User:Joseph Whaley/Sandbox 650

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
<Structure load='<Structure load='2PHA' size='500' frame='true' align='right' caption='This is the structure of Arginase' scene='Insert optional scene name here' />
<Structure load='<Structure load='2PHA' size='500' frame='true' align='right' caption='This is the structure of Arginase' scene='Insert optional scene name here' />
-
Carbamoyl-Phosphate Synthetase I is an enzyme located within the Mitochondria during the Urea Cycle; with its production, Urea will subsequently be formed. Urea will then be transported throughout the blood back to the kidneys where excretion will ensue. It is comprised from a series of reaction, The set of reactions begins with the phosphorylation of bicarbonate. This bicarbonate molecule will then bind an ammonia from glutamine thereby causing a reaction with carboxyphosphate. This will result in the production of Carbomate which is then phosphorylated to become carbamoyl-phosphate.
+
== '''Structure and Functionality''' ==
 +
Arginase belongs to the hydrolase family and is typically in the alpha-beta-alpha structure. Arginase is the fifth and final enzyme used in the Urea Cycle to produce ornithine from arginine and exert ammonia as a biproduct. In order for arginase to to produce ornithine, the active site of arginine must be bound by a metal ion in order to facilitate hydrogen-bonding-assisted stability of the substrate. The enzyme demonstrates a highly specific active site allowing for a conserved structural arrangement allowing for the hydrolysis of arginine to form ornithine.
 +
 
 +
 
 +
 
 +
 
 +
 
 +
 
 +
 
 +
== '''References''' ==
 +
^ MeSH Ureohydrolases
 +
^ a b Lee J, Suh SW, Kim KH, Kim D, Yoon HJ, Kwon AR, Ahn HJ, Ha JY, Lee HH (2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): -. doi:10.1074/jbc.M409246200. PMID 15355972.
 +
^ Christianson DW, Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F (2005). "Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response". Proc. Natl. Acad. Sci. U.S.A. 102 (37): -. doi:10.1073/pnas.0504027102. PMC 1201588. PMID 16141327. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1201588.
 +
^ a b Clifton IJ, Elkins JM, Hernandez H (2002). "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis". Biochem. J. 366 (Pt 2): -. doi:10.1042/BJ20020125. PMC 1222790. PMID 12020346. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222790.
 +
^ Baker BS, Tata JR, Xu Q (1993). "Developmental and hormonal regulation of the Xenopus liver-type arginase gene". Eur. J. Biochem. 211 (3): 891–898. doi:10.1111/j.1432-1033.1993.tb17622.x. PMID 7916684.
 +
^ Ahn HJ, Kim KH, Lee J, et al. (November 2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): 50505–13. doi:10.1074/jbc.M409246200. PMID 15355972. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15355972.
 +
^ "IPR006035 Ureohydrolase". http://www.ebi.ac.uk/interpro/IEntry?ac=IPR006035. Retrieved 2009-02-17.

Revision as of 04:32, 8 November 2012

This is the structure of Arginase

Drag the structure with the mouse to rotate

Structure and Functionality

Arginase belongs to the hydrolase family and is typically in the alpha-beta-alpha structure. Arginase is the fifth and final enzyme used in the Urea Cycle to produce ornithine from arginine and exert ammonia as a biproduct. In order for arginase to to produce ornithine, the active site of arginine must be bound by a metal ion in order to facilitate hydrogen-bonding-assisted stability of the substrate. The enzyme demonstrates a highly specific active site allowing for a conserved structural arrangement allowing for the hydrolysis of arginine to form ornithine.




References

^ MeSH Ureohydrolases ^ a b Lee J, Suh SW, Kim KH, Kim D, Yoon HJ, Kwon AR, Ahn HJ, Ha JY, Lee HH (2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): -. doi:10.1074/jbc.M409246200. PMID 15355972. ^ Christianson DW, Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F (2005). "Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response". Proc. Natl. Acad. Sci. U.S.A. 102 (37): -. doi:10.1073/pnas.0504027102. PMC 1201588. PMID 16141327. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1201588. ^ a b Clifton IJ, Elkins JM, Hernandez H (2002). "Oligomeric structure of proclavaminic acid amidino hydrolase: evolution of a hydrolytic enzyme in clavulanic acid biosynthesis". Biochem. J. 366 (Pt 2): -. doi:10.1042/BJ20020125. PMC 1222790. PMID 12020346. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1222790. ^ Baker BS, Tata JR, Xu Q (1993). "Developmental and hormonal regulation of the Xenopus liver-type arginase gene". Eur. J. Biochem. 211 (3): 891–898. doi:10.1111/j.1432-1033.1993.tb17622.x. PMID 7916684. ^ Ahn HJ, Kim KH, Lee J, et al. (November 2004). "Crystal structure of agmatinase reveals structural conservation and inhibition mechanism of the ureohydrolase superfamily". J. Biol. Chem. 279 (48): 50505–13. doi:10.1074/jbc.M409246200. PMID 15355972. http://www.jbc.org/cgi/pmidlookup?view=long&pmid=15355972. ^ "IPR006035 Ureohydrolase". http://www.ebi.ac.uk/interpro/IEntry?ac=IPR006035. Retrieved 2009-02-17.

Proteopedia Page Contributors and Editors (what is this?)

Joseph Whaley

Retrieved from "http://52.214.119.220/wiki/index.php/User:Joseph_Whaley/Sandbox_650"
Personal tools