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Are the given reactions examples of general acid/base catalysis, covalent catalysis, catalysis by approximation (proximity effect), or metal-ion catalysis? Glu HN R' Enzyme substrate complex Glu H HN R' oe ***** Zn2+ Tetrahedral intermediate NMP kinases bring two nucleotides, such as AMP and ATP, together to facilitate the transfer of a phosphoryl group from one nucleotide to the other (creating two ADP). The enzyme positions the adenosine triphosphate (ATP) such that the gamma phosphate group is placed adjacently to the phosphate group of the NMP kinase. This facilitates the transfer of the phosphate between the two molecule. In aspartate ammonia lyase, a deprotonated serine sidechain performs a nucleophilic attack on a carbonyl carbon of the substrate. An active site histidine abstracts a proton from a substrate, making it more reactive, and then donates the proton back to the product. general acid/base catalysis catalysis by approximation metal-ion catalysis covalent catalysis

Are the given reactions examples of general acid/base catalysis, covalent catalysis, catalysis by approximation (proximity effect), or metal-ion catalysis? Glu HN R' Enzyme substrate complex Glu H HN R' oe ***** Zn2+ Tetrahedral intermediate NMP kinases bring two nucleotides, such as AMP and ATP, together to facilitate the transfer of a phosphoryl group from one nucleotide to the other (creating two ADP). The enzyme positions the adenosine triphosphate (ATP) such that the gamma phosphate group is placed adjacently to the phosphate group of the NMP kinase. This facilitates the transfer of the phosphate between the two molecule. In aspartate ammonia lyase, a deprotonated serine sidechain performs a nucleophilic attack on a carbonyl carbon of the substrate. An active site histidine abstracts a proton from a substrate, making it more reactive, and then donates the proton back to the product. general acid/base catalysis catalysis by approximation metal-ion catalysis covalent catalysis

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
Problem 1P
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The options to pick for each are:
- general acid/base catalysis
- catalysis by approximation
- metal-ion catalysis
- covalent catalysis

Are the given reactions examples of general acid/base catalysis, covalent catalysis, catalysis by approximation (proximity effect), or metal-ion catalysis? Glu H R. HN. R' Enzyme substrate complex Glu R H HN R' Zn2+ PERE Tetrahedral intermediate NMP kinases bring two nucleotides, such as AMP and ATP, together to facilitate the transfer of a phosphoryl group from one nucleotide to the other (creating two ADP). The enzyme positions the adenosine triphosphate (ATP) such that the gamma phosphate group is placed adjacently to the phosphate group of the NMP kinase. This facilitates the transfer of the phosphate between the two molecule. In aspartate ammonia lyase, a deprotonated serine sidechain performs a nucleophilic attack on a carbonyl carbon of the substrate. An active site histidine abstracts a proton from a substrate, making it more reactive, and then donates the proton back to the product. general acid/base catalysis catalysis by approximation metal-ion catalysis covalent catalysis
Transcribed Image Text:Are the given reactions examples of general acid/base catalysis, covalent catalysis, catalysis by approximation (proximity effect), or metal-ion catalysis? Glu H R. HN. R' Enzyme substrate complex Glu R H HN R' Zn2+ PERE Tetrahedral intermediate NMP kinases bring two nucleotides, such as AMP and ATP, together to facilitate the transfer of a phosphoryl group from one nucleotide to the other (creating two ADP). The enzyme positions the adenosine triphosphate (ATP) such that the gamma phosphate group is placed adjacently to the phosphate group of the NMP kinase. This facilitates the transfer of the phosphate between the two molecule. In aspartate ammonia lyase, a deprotonated serine sidechain performs a nucleophilic attack on a carbonyl carbon of the substrate. An active site histidine abstracts a proton from a substrate, making it more reactive, and then donates the proton back to the product. general acid/base catalysis catalysis by approximation metal-ion catalysis covalent catalysis
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