User:Betsy Johns/Sandbox 1
From Proteopedia
(Difference between revisions)
Line 3: | Line 3: | ||
==Introduction== | ==Introduction== | ||
- | |||
- | [[Image:DGAT Mechanism.png|100 px|right|thumb|Figure 1: DGAT Mechanism]] | ||
Diacylglycerol acyltransferase (DGAT) is a membrane protein that synthesizes triacylglycerides from its two substrates diacylglycerol (DAG) and fatty acyl-CoA for dietary fat absorption and fat storage. DGAT can be found expressed in the small intestine’s epithelial cells, in the liver where it synthesizes fat for storage, and in the female mammary glands where it produces fat for milk <ref name="Wang">PMID: 32433610</ref>. DGAT is a member of the membrane-bound O- acyltransferases (MBOAT) family <ref name="Sui">PMID: 32433611</ref>. All of the enzymes within this family are transmembrane enzymes that acylate lipids or proteins. Additionally, MBOAT enzymes have a conserved MBOAT core, a channel-like region that acts as the enzyme’s active site. Another feature of note within this MBOAT core is the conserved catalytic Histidine. | Diacylglycerol acyltransferase (DGAT) is a membrane protein that synthesizes triacylglycerides from its two substrates diacylglycerol (DAG) and fatty acyl-CoA for dietary fat absorption and fat storage. DGAT can be found expressed in the small intestine’s epithelial cells, in the liver where it synthesizes fat for storage, and in the female mammary glands where it produces fat for milk <ref name="Wang">PMID: 32433610</ref>. DGAT is a member of the membrane-bound O- acyltransferases (MBOAT) family <ref name="Sui">PMID: 32433611</ref>. All of the enzymes within this family are transmembrane enzymes that acylate lipids or proteins. Additionally, MBOAT enzymes have a conserved MBOAT core, a channel-like region that acts as the enzyme’s active site. Another feature of note within this MBOAT core is the conserved catalytic Histidine. | ||
Line 14: | Line 12: | ||
== Function == | == Function == | ||
+ | |||
+ | [[Image:DGAT Mechanism.png|100 px|right|thumb|Figure 1: DGAT Mechanism]] | ||
<scene name='87/877512/Dimer_interface/5'>H bonding at interface</scene> | <scene name='87/877512/Dimer_interface/5'>H bonding at interface</scene> |
Revision as of 15:58, 4 April 2021
Diacylglycerol acyltransferase, DGAT
|
References
- ↑ 1.0 1.1 Wang L, Qian H, Nian Y, Han Y, Ren Z, Zhang H, Hu L, Prasad BVV, Laganowsky A, Yan N, Zhou M. Structure and mechanism of human diacylglycerol O-acyltransferase 1. Nature. 2020 May;581(7808):329-332. doi: 10.1038/s41586-020-2280-2. Epub 2020 May, 13. PMID:32433610 doi:http://dx.doi.org/10.1038/s41586-020-2280-2
- ↑ 2.0 2.1 Sui X, Wang K, Gluchowski NL, Elliott SD, Liao M, Walther TC, Farese RV Jr. Structure and catalytic mechanism of a human triacylglycerol-synthesis enzyme. Nature. 2020 May;581(7808):323-328. doi: 10.1038/s41586-020-2289-6. Epub 2020 May, 13. PMID:32433611 doi:http://dx.doi.org/10.1038/s41586-020-2289-6
Student Contributors
- Betsy Johns
- Elise Wang
- Tyler Bihasa