Results
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| Property | Organism | Value | Units | ID | Details |
|---|---|---|---|---|---|
| kcat of reactions associated with: | Unspecified | Central-CE (carbohydrate energy) metabolism 79 s^-1: secondary metabolism 2.5s^-1 | sec^-1 | 111415 | Bar-Even A. et al., The... |
| Median kcat of isomerases & ligases | Unspecified | isomerases 33.5s^-1: ligases 3.7s^-1 | sec^-1 | 111416 | Bar-Even A. et al., The... |
| Q10 values for the identified pairs of non-enzymatic and enzyme-catalyzed reactions | Microbes | Table - link | N/A | 112398 | Elias M, Wieczorek G... |
| Estimated origin of the enzyme lysozyme, encoded by the LYZ gene | Unspecified | 400 - 600 | million years ago | 112309 | Rubio CA. The Natural... |
| Km for NH4+ | Bacteria Escherichia coli | 100 glutamine synthetase (GS): 2,000 glutamate dehydrogenase (GDH) | µM | 106346 | Boogerd FC, Ma H, Bruggeman... |
| Enzyme activities relevant for autotrophic CO2 fixation and glyoxylate assimilation at 55°C | Bacteria Chloroflexus aurantiacus | Table - link | N/A | 106063 | Herter S. et al., Autotrophic... |
| Effects of Adenylate Mixtures on NAD-Malic Enzyme with limiting and saturating substrate and activator concentrations | C4 plants | Table - link | N/A | 103981 | Furbank RT, Agostino A... |
| Turnover rate of RNase E | Unspecified | 12 | Min^-1 | 108612 | Garrey SM et al., Substrate... |
| Kcat/Km of mitochondrial complex I for NADH oxidation by the flavin | Cow Bos Taurus | ~1e8 | M^-1×sec^-1 | 109179 | Hirst J. Mitochondrial... |
| Kcat for NADH oxidation by the flavin of mitochondrial complex I | Cow Bos Taurus | >15,000 | Sec^-1 | 109188 | Hirst J. Mitochondrial... |
| Typical enzymatic turnover rate in biosynthetic pathways | Various | 7 (× /27) | 1/sec | 105245 | Liebermeister W, Klipp... |
| Typical empirical substarate concentration in biosynthetic pathways | Various | 0.17 (× /20) | mM | 105246 | Liebermeister W, Klipp... |
| Estimated protein concentration in biosynthetic pathways | Budding yeast Saccharomyces cerevisiae | 36 (× /4.7) | nM | 105247 | Liebermeister W, Klipp... |
| Affinity (Km) at which acetyl-CoA synthetase (ACS) scavenges acetate | Bacteria Escherichia coli | 200 | μM | 109945 | Valgepea K, Adamberg K... |
| Difference between in vivo & in vitro measurements of kinetic parameters | Generic | ≤3 | orders of magnitude | 111410 | Bar-Even A. et al., The... |
| Median turnover number for the entire data set of enzymes and natural substrates | Generic | ~10 | sec^-1 | 111411 | Bar-Even A. et al., The... |
| Median kcat/KM number for the entire data set of enzymes and natural substrates | Generic | ~10^5 | M^-1×sec^-1 | 111412 | Bar-Even A. et al., The... |
| Median KM for the entire data set of enzymes and natural substrates | Generic | ~100 | µM | 111413 | Bar-Even A. et al., The... |
| Turnover number of purine ribonucleoside phosphorylase | Unspecified | 40 | sec^-1 | 111873 | Malinen AM et al., Active... |
| Ratio between pantothenate production and pantothenate phosphorylation | Bacteria Escherichia coli | 15 | times more pantothenate produced than phsophorylated | 114601 | Vallari DS, Jackowski... |