nolpyruvate carboxykinase which is involved in gluconeogenesis. This process s t
ID: 204681 • Letter: N
Question
nolpyruvate carboxykinase which is involved in gluconeogenesis. This process s the biological equivalent to the reverse of gycolysis, and has been n humans the PEPCK gene encodes phosphoen shown to be regulated by the glu documented case where a mutation caused glycine to be replaced by arginine ucocorticoid receptor and responds to cortisol (stress hormone) levels. It is critically important to regulating blood sugar levels. There has been at least one The following is a fragment of the PEPCK gene (template strand) and does not contain the start codon. 1. Transcribe and translate this provided sequence 2. Identify where the mutation occurs (underline, highlight or bold that letter) 3. Describe what kind of mutation this is. Be specific. 4. Explain what kind of impact you think this might have on the protein structure and onExplanation / Answer
1. Template strand: 5 / ATC CCT GAC GCA CTC AAC CTT CCA CCC GGG 3 /
Template strand: 3 / GGG CCC CCA CTT AAC CTC GCA GAC CCT ATC 5 / (as the template strand is read in the 3/ to 5/ direction).
mRNA sequence: 5 / CCC GGG GGU GAA UUG GAG CGU CUG GGA UAG 3 /
Peptide sequence: Pro Gly Gly Glu Leu Glu Arg Leu Gly Stop
2. CCC GGG GGU GAA UUG GAG CGU CUG GGA UAG
The three codons, GGG, GGU, GGA, coding for glycine can undergo point mutation (with the first G replaced with C) to generate the codons CGG, CGU, CGA that encodes for Arginine.
3. Since in this type of mutation, Glycine is substituted with Arginine hence this is an example of missense mutation.
4. Since this mutation results in substitution of a neutral non polar amino acid with that of a positively charged amino acid, this can lead to distortion of the structure of the enzyme as the positively charged R-group can easily form a salt bridge with any of the neighboring negatively charged amino acid, leading to distorted structure of the enzyme. If this peptide is a part of the active site of the enzyme then the enzyme may even fail to carry out the catalysis. the person harboring this mutation will fail to carry out gluconeogenesis and failure to maintain normal blood glucose levels during fasting state.
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