Removing a specific segment of the human tissue transglutaminase protein decreases its ability to perform one enzymatic function by more than 95% while increasing another enzymatic function by up to...
Mechanism
Synthesis from 1 study
This protein has two jobs: linking proteins together and breaking down energy molecules. A part at the end of the protein stops it from breaking down energy, but helps it link proteins. When that end part is removed, it can't link proteins anymore, but it starts breaking down energy much faster...
Most probable mechanism
A specific part at the end of this protein blocks it from breaking down energy molecules like GTP and ATP, while also helping it do its main job of linking proteins together. When that end part is removed, the protein can no longer link proteins well, but it starts breaking down energy molecules much faster because the blockage is gone.
The C-terminal region (residues 345–538) physically obstructs access to the nucleotide-binding and hydrolysis site located in the N-terminal domain (residues 1–185), preventing efficient binding and catalysis of GTP and ATP.
Removal of the C-terminal region exposes the catalytic site, allowing unrestricted binding of GTP and ATP and increasing the rate of hydrolysis to GDP/GMP and ADP/AMP without altering substrate affinity.
The same C-terminal region is required to maintain the structural conformation necessary for calcium-dependent transglutaminase activity, and its deletion disrupts the active site geometry required for protein cross-linking.
Evidence from Studies
Supporting (1)
Community contributions welcome
C-terminal Deletion of Human Tissue Transglutaminase Enhances Magnesium-dependent GTP/ATPase Activity*
Contradicting (0)
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Gold Standard Evidence Needed
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