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Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH 5.0 pH 7.0 pH 9.5 pH 10.5 1HH N M NM NMN M What amino acid was altered in the normal peptide and what amino acid replaced it on the mutant peptide?

Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH 5.0 pH 7.0 pH 9.5 pH 10.5 1HH N M NM NMN M What amino acid was altered in the normal peptide and what amino acid replaced it on the mutant peptide?

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH 5.0 pH 7.0 pH 9.5 pH 10.5 14.4 HH HH N M NM N M NM What amino acid was altered in the normal peptide and what amino acid replaced it on the mutant peptide?
Transcribed Image Text:Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH 5.0 pH 7.0 pH 9.5 pH 10.5 14.4 HH HH N M NM N M NM What amino acid was altered in the normal peptide and what amino acid replaced it on the mutant peptide?
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