Results
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Property | Organism | Value | Units | ID | Details |
---|---|---|---|---|---|
Rate constants used in the simulation of the kinetics of nitrogenase at 23° pH 7.4 | Bacteria Klebsiella pneumoniae | Table - link | N/A | 111320 | Orme-Johnson WH. Molecular... |
Kinetics of glucoamylase production in batch and continuous cultures | Budding yeast Saccharomyces cerevisiae | Table - link | N/A | 107565 | Kilonzo PM, Margaritis A... |
Kinetics of blood cell turnover under steady state conditions | Human Homo sapiens | total blood cell production rate ~490E9 Figure link | cells/day | 113413 | Fliedner TM, Graessle D... |
Thermodynamics of Enzyme-Catalyzed Reactions | Generic | Database - link | N/A | 103383 | http://xpdb.nist.gov... |
Enzyme concentration in mitochondrial matrix | Unspecified | 270-560 | mg protein/ml | 108992 | Partikian, A., B. Olveczky... |
Enzyme concentration in mitochondrial matrix | Pigeon Columba livia | 27 | % | 108994 | Srere, P.A. 1980. The... |
Enzyme Activities in human erythrocytes | Human Homo sapiens | Table - link | N/A | 101863 | See table for refere... |
Kinetics of phosphorylation of ADAP peptide (645-661) by various protein kinases | Mammals | Table - link | N/A | 110569 | Gandy S, Czernik AJ,... |
Michaelis–Menten constant (Km) of proteorhodopsin | Bacteria Escherichia coli | 1000 | photons/sec/nm^2 | 111064 | Walter JM, Greenfield D... |
Bimolecular rate constants for formation of successively more constrained protein-protein complexed states N | Generic | Table - link | M^-1×sec^-1 | 112542 | Northrup SH, Erickson... |
Protein-protein bond formation bimolecular rate constant | Generic | ~10^6 (0.5×10^6 - 5.0×10^6) | M^-1×sec^-1 | 112534 | Northrup SH, Erickson... |
Protein-protein association bimolecular rate constant predicted by Brownian simulation | Generic | 2e+6 | M^-1×sec^-1 | 112535 | Northrup SH, Erickson... |
Rate constant of polymerization of ATP actin onto the barbed end of an actin filament | Generic | 2×10^6 - 8×10^6 | M^-1×sec^-1 | 112536 | Northrup SH, Erickson... |
Rate constant of association of hemoglobin dimers to form tetramers | Unspecified | 0.4×10^6 - 0.6×10^6 | M^-1×sec^-1 | 112537 | Northrup SH, Erickson... |
Rate constant for polyclonal antibodies binding to hemoglobin and cytochrome c | Rabbit | 0.6×10^6 - 1.0×10^6 | M^-1×sec^-1 | 112538 | Northrup SH, Erickson... |
Rate constant for insulin dimerization | Pig Sus species | 1e+8 | M^-1×sec^-1 | 112540 | Northrup SH, Erickson... |
Rate constant for interaction of cytochrome c with cytochrome c peroxidase and with cytochrome b5 | Various | 10^7 - 10^9 | M^-1×sec^-1 | 112541 | Northrup SH, Erickson... |
Difference between catalyzed and uncatalysed reaction in which OMP decarboxylase turns its substrate over | Budding yeast Saccharomyces cerevisiae | 20 | order of magnitudes faster | 113581 | Miller BG, Wolfenden... |
Kinetics of GlpF and AqpZ, the glycerol and water channels | Bacteria Escherichia coli | Table - link | N/A | 103800 | Borgnia MJ, Agre P. ... |
BRENDA - a database of enzyme properties | Generic | Database - link | N/A | 100598 | Schomburg I, Chang A... |