Why was it necessary to use phosphoaminophosphonic acid-adenylate ester (ANP) in the ATP synthase enzyme active site rather than ATP to resolve the molecular structure of the ATP synthase active site by x-ray crystallography? C ANP - Mg²+ E193 T164 E189 31 K ANP has a S-S bond in the purine ring of the nucleotide to aid in crystallography. ANP is nonhydrolyzable and will trap the enzyme in the desired conformation. ATP cannot be used in a cell free system because it will be readily hydrolyzed. ATP is twice as large as ANP and will not fit in the ATP synthase active site. ANP is hydrophobic and ATP is hydrophilic, which makes ANP a better reactant.

Biochemistry
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Chapter1: Biochemistry: An Evolving Science
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Why was it necessary to use
phosphoaminophosphonic
acid-adenylate ester (ANP) in
the ATP synthase enzyme active site rather than ATP to resolve the molecular
structure of the ATP synthase active site by x-ray crystallography?
ANP
Mg²+
E193
T164
E189
31
ANP has a S-S bond in the purine ring of the nucleotide to aid in crystallography.
ANP is nonhydrolyzable and will trap the enzyme in the desired conformation.
ATP cannot be used in a cell free system because it will be readily hydrolyzed.
ATP is twice as large as ANP and will not fit in the ATP synthase active site.
ANP is hydrophobic and ATP is hydrophilic, which makes ANP a better reactant.
Transcribed Image Text:Why was it necessary to use phosphoaminophosphonic acid-adenylate ester (ANP) in the ATP synthase enzyme active site rather than ATP to resolve the molecular structure of the ATP synthase active site by x-ray crystallography? ANP Mg²+ E193 T164 E189 31 ANP has a S-S bond in the purine ring of the nucleotide to aid in crystallography. ANP is nonhydrolyzable and will trap the enzyme in the desired conformation. ATP cannot be used in a cell free system because it will be readily hydrolyzed. ATP is twice as large as ANP and will not fit in the ATP synthase active site. ANP is hydrophobic and ATP is hydrophilic, which makes ANP a better reactant.
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