Cassady sandbox1: Difference between revisions

Line 12:

==Mechanism==

Phosphofructokinase binds both Mg2+-ATP and fructose-6-phosphate (F6P) to make fructose-1,6-bisphosphate and Mg2+-ADP. Although the image with both of these products has not been determined, <scene name='Zach_Westrick_Sandbox/Products_2/2'>F6P and Mg2+-ADP</scene> bound to the enzyme has been. There are three ligand binding sites per subunit. Two make up the active site, which binds F6P and ATP, while the third is an allosteric binding site.<ref>PMID:6115424</ref> Some proposed residues involved at the active site include <scene name='Zach_Westrick_Sandbox/Active_site_2/1'>ASP 127 and ARG 171</scene>.<ref>http://www.nature.com/nature/journal/v327/n6121/abs/327437a0.html</ref> PFK ~~exist~~ in two conformational states, both <scene name='Zach_Westrick_Sandbox/R_state/1'>R</scene> and <scene name='Zach_Westrick_Sandbox/T_state/1'>T states</scene> which are in equilibrium. ATP binds ~~both~~ active and allosteric sites in both conformations.

Phosphofructokinase binds both Mg2+-ATP and fructose-6-phosphate (F6P) to make fructose-1,6-bisphosphate and Mg2+-ADP. Although the image with both of these products has not been determined, <scene name='Zach_Westrick_Sandbox/Products_2/2'>F6P and Mg2+-ADP</scene> bound to the enzyme has been. There are three ligand binding sites per subunit. Two make up the active site, which binds F6P and ATP, while the third is an allosteric binding site.<ref>PMID:6115424</ref> Some proposed residues involved at the active site include <scene name='Zach_Westrick_Sandbox/Active_site_2/1'>ASP 127 and ARG 171</scene>.<ref>http://www.nature.com/nature/journal/v327/n6121/abs/327437a0.html</ref> PFK exists in two conformational states, both <scene name='Zach_Westrick_Sandbox/R_state/1'>R</scene> and <scene name='Zach_Westrick_Sandbox/T_state/1'>T states</scene> which are in equilibrium. ATP binds the active and allosteric sites in both conformations.

[[Image:PFK mech.JPG]]

Cassady sandbox1: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 12: / Line 12: @@
 ==Mechanism==
-Phosphofructokinase binds both Mg2+-ATP and fructose-6-phosphate (F6P) to make fructose-1,6-bisphosphate and Mg2+-ADP. Although the image with both of these products has not been determined, <scene name='Zach_Westrick_Sandbox/Products_2/2'>F6P and Mg2+-ADP</scene> bound to the enzyme has been. There are three ligand binding sites per subunit. Two make up the active site, which binds F6P and ATP, while the third is an allosteric binding site.<ref>PMID:6115424</ref> Some proposed residues involved at the active site include <scene name='Zach_Westrick_Sandbox/Active_site_2/1'>ASP 127 and ARG 171</scene>.<ref>http://www.nature.com/nature/journal/v327/n6121/abs/327437a0.html</ref> PFK exist in two conformational states, both  <scene name='Zach_Westrick_Sandbox/R_state/1'>R</scene> and <scene name='Zach_Westrick_Sandbox/T_state/1'>T states</scene> which are in equilibrium. ATP binds both active and allosteric sites in both conformations.
+Phosphofructokinase binds both Mg2+-ATP and fructose-6-phosphate (F6P) to make fructose-1,6-bisphosphate and Mg2+-ADP. Although the image with both of these products has not been determined, <scene name='Zach_Westrick_Sandbox/Products_2/2'>F6P and Mg2+-ADP</scene> bound to the enzyme has been. There are three ligand binding sites per subunit. Two make up the active site, which binds F6P and ATP, while the third is an allosteric binding site.<ref>PMID:6115424</ref> Some proposed residues involved at the active site include <scene name='Zach_Westrick_Sandbox/Active_site_2/1'>ASP 127 and ARG 171</scene>.<ref>http://www.nature.com/nature/journal/v327/n6121/abs/327437a0.html</ref> PFK exists in two conformational states, both  <scene name='Zach_Westrick_Sandbox/R_state/1'>R</scene> and <scene name='Zach_Westrick_Sandbox/T_state/1'>T states</scene> which are in equilibrium. ATP binds the active and allosteric sites in both conformations.
 [[Image:PFK mech.JPG]]