It is vitamin B, vitamin D, vitamin A, vitamin E, and vitamin K
The answer is lag. The number of bacterial cells doubles at a constant, exponential rate during log phase, while growth rate and death rate are the same during stationary phase. The fourth phase is the death phase, when the rate of cell death is faster than the population growth.
Answer: herbivore, eukaryote, primary consumer
Explanation:
The red squirrel can be described by the following features.
1. Herbivore: A herbivore is an animal which is dependent upon the plant and their products for it's food requirement. Here, the red squirrel is the herbivore because it is dependent upon the spruce tree seeds for their food requirement.
2. Eukaryote: A eukaryotic organism is the one which has well define nucleus and encloses the genetic material in the nucleus. The red squirrel is a complex eukaryotic organism.
3. Primary consumer: In a food chain a primary consumer is an organism which is dependent upon plants and their food products for energy and food needs. The red squirrel is the primary consumer this is because of the fact that it consumes on the seeds of the spruce trees.
This would be the organ. The order of all would be organelle, cell, tissue, organ, organ system, organism.
Answer:
a) The response indicates that a pH below or above this range will most likely cause enolase to denature/change its shape and be less efficient or unable to catalyze the reaction.
b)The response indicates that the appropriate negative control is to measure the reaction rate (at the varying substrate concentrations) without any enzyme present.
c)The response indicated that the enolase has a more stable/functional/correct/normal protein structure at the higher temperature of 55°C than at 37°C because the enzyme is from an organism that is adapted to growth at 55°C.
Explanation:
Enolase catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during both glycolysis and gluconeogenesis.In bacteria, enolases are highly conserved enzymes and commonly exist as homodimers.
The temperature optimum for enolase catalysis was 80°C, close to the measured thermal stability of the protein which was determined to be 75°C, while the pH optimum for enzyme activity was 6.5. The specific activities of purified enolase determined at 25 and 80°C were 147 and 300 U mg−1 of protein, respectively. Km values for the 2-phosphoglycerate/phosphoenolpyruvate reaction determined at 25 and 80°C were 0.16 and 0.03 mM, respectively. The Km values for Mg2+ binding at these temperatures were 2.5 and 1.9 mM, respectively.
Enolase-1 from Chloroflexus aurantiacus (EnoCa), a thermophilic green non-sulfur bacterium that grows photosynthetically under anaerobic conditions. The biochemical and structural properties of enolase from C. aurantiacus are consistent with this being thermally adapted.
