Difference between revisions of "3-phosphoglycerate kinase"
Line 8: | Line 8: | ||
== Rate equation == | == Rate equation == | ||
− | <center><math> \frac{V_{mf}\frac{[1,3BPG][ADP]}{ | + | Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used. |
+ | |||
+ | <center><math> \frac{V_{mf}\frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} - V_{mr}\frac{[3PG][ATP]}{K_{3PG} K_{ATP}}}{1 + \frac{[1,3BPG]}{K_{1,3BPG}} + \frac{[ADP]}{K_{ADP}} + \frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} + \frac{[3PG][ATP]}{K_{3PG} K_{ATP}} + \frac{[3PG]}{K_{3PG}} + \frac{[ADP]}{K_{ADP}} } </math></center> |
Revision as of 11:05, 27 February 2014
Phosphoglycerate kinase (PGK) is an enzyme that catalyzes the reversible transfer of a phosphate group from 1,3-bisphosphoglycerate (1,3-BPG) to ADP producing 3-phosphoglycerate (3-PG) and ATP. Like all kinases it is a transferase.
Chemical equation
![1,3BPG + ADP \rightleftharpoons 3PG + ATP](/wiki/images/math/c/3/9/c39a15c314413cab0ee1c050fc4b274f.png)
Rate equation
Random Bi-Bi reversible Michaelis-Menten euation for non-interacting substrates are used.
![\frac{V_{mf}\frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} - V_{mr}\frac{[3PG][ATP]}{K_{3PG} K_{ATP}}}{1 + \frac{[1,3BPG]}{K_{1,3BPG}} + \frac{[ADP]}{K_{ADP}} + \frac{[1,3BPG][ADP]}{K_{1,3BPG} K_{ADP}} + \frac{[3PG][ATP]}{K_{3PG} K_{ATP}} + \frac{[3PG]}{K_{3PG}} + \frac{[ADP]}{K_{ADP}} }](/wiki/images/math/8/e/b/8eb366ea68004741a7ace7e2cf32d509.png)