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Column flow reactor using acetohydroxyacid synthase I from Escherichia coli as catalyst in continuous synthesis of R-phenylacetyl carbinol.
- Published in:
- Biotechnology & Bioengineering, 2005, v. 89, n. 6, p. 733, doi. 10.1002/bit.20392
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- Article
Substrate range of acetohydroxy acid synthase I from Escherichia coli in the stereoselective synthesis of α-hydroxy ketones.
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- Biotechnology & Bioengineering, 2004, v. 88, n. 7, p. 825, doi. 10.1002/bit.20275
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- Article
AN HERBICIDE (SULFOMETURON METHYL) RESISTANT MUTANT IN <em>PROPHYRIDIUM</em> (RHODOPHYTA).
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- Journal of Phycology, 1989, v. 25, n. 1, p. 108, doi. 10.1111/j.0022-3646.1989.00108.x
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- Article
Reaction mechanisms of thiamin diphosphate enzymes: new insights into the role of a conserved glutamate residue.
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- FEBS Journal, 2009, v. 276, n. 9, p. 2447, doi. 10.1111/j.1742-4658.2009.06965.x
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- Article
Acetohydroxyacid synthase: A new enzyme for chiral synthesis of R-phenylacetylcarbinol.
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- Biotechnology & Bioengineering, 2003, v. 83, n. 7, p. 833, doi. 10.1002/bit.10728
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- Article
Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes.
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- Nature Chemical Biology, 2008, v. 4, n. 2, p. 113, doi. 10.1038/nchembio.62
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- Article
Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I.
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- FEBS Journal, 2012, v. 279, n. 11, p. 1967, doi. 10.1111/j.1742-4658.2012.08577.x
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- Article