Glycerate kinase
From Proteopedia
(Difference between revisions)
| Line 47: | Line 47: | ||
== 3D Structures of glycerate kinase == | == 3D Structures of glycerate kinase == | ||
| + | |||
| + | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
[[1to6]] – GK – ''Neisseria meningitides'' | [[1to6]] – GK – ''Neisseria meningitides'' | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 08:42, 10 March 2013
Image:1to6.png
Crystal Structure of glycerate kinase, 1to6
Glycerate kinase (GK) catalyzes the conversion of ATP + glycerate to ADP + 3-phospho-glycerate. GK participates in the metabolic pathways of serine/glycine/threonine, glycolipid and glyoxylate-dicarboxylate. GK is the last step in the pathway which starts with glucose and ends with 2-phosphoglycerate.
Contents |
3D Structures of glycerate kinase
Updated on 10-March-2013
1to6 – GK – Neisseria meningitides
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Eran Hodis
