Rhea - reaction knowledgebase

Enzymes

UniProtKB ^help_outline	5 proteins
Enzyme class ^help_outline	EC 2.7.1.165 glycerate 2-kinase
GO Molecular Function ^help_outline	GO:0043798 glycerate 2-kinase activity

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Name ^help_outline (R)-glycerate Identifier CHEBI:16659 Charge -1 Formula C3H5O4 InChIKey^help_outline RBNPOMFGQQGHHO-UWTATZPHSA-M SMILES^help_outline OC[C@@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 22 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline ATP Identifier CHEBI:30616 (Beilstein: 3581767) ^help_outline Charge -4 Formula C10H12N5O13P3 InChIKey^help_outline ZKHQWZAMYRWXGA-KQYNXXCUSA-J SMILES^help_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,308 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline (2R)-2-phosphoglycerate Identifier CHEBI:58289 Charge -3 Formula C3H4O7P InChIKey^help_outline GXIURPTVHJPJLF-UWTATZPHSA-K SMILES^help_outline OC[C@@H](OP([O-])([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) ^help_outline Charge -3 Formula C10H12N5O10P2 InChIKey^help_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILES^help_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 855 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Name ^help_outline H⁺ Identifier CHEBI:15378 Charge 1 Formula H InChIKey^help_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILES^help_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,836 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule

Cross-references

	RHEA:27377	RHEA:27378	RHEA:27379	RHEA:27380
Reaction direction	undefined	left-to-right	right-to-left	bidirectional
UniProtKB ^help_outline	5 proteins	1 proteins
EC numbers ^help_outline	2.7.1.165
Gene Ontology ^help_outline	GO:0043798
MetaCyc ^help_outline		GKI-RXN
EcoCyc ^help_outline		GKI-RXN

Publications

A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.

Liu B., Wu L., Liu T., Hong Y., Shen Y., Ni J.

A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme dis ... >> More

A glycerate kinase gene (ST2037) from the hyperthermophilic crenarchaeon Sulfolobus tokodaii was cloned and expressed in Escherichia coli. The purified homodimeric protein (45 kDa) specifically catalyzed the formation of 2-phosphoglycerate with D-glycerate as substrate. The thermostable enzyme displayed maximum activity (over 20 min) at 90 degrees C and pH 4.5. The maximal activity was in the presence of Co(2+). The MOFRL family glycerate kinase used AMP as phosphate donor with maximal activity towards GTP. These characteristics of the enzyme suggested its potential in the catalytic production of 2-phosphoglycerate. << Less

Biotechnol. Lett. 31:1937-1941(2009) [PubMed] [EuropePMC]
A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization.

Liu B., Hong Y., Wu L., Li Z., Ni J., Sheng D., Shen Y.

A glycerate kinase (GK) gene (PH0495) from the hyperthermophilic archaeon Pyrococcus horikoshii, was cloned and expressed in Escherichia coli. The recombinant protein was purified to homogeneity by affinity chromatography and ion exchange chromatography. The enzyme was likely a homodimer based on ... >> More

A glycerate kinase (GK) gene (PH0495) from the hyperthermophilic archaeon Pyrococcus horikoshii, was cloned and expressed in Escherichia coli. The recombinant protein was purified to homogeneity by affinity chromatography and ion exchange chromatography. The enzyme was likely a homodimer based on SDS-PAGE (47 kDa) and gel filtration chromatography (100 kDa) analysis. A radioisotope-labeling examination method was initially used for the enzymatic activity detection, and the enzyme (GK(ph)) was found to catalyze the formation of 2-phosphoglycerate using D: -glycerate as the substrate. The enzyme exhibited unique phosphoryl donor specificity with maximal activity towards pyrophosphate. The temperature and pH optima of the enzyme were 45 degrees C and 7.0, respectively, and about half of the maximal activity remained at 100 degrees C. The enzyme was highly thermostable with almost no loss of activity at 90 degrees C for 12 h. Based on sequence alignment and structural comparison it was assigned to group I of the trichotomy of GKs. << Less

Extremophiles 11:733-739(2007) [PubMed] [EuropePMC]
Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus.

Reher M., Bott M., Schonheit P.

Picrophilus torridus has been shown to degrade glucose via a nonphosphorylative Entner-Doudoroff (ED) pathway. Here we report the characterization of a key enzyme of this pathway, glycerate kinase (2-phosphoglycerate forming). The enzyme was purified 5,100-fold to homogeneity. The 95 kDa homodimer ... >> More

Picrophilus torridus has been shown to degrade glucose via a nonphosphorylative Entner-Doudoroff (ED) pathway. Here we report the characterization of a key enzyme of this pathway, glycerate kinase (2-phosphoglycerate forming). The enzyme was purified 5,100-fold to homogeneity. The 95 kDa homodimeric protein catalyzed the ATP-dependent phosphorylation of glycerate specifically to 2-phosphoglycerate. The enzyme showed highest activity at 60 degrees C and pH 7.3, with ATP as phosphoryl donor and Mg(2+) as divalent cation. By MALDI-TOF analysis, ORF Pto1442 was identified in the genome of P. torridus as the encoding gene, designated gck. Homologs with high sequence identity were identified in the genomes of the archaea Thermoplasma and Sulfolobus spp. and Thermoproteus tenax, for which the operation of nonphosphorylative ED pathways, involving 2-phosphoglycerate forming glycerate kinases, has been proposed. << Less

FEMS Microbiol. Lett. 259:113-119(2006) [PubMed] [EuropePMC]

RHEA:27377 (R)-glycerate + ATP = (2R)-2-phosphoglycerate + ADP + H(+)

Enzymes

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Cross-references

Publications

A MOFRL family glycerate kinase from the thermophilic crenarchaeon, Sulfolobus tokodaii, with unique enzymatic properties.

A unique highly thermostable 2-phosphoglycerate forming glycerate kinase from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning, expression and characterization.

Characterization of glycerate kinase (2-phosphoglycerate forming), a key enzyme of the nonphosphorylative Entner-Doudoroff pathway, from the thermoacidophilic euryarchaeon Picrophilus torridus.