About this item
- Title
- Understanding enzymatic mechanism and allostery using macromolecular rate theory
- Content partner
- University of Waikato
- Collection
- ResearchCommons@Waikato
- Description
Intricate systems of regulation at many levels act to control enzyme rates to tune metabolism across biosynthetic pathways. Allostery is a ubiquitous regulatory mechanism for feedback and regulation of enzymes in biosynthetic pathways. ATP-phosphoribosyltransferase from Mycobacterium tuberculosis (mtuATP-PRT) catalyses the first committed step in de novo histidine biosynthesis, and allosteric product inhibition of ATP-PRT by L-His is key to regulating metabolic flux in this pathway. mtuATP-PR...
- Format
- Research paper
- Research format
- Thesis
- Thesis level
- Doctoral
- Date created
- 2022
- Creator
- Grout, Emily Katherine
- URL
- https://hdl.handle.net/10289/14987
- Related subjects
- Biochemistry / Enzyme / Kinetics / Allostery / Thermodynamics / Macromolecular rate theory / MMRT / Crystallography / Molecular dynamics / Phylogenetics / Allosteric enzymes -- Mathematical models / Allosteric regulation -- Mathematical models / Enzyme kinetics -- Mathematical models / Enzymes -- Regulation -- Mathematical models / Enzymes -- Biotechnology -- Mathematical models / Enzymes -- Analysis -- Mathematical models / Heat
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Report this itemDigitalNZ brings together more than 30 million items from institutions so that they are easy to find and use. This information is the best information we could find on this item. This item was added on 23 July 2022, and updated 24 August 2023.
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