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User:Megan Leaman/Sandbox 1
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=Human Diacylglycerol O-Transferase 1= | =Human Diacylglycerol O-Transferase 1= | ||
<StructureSection load='YOUR PDB CODE' size='350' frame='true' side='right' caption='Human Diacylglycerol O-Transferase 1 6VYI' scene=’His415 in Active Site’> | <StructureSection load='YOUR PDB CODE' size='350' frame='true' side='right' caption='Human Diacylglycerol O-Transferase 1 6VYI' scene=’His415 in Active Site’> | ||
| - | + | Diacylglycerol acyltransferase (DGAT) catalyzes the final and only committed step of triacylglycerol synthesis.2 It does this by using diacylglycerol (DAG) and oleoyl CoA as substrates. DGAT plays a pivotal role in the metabolism of DAG and is important to the process of triacylglycerol metabolism. This metabolism is involved in intestinal fat absorption, lipoprotein assembly, lactation, and adipose tissue formation.1 | |
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[[Image:Dgat full molecule.png|400 px|right|thumb|Figure 1]] | [[Image:Dgat full molecule.png|400 px|right|thumb|Figure 1]] | ||
== Function == | == Function == | ||
Revision as of 19:50, 4 April 2021
Human Diacylglycerol O-Transferase 1
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References
- ↑ Ransey E, Paredes E, Dey SK, Das SR, Heroux A, Macbeth MR. Crystal structure of the Entamoeba histolytica RNA lariat debranching enzyme EhDbr1 reveals a catalytic Zn(2+) /Mn(2+) heterobinucleation. FEBS Lett. 2017 Jul;591(13):2003-2010. doi: 10.1002/1873-3468.12677. Epub 2017, Jun 14. PMID:28504306 doi:http://dx.doi.org/10.1002/1873-3468.12677
Student Contributors
- Megan Leaman
- Grace Hall
- Karina Latsko
