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![[Figure 2]](ag5030fig2mag.jpg)
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Figure 2
LC, UV and MS spectra for reactions catalyzed by Hmo and its mutants. (a) LC traces of enzymatic reactions with (S)-mandelate (1) as the substrate catalyzed by Hmo and its mutants: a, WT Hmo; b, Y128F mutant; c, R163L mutant; d, H252F mutant; e, R255A mutant; f, (S)-mandelate standard (1); g, benzoylformate standard (2). (b) Enzymatic reactions catalyzed by the Y128F mutant, where benzoate (3) is the major kinetic product over 420 min. (c) Mass spectra of methyl benzoate analyzed by GC-MS for enzymatic reactions conducted in the presence of H218O (left) and 18O2 (right). (d) Formation of hydrogen peroxide (H2O2) in enzymatic reactions catalyzed by WT Hmo and the Y128F mutant in the presence of (S)-mandelate (SMA) or 4-hydroxy-(S)-mandelate (4HSMA). (e) LC traces of enzymatic reactions catalyzed by the R163L mutant with α-(S)-mandelic amide as the substrate (i), in which the product is 2-oxo-2-phenylacetamide showing the same retention as the synthetic reference (ii). |
![[Figure 2]](ag5030fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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