Erratum to: Two O-methyltransferases involved in the biosynthesis of methoxypyrazines: grape-derived aroma compounds important to wine flavour

Erratum to: Two O-methyltransferases involved in the biosynthesis of methoxypyrazines:... Plant Mol Biol (2013) 81:523 DOI 10.1007/s11103-013-0012-9 ERRATUM Erratum to: Two O-methyltransferases involved in the biosynthesis of methoxypyrazines: grape-derived aroma compounds important to wine flavour • • • Jake D. Dunlevy Kathleen L. Soole Michael V. Perkins • • • Eric G. Dennis Robert A. Keyzers Curtis M. Kalua Paul K. Boss Published online: 8 February 2013 Springer Science+Business Media Dordrecht 2013 Table 1 Kinetic parameters of recombinant VvOMT1 and VvOMT2 Erratum to: Plant Mol Biol (2010) 74:77–89 using HPs as substrates DOI 10.1007/s11103-010-9655-y -1 Enzyme Substrate Apparent k (s ) k /K cat cat m -1 -1 K (lM) (M s ) Due to an unfortunate turn of events, an incorrect version m of Table 1 has been used in the above mentioned publi- VvOMT1 IBHP 539 (31) 0.71 (0.03) 1,317 (62) cation. The k and k /K values in the original publi- cat cat m IPHP 493 (28) 0.36 (0.02) 730 (31) cation were found to be incorrectly calculated, and these VvOMT2 IBHP 628 (29) 0.09 (0.002) 137 (3) have been corrected in the following table. The original IPHP 1,264 (120) 0.19 (0.01) 150 (10) values would have implied that the enzyme is inactive Standard error values are given in parentheses against the hydroxypyrazine substrates. The corrected table shows that the VvOMT1 and VvOMT2 enzymes have k cat values, when hydroxypyrazines are used as substrates, that suggest catalytic production of methoxypyrazines by these enzymes is possible. The online version of the original article can be found under doi:10.1007/s11103-010-9655-y. J. D. Dunlevy  K. L. Soole School of Biological Science, Flinders University of South Australia, GPO Box 2100, Adelaide, SA 5001, Australia M. V. Perkins  E. G. Dennis School of Chemistry, Physics and Earth Sciences, Flinders University of South Australia, GPO Box 2100, Adelaide, SA 5001, Australia R. A. Keyzers  C. M. Kalua  P. K. Boss (&) CSIRO Plant Industry and Food Futures Flagship, PO Box 350, Glen Osmond, SA 5064, Australia e-mail: paul.boss@csiro.au http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Plant Molecular Biology Springer Journals

Erratum to: Two O-methyltransferases involved in the biosynthesis of methoxypyrazines: grape-derived aroma compounds important to wine flavour

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Publisher
Springer Netherlands
Copyright
Copyright © 2013 by Springer Science+Business Media Dordrecht
Subject
Life Sciences; Plant Sciences; Biochemistry, general; Plant Pathology
ISSN
0167-4412
eISSN
1573-5028
D.O.I.
10.1007/s11103-013-0012-9
Publisher site
See Article on Publisher Site

Abstract

Plant Mol Biol (2013) 81:523 DOI 10.1007/s11103-013-0012-9 ERRATUM Erratum to: Two O-methyltransferases involved in the biosynthesis of methoxypyrazines: grape-derived aroma compounds important to wine flavour • • • Jake D. Dunlevy Kathleen L. Soole Michael V. Perkins • • • Eric G. Dennis Robert A. Keyzers Curtis M. Kalua Paul K. Boss Published online: 8 February 2013 Springer Science+Business Media Dordrecht 2013 Table 1 Kinetic parameters of recombinant VvOMT1 and VvOMT2 Erratum to: Plant Mol Biol (2010) 74:77–89 using HPs as substrates DOI 10.1007/s11103-010-9655-y -1 Enzyme Substrate Apparent k (s ) k /K cat cat m -1 -1 K (lM) (M s ) Due to an unfortunate turn of events, an incorrect version m of Table 1 has been used in the above mentioned publi- VvOMT1 IBHP 539 (31) 0.71 (0.03) 1,317 (62) cation. The k and k /K values in the original publi- cat cat m IPHP 493 (28) 0.36 (0.02) 730 (31) cation were found to be incorrectly calculated, and these VvOMT2 IBHP 628 (29) 0.09 (0.002) 137 (3) have been corrected in the following table. The original IPHP 1,264 (120) 0.19 (0.01) 150 (10) values would have implied that the enzyme is inactive Standard error values are given in parentheses against the hydroxypyrazine substrates. The corrected table shows that the VvOMT1 and VvOMT2 enzymes have k cat values, when hydroxypyrazines are used as substrates, that suggest catalytic production of methoxypyrazines by these enzymes is possible. The online version of the original article can be found under doi:10.1007/s11103-010-9655-y. J. D. Dunlevy  K. L. Soole School of Biological Science, Flinders University of South Australia, GPO Box 2100, Adelaide, SA 5001, Australia M. V. Perkins  E. G. Dennis School of Chemistry, Physics and Earth Sciences, Flinders University of South Australia, GPO Box 2100, Adelaide, SA 5001, Australia R. A. Keyzers  C. M. Kalua  P. K. Boss (&) CSIRO Plant Industry and Food Futures Flagship, PO Box 350, Glen Osmond, SA 5064, Australia e-mail: paul.boss@csiro.au

Journal

Plant Molecular BiologySpringer Journals

Published: Feb 8, 2013

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