPHM; Janssen, DB; Fraaije, MW

HERO ID

4415013

Reference Type

Journal Article

Year

2009

HERO ID 4415013
In Press No
Year 2009
Title Exploring the Biocatalytic Scope of Alditol Oxidase from Streptomyces coelicolor
Authors van Hellemond, EW; Vermote, L; Koolen, W; Sonke, T; Zandvoort, E; Heuts, DPHM; Janssen, DB; Fraaije, MW
Journal Advanced Synthesis & Catalysis
Volume 351
Issue 10
Page Numbers 1523-1530
Abstract The substrate scope of the flavoprotein alditol oxidase (AldO) from Streptomyces coelicolor A3(2), recombinantly produced in Escherichia coli, was explored. While it has been established that AldO efficiently oxidizes alditols to D-aldoses. this study revealed that the enzyme is also active with a broad range of aliphatic and aromatic alcohols. Alcohols containing hydroxy groups at the C-1 and C-2 positions like 1,2,4-butanetriol (K(m) =170 mM, k(cat) = 4.4 s(-1)), 1,2-pentanediol (K(m) = 52 mM, k(cat) = 0.85 s(-1)) and 1,2-hexanediol (K(m) = 97 mM, k(cat) = 2.0 s(-1)) were readily accepted by AIM Furthermore, the enzyme was highly enantioselective for the oxidation of 1,2-diols [e.g.. for 1-phenyl-1,2-ethanediol the (R)-enantiomer was preferred with all E-value of 74]. For several diols the oxidation products were determined by GC-MS and NMR. Interestingly. for all tested 1,2-diols the products were found to be the alpha-hydroxy acids instead of the expected alpha-hydroxy aldehydes. Incubation of (R)-1-phenyl-1,2-ethanediol with (18)O-labelled water (H(2)(18)O) revealed that a second enzymatic oxidation step occurs via the hydrate product intermediate. The relaxed Substrate specificity. excellent enantioselectivity, and independence of coenzymes make AldO an attractive enzyme for the preparation of optically pure 1,2-diols and alpha-hydroxy acids.
Doi 10.1002/adsc.200900176
Wosid WOS:000268200500010
Is Certified Translation No
Dupe Override No
Is Public Yes
Keyword alcohol oxidation; alditol oxidase; biocatalysis; 1,2-diols; alpha-hydroxy acids
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