Difference between revisions of "Os12g0100500"
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| − | + | The rice gene '''''Os12g0100500''''' was not functionally studied yet. | |
==Annotated Information== | ==Annotated Information== | ||
| − | ''Os12g0100500'' in rice hasn't been studied. However, by running blast, we can find that query coverage is 100% with predicted protein | + | * ''Os12g0100500'' in rice hasn't been studied. However, by running blast, we can find that query coverage is 100% with predicted protein. |
| + | * This gene is predicted to be coding Lysophospholipase [Lipid metabolism]; COG2267. | ||
| + | ===Gene Symbol=== | ||
| + | *'''''Os12g0100500''''' '''''<=>''''' '''''COG2267, OsCOG2267''''' | ||
| + | |||
===Function=== | ===Function=== | ||
| − | In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction | + | * In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction |
| − | + | * 2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate | |
| − | 2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate | + | * Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate. |
| − | Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate. | + | * This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds. |
| − | This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds | ||
| − | |||
| − | |||
===Evolution=== | ===Evolution=== | ||
| − | + | * This family consists of lysophospholipase / phospholipase B EC 3.1.1.5 and cytosolic phospholipase A2 which also has a C2 domain IPR000008. | |
| + | * Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells. | ||
| + | * Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids, | ||
| + | * the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in. | ||
You can also add sub-section(s) at will. | You can also add sub-section(s) at will. | ||
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==References== | ==References== | ||
| − | [1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085. | + | * [1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085. |
| − | [2]Jump up to: a b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052. | + | * [2]Jump up to: a b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052. |
[[Category:Genes]] | [[Category:Genes]] | ||
| Line 30: | Line 34: | ||
[[Category:Japonica Chromosome 12]] | [[Category:Japonica Chromosome 12]] | ||
[[Category:Chromosome 12]] | [[Category:Chromosome 12]] | ||
| + | == Structured Information == | ||
Latest revision as of 09:29, 8 May 2017
The rice gene Os12g0100500 was not functionally studied yet.
Contents
Annotated Information
- Os12g0100500 in rice hasn't been studied. However, by running blast, we can find that query coverage is 100% with predicted protein.
- This gene is predicted to be coding Lysophospholipase [Lipid metabolism]; COG2267.
Gene Symbol
- Os12g0100500 <=> COG2267, OsCOG2267
Function
- In enzymology, a lysophospholipase (EC 3.1.1.5) is an enzyme that catalyzes the chemical reaction
- 2-lysophosphatidylcholine + H2O \rightleftharpoons glycerophosphocholine + a carboxylate
- Thus, the two substrates of this enzyme are 2-lysophosphatidylcholine and H2O, whereas its two products are glycerophosphocholine and carboxylate.
- This enzyme belongs to the family of hydrolases, specifically those acting on carboxylic ester bonds.
Evolution
- This family consists of lysophospholipase / phospholipase B EC 3.1.1.5 and cytosolic phospholipase A2 which also has a C2 domain IPR000008.
- Phospholipase B enzymes catalyse the release of fatty acids from lysophospholipids and are capable in vitro of hydrolyzing all phospholipids extractable from yeast cells.
- Cytosolic phospholipase A2 associates with natural membranes in response to physiological increases in Ca2+ and selectively hydrolyses arachidonyl phospholipids,
- the aligned region corresponds the carboxy-terminal Ca2+-independent catalytic domain of the protein as discussed in.
You can also add sub-section(s) at will.
Labs working on this gene
Please input related labs here.
References
- [1] Nalefski EA, Sultzman LA, Martin DM, Kriz RW, Towler PS, Knopf JL, Clark JD (1994). "Delineation of two functionally distinct domains of cytosolic phospholipase A2, a regulatory Ca(2+)-dependent lipid-binding domain and a Ca(2+)-independent catalytic domain". J. Biol. Chem. 269 (27): 18239–18249. PMID 8027085.
- [2]Jump up to: a b Lee KS, Patton JL, Fido M, Hines LK, Kohlwein SD, Paltauf F, Henry SA, Levin DE (1994). "The Saccharomyces cerevisiae PLB1 gene encodes a protein required for lysophospholipase and phospholipase B activity". J. Biol. Chem. 269 (31): 19725–19730. PMID 8051052.
