Publications

• Purification and properties of D-glycerate 3-kinase from Escherichia coli.

  Doughty C.C., Hayashi J.A., Guenther H.L.

  J. Biol. Chem. 241:568-572(1966) [PubMed] [EuropePMC]

• Studies on the purification and properties of D-glyceric acid kinase of liver.

  ICHIHARA A., GREENBERG D.M.

  J Biol Chem 225:949-958(1957) [PubMed] [EuropePMC]

• D-glycerate 3-kinase, the last unknown enzyme in the photorespiratory cycle in Arabidopsis, belongs to a novel kinase family.

  Boldt R., Edner C., Kolukisaoglu U., Hagemann M., Weckwerth W., Wienkoop S., Morgenthal K., Bauwe H.

  D-GLYCERATE 3-KINASE (GLYK; EC 2.7.1.31) catalyzes the concluding reaction of the photorespiratory C2 cycle, an indispensable ancillary metabolic pathway to the photosynthetic C3 cycle that enables land plants to grow in an oxygen-containing atmosphere. Except for GLYK, all other enzymes that cont ... >> More

  D-GLYCERATE 3-KINASE (GLYK; EC 2.7.1.31) catalyzes the concluding reaction of the photorespiratory C2 cycle, an indispensable ancillary metabolic pathway to the photosynthetic C3 cycle that enables land plants to grow in an oxygen-containing atmosphere. Except for GLYK, all other enzymes that contribute to the C2 cycle are known by their primary structures, and the encoding genes have been identified. We have purified and partially sequenced this yet missing enzyme from Arabidopsis thaliana and identified it as a putative kinase-annotated single-copy gene At1g80380. The exclusive catalytic properties of the gene product were confirmed after heterologous expression in Escherichia coli. Arabidopsis T-DNA insertional knockout mutants show no GLYK activity and are not viable in normal air; however, they grow under elevated CO2, providing direct evidence of the obligatory nature of the ultimate step of the C2 cycle. The newly identified GLYK is both structurally and phylogenetically distinct from known glycerate kinases from bacteria and animals. Orthologous enzymes are present in other plants, fungi, and some cyanobacteria. The metabolic context of GLYK activity in fungi and cyanobacteria remains to be investigated. << Less

  Plant Cell 17:2413-2420(2005) [PubMed] [EuropePMC]

• Isolation and characterization of the human D-glyceric acidemia related glycerate kinase gene GLYCTK1 and its alternatively splicing variant GLYCTK2.

  Guo J.-H., Hexige S., Chen L., Zhou G.-J., Wang X., Jiang J.-M., Kong Y.-H., Ji G.-Q., Wu C.-Q., Zhao S.-Y., Yu L.

  Deficiency of human glycerate kinase leads to D-glycerate acidemia/D-glyceric aciduria. Through PCR cloning assisted by in silico approach, we isolated the human glycerate kinase genes--Glycerate Kinase 1 (GLYCTK1) and its alternatively splicing variant--Glycerate Kinase 2 (GLYCTK2), which might b ... >> More

  Deficiency of human glycerate kinase leads to D-glycerate acidemia/D-glyceric aciduria. Through PCR cloning assisted by in silico approach, we isolated the human glycerate kinase genes--Glycerate Kinase 1 (GLYCTK1) and its alternatively splicing variant--Glycerate Kinase 2 (GLYCTK2), which might be associated with D-glycerate acidemia/D-glyceric aciduria. The locus of GLYCTK gene is mapped to 3p21. PCR amplification in seventeen human tissue cDNAs revealed that both GLYCTK1 and GLYCTK2 are expressed widely almost in all these tissues. The expression of mouse Glyctk in various tissues was demonstrated by in situ hybridization. Both GLYCTK1 and GLYCTK2 proteins are localized in cytosol, and GLYCTK2 proteins are specifically localized in mitochondria. Present results revealed the characteristic expression pattern of murine Glyctk in neural system, skeleton muscle, supporting that glycerate kinase is implicated in D-glycerate acidemia/D-glyceric aciduria. << Less

  DNA Seq. 17:1-7(2006) [PubMed] [EuropePMC]

• Glycerate kinase from leaves of C3 plants.

  Schmitt M.R., Edwards G.E.

  D-Glycerate-3-kinase (EC 2.7.1.31) in six C3 species, including dicots (Pisum sativum, Spinacea oleracea, Antirrhinum majus) and monocots (Secale cereale, Hordeum vulgare, Avena sativa), ranged in activity from 44 to 353 mumol X mg chl-1 X h-1. Studies with protoplast extracts of these species ind ... >> More

  D-Glycerate-3-kinase (EC 2.7.1.31) in six C3 species, including dicots (Pisum sativum, Spinacea oleracea, Antirrhinum majus) and monocots (Secale cereale, Hordeum vulgare, Avena sativa), ranged in activity from 44 to 353 mumol X mg chl-1 X h-1. Studies with protoplast extracts of these species indicate that the enzyme is localized in the chloroplasts. Glycerate kinase was partially purified from Secale (rye, 288-fold) and Pisum (pea, 252-fold) chloroplasts by DEAE-cellulose chromatography, sucrose gradient centrifugation, and chromatofocusing. The enzymes from both species showed similar physical (Mr = 41,000, pI = 4.6-4.7) and kinetic (Km ATP = 655 to 692 microM, Km D-glycerate = 180-188 microM) properties. Activity of the enzyme was essentially insensitive to variations in assay pH from 6.4 to 9.0 and to energy charge variations from 0.4 to 1.0. Rye glycerate kinase was able to utilize UTP and GTP but less effectively than ATP. Neither ADP nor pyrophosphate served as an energy source. Mn2+, Co2+, Ca2+, and Sr2+ could function as metal cofactors, although to a lesser extent than Mg2+. Millimolar levels of sulfate were found to significantly inhibit the enzyme while similar concentrations of other anions (Cl-, NO-3, NO-2, and acetate) had little or no effect. << Less

  Arch Biochem Biophys 224:332-341(1983) [PubMed] [EuropePMC]