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Overview of ATCase Regulation

The document discusses aspartate transcarbamoylase (ATCase), an allosteric enzyme that is feedback inhibited by CTP, the final product of the pyrimidine pathway. ATCase is composed of catalytic and regulatory subunits; the regulatory subunits are responsible for the enzyme's regulation by ATP and CTP. Experiments showing the dissociation of ATCase into subunits after treatment with p-hydroxymercuribenzoate helped reveal that the regulatory subunits control the enzyme's activity in response to metabolic effectors.

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Romi George
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0% found this document useful (0 votes)
20 views24 pages

Overview of ATCase Regulation

The document discusses aspartate transcarbamoylase (ATCase), an allosteric enzyme that is feedback inhibited by CTP, the final product of the pyrimidine pathway. ATCase is composed of catalytic and regulatory subunits; the regulatory subunits are responsible for the enzyme's regulation by ATP and CTP. Experiments showing the dissociation of ATCase into subunits after treatment with p-hydroxymercuribenzoate helped reveal that the regulatory subunits control the enzyme's activity in response to metabolic effectors.

Uploaded by

Romi George
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PPTX, PDF, TXT or read online on Scribd

Sadia Sayed

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 ATCase is feedback inhibited by the final product of the prymidine
pathway
 ATCase is the most intensely studied allosteric enzyme. It is feedback
inhibited by CTP. ATP activates it.
 Importance of this regulation
1. ATP activates this enzyme, signaling that energy is available for DNA
synthesis.
2. CTP inhibits it, stating that there is enough prymidine no need to make
more!
 ATCase has catalytic and regulatory subunits.
 Catalytic subunits: catalytically active by no regulation by ATP and CTP.
 Regulatory subunits: catalytically inactive but regulated by ATP and
CTP. Reulatory subunits vanish when the enzyme is treated with p-
hydroxymercuribenzoate.

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Ultracentrifugation of ATCase: A) native B) dissociation after p-
hydroxymercuribenzoate

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PALA

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Active site of ATCase

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Quaternary structural changes T --> R in
ATCase

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