Carbamoyl phosphate synthetase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (09:15, 22 April 2019) (edit) (undo)
 
(5 intermediate revisions not shown.)
Line 2: Line 2:
== Function ==
== Function ==
-
'''Carbamoyl phosphate synthetase''' (CPS) catalyzes the production of carbamoyl phosphate from ATP, Mg+2, bicarbonate andglutamine. CPS is part of the pyrimidine and arginine biosynthesis as well as the urea cycle in vertebrates. Ornithine is an allosteric effector of CPS.<ref>PMID:5329589</ref> There are 3 forms of CPS:<br />
+
'''Carbamoyl phosphate synthetase''' (CPS) catalyzes the production of carbamoyl phosphate from ATP, Mg+2, bicarbonate and glutamine. CPS is part of the pyrimidine and arginine biosynthesis as well as the urea cycle in vertebrates. Ornithine is an allosteric effector of CPS.<ref>PMID:5329589</ref> There are 3 forms of CPS:<br />
* '''CPS I''' participates in the urea cycle. CPS I uses glutamine for NH3 source.<br />
* '''CPS I''' participates in the urea cycle. CPS I uses glutamine for NH3 source.<br />
* '''CPS II''' participates in pyrimidine metabolism<br />
* '''CPS II''' participates in pyrimidine metabolism<br />
Line 13: Line 13:
== Structural highlights ==
== Structural highlights ==
-
CPS I and II are composed of 2 subunits. The large subunit contain active sites which bind nucleotides and other effectors. The small subunit catalyzes the hydrolysis of glutamine to glutamate and NH3. The <scene name='49/493669/Cv/3'>small subunit active site contains an active Cys residue</scene>.<ref>PMID:9636022</ref> CPS I contains a methylglyoxal synthetase (MGS) domain which binds <scene name='49/493669/Cv/6'>L-ornithine</scene>. Water molecules are shown as red spheres.
+
CPS I and II are composed of 2 subunits. The large subunit contain active sites which bind nucleotides and other effectors. The small subunit catalyzes the hydrolysis of glutamine to glutamate and NH3. The <scene name='49/493669/Cv/3'>small subunit active site contains an active Cys residue</scene>.<ref>PMID:9636022</ref> CPS I contains a methylglyoxal synthetase (MGS) domain which binds <scene name='49/493669/Cv/6'>L-ornithine</scene>. Water molecules are shown as red spheres.
-
</StructureSection>
+
<scene name='49/493669/Cv/11'>ADP binding site</scene>.
-
==3D structures of carbamoyl phosphate synthetase==
+
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
<scene name='49/493669/Cv/12'>Mn coordination site</scene>.
-
[[1jdb]] - EcCPS + phosphate + glutamine + ADP – ''Escherichia coli''<br />
+
<scene name='49/493669/Cv/13'>K coordination site</scene>.
-
[[1a9x]], [[1cs0]] - EcCPS + phosphate + ornithine + ADP<BR />
+
 
-
[[1c30]], [[1m6v]] - EcCPS (mutant) + phosphate + ornithine + ADP<BR />
+
==3D structures of carbamoyl phosphate synthetase==
-
[[1bxr]] - EcCPS + ornithine + AMPPNP<br />
+
[[Carbamoyl phosphate synthetase 3D structures]]
-
[[1ce8]] - EcCPS + phosphate + ornithine + inosinic acid + ADP<BR />
+
 
-
[[1c3o]] - EcCPS (mutant) + phosphate + ornithine + glutamine + ADP<BR />
+
</StructureSection>
-
[[1kee]] - EcCPS + phosphate + ornithine + acivicin + ADP<BR />
+
-
[[1t36]] - EcCPS (mutant) + phosphate + ornithine + UMP + ADP<BR />
+
-
[[5dot]] – hCPS I – human<br />
+
-
[[2yvq]] – CPS I MGS domain <br />
+
-
[[5dou]] – hCPS I + phosphate + ADP <br />
+
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

E. coli carbamoyl phosphate synthetase large chain (cyan) and small chain (salmon) complex with ADP, phosphate and ornithine, 1a9x

Drag the structure with the mouse to rotate

References

  1. Kalman SM, Duffield PH, Brzozowski T. Purification and properties of a bacterial carbamyl phosphate synthetase. J Biol Chem. 1966 Apr 25;241(8):1871-7. PMID:5329589
  2. Thoden JB, Miran SG, Phillips JC, Howard AJ, Raushel FM, Holden HM. Carbamoyl phosphate synthetase: caught in the act of glutamine hydrolysis. Biochemistry. 1998 Jun 23;37(25):8825-31. PMID:9636022 doi:http://dx.doi.org/10.1021/bi9807761

Proteopedia Page Contributors and Editors (what is this?)

Alexander Berchansky, Michal Harel

Personal tools