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LMP007740

UniProt Annotations

Entry Information
Gene Nameglycerol kinase
Protein EntryGLPK_ECOLI
UniProt IDP0A6F3
SpeciesE. coli
Comments
Comment typeDescription
Biophysicochemical PropertiesKinetic parameters: KM=1.3 uM for glycerol {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; KM=400 uM for D-glyceraldehyde {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; KM=500 uM for dihydroxyacetone {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; KM=3 mM for L-glyceraldehyde {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; KM=4 mM for ATP {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843}; pH dependence: Optimum pH is 9.8. {ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908, ECO:0000269|PubMed:9817843};
Catalytic ActivityATP + glycerol = ADP + sn-glycerol 3- phosphate. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:5335908}.
Enzyme RegulationActivity of this regulatory enzyme is affected by several metabolites. The non-competitive allosteric inhibition by fructose 1,6-bisphosphate (FBP) causes alterations in the quaternary structure of the enzyme. FBP inhibition requires that the enzyme exist only in a tetrameric state. Salt such as KCl reduces the affinity of the tetrameric form of the enzyme for FBP. Unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system, also inhibits non-competitively and allostericaly the activity. Unlike FBP, both the dimer and the tetramer appear to be fully sensitive to enzyme EIIA-Glc inhibition. Zn(+2) greatly enhances the inhibitory potency of EIIA-Glc. Both allosteric regulatory agents is strongly pH dependent, with maximal inhibition occurring at pH 6.5. {ECO:0000269|PubMed:215195, ECO:0000269|PubMed:2985549, ECO:0000269|PubMed:31903, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5328677, ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9817843, ECO:0000269|PubMed:9843423}.
FunctionKey enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn- glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:2826434, ECO:0000269|PubMed:4575199, ECO:0000269|PubMed:5335908}.
InductionBy L-alpha-glycerol 3-phosphate. {ECO:0000269|PubMed:2826434}.
PathwayPolyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00186}.
SimilarityBelongs to the FGGY kinase family. {ECO:0000255|HAMAP- Rule:MF_00186}.
SubunitHomotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc (crr). Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization. {ECO:0000255|HAMAP-Rule:MF_00186, ECO:0000269|PubMed:10090737, ECO:0000269|PubMed:17441732, ECO:0000269|PubMed:215194, ECO:0000269|PubMed:215195, ECO:0000269|PubMed:4934840, ECO:0000269|PubMed:8170944, ECO:0000269|PubMed:8430315, ECO:0000269|PubMed:9817843, ECO:0000269|PubMed:9843423}.
Web ResourceName=Worthington enzyme manual; URL="http://www.worthington-biochem.com/GKEC/";