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In their analysis, Michaelis and Menten (and also Henri) assumed that the substrate is in instantaneous chemical equilibrium with the complex, which implies [13] [28] + = in which e is the concentration of free enzyme (not the total concentration) and x is the concentration of enzyme-substrate complex EA.
A biogeochemical cycle, or more generally a cycle of matter, [1] is the movement and transformation of chemical elements and compounds between living organisms, the atmosphere, and the Earth's crust. Major biogeochemical cycles include the carbon cycle, the nitrogen cycle and the water cycle. In each cycle, the chemical element or molecule is ...
The analysis of these reactions is much simpler if the concentration of substrate A is kept constant and substrate B varied. Under these conditions, the enzyme behaves just like a single-substrate enzyme and a plot of v by [S] gives apparent K M and V max constants for substrate B.
The most abundant ion in plant cells is the potassium ion. [2] Plants take up potassium for plant growth and function. A portion of potassium uptake in plants can be attributed to weathering of primary minerals, but plants can also ‘pump’ potassium from deeper soil layers to increase levels of surface K. [2] Potassium stored in plant matter can be returned to the soil during decomposition ...
Bioenergetics is a field in biochemistry and cell biology that concerns energy flow through living systems. [1] This is an active area of biological research that includes the study of the transformation of energy in living organisms and the study of thousands of different cellular processes such as cellular respiration and the many other metabolic and enzymatic processes that lead to ...
Kinetically perfect enzymes have a specificity constant, k cat /K m, on the order of 10 8 to 10 9 M −1 s −1.The rate of the enzyme-catalysed reaction is limited by diffusion and so the enzyme 'processes' the substrate well before it encounters another molecule.
PEPCK (EC 4.1.1.49) is one of three decarboxylation enzymes used in the inorganic carbon concentrating mechanisms of C 4 and CAM plants. The others are NADP-malic enzyme and NAD-malic enzyme . [ 17 ] [ 18 ] In C 4 carbon fixation, carbon dioxide is first fixed by combination with phosphoenolpyruvate to form oxaloacetate in the mesophyll .
Phosphoenolpyruvate carboxylase (also known as PEP carboxylase, PEPCase, or PEPC; EC 4.1.1.31, PDB ID: 3ZGE) is an enzyme in the family of carboxy-lyases found in plants and some bacteria that catalyzes the addition of bicarbonate (HCO 3 −) to phosphoenolpyruvate (PEP) to form the four-carbon compound oxaloacetate and inorganic phosphate: [1]