Glycerol kinase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
 
+
<StructureSection load='1xup' size='350' side='right' caption='Glycerol kinase complex with glycerol (PDB entry [[1xup]])' scene=''>
-
<StructureSection load='1xup' size='350' side='right' caption='Human α-defensin 1 (PDB entry [[2pm4]])' scene=''>
+
== Function ==
== Function ==
'''Glycerol kinase''' (GK) phosphorylates glycerol forming glycerol 3-phosphate (G3P) using Mg-ATP as phosphate source. GK is a key enzyme in glycerol uptake and metabolism. Mutations of GK gene cause GK deficiency syndrome. PK is a multi-subunit allosteric enzyme. Its activity can be inhibited by fructose 1,6-bisphosphate (FBP) and by the glucose-specific phosphocarrier IIA(Glc). PK cofactor is a Zn atom which binds to the dimer<ref>PMID:8528769</ref>.
'''Glycerol kinase''' (GK) phosphorylates glycerol forming glycerol 3-phosphate (G3P) using Mg-ATP as phosphate source. GK is a key enzyme in glycerol uptake and metabolism. Mutations of GK gene cause GK deficiency syndrome. PK is a multi-subunit allosteric enzyme. Its activity can be inhibited by fructose 1,6-bisphosphate (FBP) and by the glucose-specific phosphocarrier IIA(Glc). PK cofactor is a Zn atom which binds to the dimer<ref>PMID:8528769</ref>.

Revision as of 07:47, 13 March 2016

Glycerol kinase complex with glycerol (PDB entry 1xup)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman

Personal tools