We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.
Arginase
From Proteopedia
(Difference between revisions)
| (7 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | <StructureSection load='1hqg' size=' | + | <StructureSection load='1hqg' size='400' side='right' caption='Structure of rat arginase containing Mn+2 (purple) complex with ornithine (cyan) and urea (yellow) (PDB code [[1hqg]]).' scene='59/593950/Cv/1'> |
== Function == | == Function == | ||
| - | '''Arginase''' (Arg) catalyzes the conversion of arginine to ornithine and urea. Arg is the final enzyme in the urea cycle. Arg requires 2 manganese ions for functioning. | + | '''Arginase''' (Arg) catalyzes the conversion of arginine to ornithine and urea. Arg is the final enzyme in the urea cycle. Arg requires 2 manganese ions for functioning.<ref>PMID:18360740</ref> |
== Disease == | == Disease == | ||
| Line 11: | Line 11: | ||
== Structural highlights == | == Structural highlights == | ||
| - | The manganese ions are located at the bottom of a 15A cleft. | + | The manganese ions are located at the bottom of a 15A cleft. <scene name='59/593950/Cv/4'>Active site</scene>. The proposed reaction mechanism involves <scene name='59/593950/Cv/5'>H141, D128, E277</scene> in rat.<ref>PMID:11258880</ref> |
| - | </ | + | |
==3D structures of arginase== | ==3D structures of arginase== | ||
| + | [[Arginase 3D structures]] | ||
| - | + | </StructureSection> | |
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
| - | + | ||
== References == | == References == | ||
Current revision
| |||||||||||
References
- ↑ Dowling DP, Di Costanzo L, Gennadios HA, Christianson DW. Evolution of the arginase fold and functional diversity. Cell Mol Life Sci. 2008 Jul;65(13):2039-55. doi: 10.1007/s00018-008-7554-z. PMID:18360740 doi:http://dx.doi.org/10.1007/s00018-008-7554-z
- ↑ Cox JD, Cama E, Colleluori DM, Pethe S, Boucher JL, Mansuy D, Ash DE, Christianson DW. Mechanistic and metabolic inferences from the binding of substrate analogues and products to arginase. Biochemistry. 2001 Mar 6;40(9):2689-701. PMID:11258880
