Table 4.
Km(O2) values for various O2-consuming enzymes.
| Enzyme | Product | Km(O2) (%) | Details | Reference |
|---|---|---|---|---|
| Nox2 | O2− | 3.5 | [77] | |
| Nox2 | O2− | 3.1 | [78] | |
| Nox2 | O2− | 2-3 | [19] | |
| Nox2 | O2− | 2-3 | [79] | |
| Nox4 | H2O2 | 18 | [78] | |
| Nox4 | H2O2 | 18 | [19] | |
| Nox4 | H2O2 | 16–20 | [79] | |
| nNOS | NO | 2.3 | Purified bovine enzyme | [45] |
| nNOS | NO/O2− | 2.2 | Partially uncoupled rat enzyme | [42, 43] |
| O2− | 3.4 | Fully uncoupled rat enzyme | ||
| nNOS | NO | 15.7 | Purified rat enzyme | [47] |
| nNOS | NO | 39.8 | Purified rat enzyme | [80] |
| nNOS | NO | 28.5 | Kinetic model based on rat enzyme data | [81, 82] |
| eNOS | NO | 0.8 | Purified bovine enzyme | [45] |
| eNOS | NO | 0.3 | Kinetic model based on rat enzyme data | [82, 83] |
| iNOS | NO | 0.63 ± 0.09 | Purified bovine enzyme | [45] |
| iNOS | NO | 11.0 | Isolated enzyme assay | [84] |
| iNOS | NO | 10.6 | Kinetic model | [82] |
| NOS | NO | 3.1–10.8 | Unspecified isoform | [48, 85] |
| XO | O2·−/H2O2 | 2.2–6.8 | Isolated from bovine milk | Fridovich et al. 1962, 1964 |
| MAO | H2O2 | 3.4–28 | Mammalian enzymes; various substrates | [86–88]; reviewed in [57] |
| HO | CO, iron, and bilirubin | <1.5 | Unspecified isoform from chicken liver | [59] |
| LOX | H2O2 | 1–2.6 | Unspecified isoform | [65] |
| COX-1 | Various | 0.4–3.1 | Arachidonic acid substrate | [63, 89–91] |
| COX-2 | Various | 1.3–1.5 | Arachidonic acid substrate | [63, 65] |
| PHD | Modified HIF | 41–46 | Various substrates | [92] |
| FIH | Modified HIF | 4–12 | Various substrates | [92] |
Nox: NADPH oxidase; NOS: nitric oxide synthase; XO: xanthine oxidase; MAO: monoamine oxidase; HO: heme oxygenase; LOX: lipoxygenase; COX: cyclooxygenase; PHD: prolyl hydroxylase; FIH: factor inhibiting HIF-1.