Arginase
From Proteopedia
(Difference between revisions)
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| - | <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 == | ||
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== Structural highlights == | == Structural highlights == | ||
| - | The manganese ions are located at the bottom of a 15A cleft. The proposed reaction mechanism involves H141, D128, E277 in rat. <scene name='59/593950/Cv/ | + | The manganese ions are located at the bottom of a 15A cleft. The proposed reaction mechanism involves H141, D128, E277 in rat. <scene name='59/593950/Cv/4'>Active site</scene>.<ref>PMID:11258880</ref> |
</StructureSection> | </StructureSection> | ||
Revision as of 11:41, 11 March 2018
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3D structures of arginase
Updated on 11-March-2018
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
