BIOCHEMISTRY Correction for “Evolutionary alteration of ALOX15 specificity optimizes the biosynthesis of antiinflammatory and proresolving lipoxins,” by Susan Adel, Felix Karst, Àngels González-Lafont, Mária Pekárová, Patricia Saura, Laura Masgrau, José M. Lluch, Sabine Stehling, Thomas Horn, Hartmut Kuhn, and Dagmar Heydeck, which appeared in issue 30, July 26, 2016, of Proc Natl Acad Sci USA (113:E4266–E4275; first published July 13, 2016; 10.1073/pnas.1604029113).
The authors note that Table 5 appeared incorrectly. The corrected table appears below.
Table 5.
Relative lipoxin synthase activity of mammalian ALOX15 orthologs
| Species | Relative lipoxin synthase activity, % | ||
| 15-/12-ratio | 5-HETE as substrate | 5,6-DiHETE as substrate | |
| 15-lipoxygenating | |||
| Human | 8.1 | 100.0 | 100 |
| Chimpanzee | 8.1 | 118.0 | 145.8 |
| Orangutan | 8.1 | 172.2 | 105.6 |
| Rabbit | 24.0 | 39.5 | 108.6 |
| ratL353F | 13.3 | 197.3 | 262.5 |
| Mean ± SD | 12.3 ± 6.9 | 125.4 ± 62.1* | 144.5 ± 68.4† |
| 12-lipoxygenating | |||
| Macaca | 0.01 | 25.7 | 19.9 |
| Mouse | 0.03 | 36.1 | 1.5 |
| Rat | 0.26 | 8.4 | 0.0 |
| Pig | 0.04 | 35.4 | 61.1 |
| humI418A | 0.11 | 29.2 | 2.1 |
| Mean ± SD | 0.09 ± 0.10 | 27.0 ± 11.2* | 17.1 ± 25.9† |
The relative lipoxin synthase activity of the ALOX15 orthologs was quantified as described in Materials and Methods. For 5S-HETE oxygenation, lipoxin A and lipoxin B isomers were quantified. During 5S,6(S/R)-DiHETE, only lipoxin A isomers were formed.
P = 0.008 by Student’s t test.
P = 0.005 by Student’s t test.
The authors also note that on page E4266, in line 20 of the Abstract, “ratPhe353Ala” should instead appear as “ratLeu353Phe;” and that on page E4270, right column, first full paragraph, line 12, “ratPhe353Leu” should instead appear as “ratLeu353Phe.” These errors do not affect the conclusions of the article.