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laiz [17]
3 years ago
5

Bipedalism in humans, when compared to knuckle walking in the African apes, represents what type of process or trait?

Biology
1 answer:
Ilia_Sergeevich [38]3 years ago
4 0

Answer: A. ancestral trait

Explanation:

Bipedalism can be define as a form of terrestrial locomotion, in which the organism moves with the help of two rear limbs or legs. Typical bipedal movements includes the hoping, running and walking. The evolution of the human bipedalism occurred in primates in about 4 million years ago with Sahelanthropus (oldest human ancestors or African Apes). The human ancestor Sahelanthropus led to the morphological alterations in the human skeleton including changes in the bones such as size of the bones of the foot, knee size, shape and orientation of the vertebral column, and leg length. All these changes contributed to the bipedalism.

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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.

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