메뉴 건너뛰기




Volumn 581, Issue 7, 2007, Pages 1297-1301

Properties of recombinant glycine decarboxylase P- and H-protein subunits from the cyanobacterium Synechocystis sp. strain PCC 6803

Author keywords

Cyanobacteria; Glycine decarboxylase; H protein; P protein; Synechocystis

Indexed keywords

GLYCINE; GLYCINE CLEAVAGE SYSTEM H PROTEIN; GLYCINE DEHYDROGENASE (DECARBOXYLATING); RECOMBINANT ENZYME;

EID: 33947429268     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.02.037     Document Type: Article
Times cited : (13)

References (26)
  • 2
    • 0034788469 scopus 로고    scopus 로고
    • Non-ketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis
    • Applegarth D.A., and Toone J.R. Non-ketotic hyperglycinemia (glycine encephalopathy): laboratory diagnosis. Mol. Genet. Metab. 74 (2001) 139-146
    • (2001) Mol. Genet. Metab. , vol.74 , pp. 139-146
    • Applegarth, D.A.1    Toone, J.R.2
  • 3
    • 0020482642 scopus 로고
    • Mutants of the cruciferous plant Arabidopsis thaliana lacking glycine decarboxylase activity
    • Somerville C.R., and Ogren W.L. Mutants of the cruciferous plant Arabidopsis thaliana lacking glycine decarboxylase activity. Biochem. J. 202 (1982) 373-380
    • (1982) Biochem. J. , vol.202 , pp. 373-380
    • Somerville, C.R.1    Ogren, W.L.2
  • 5
    • 13844255945 scopus 로고    scopus 로고
    • The glycine decarboxylase complex is not essential for the cyanobacterium Synechocystis sp. strain PCC 6803
    • Hagemann M., Vinnemeier J., Oberpichler I., Boldt R., and Bauwe H. The glycine decarboxylase complex is not essential for the cyanobacterium Synechocystis sp. strain PCC 6803. Plant Biol. 7 (2005) 15-22
    • (2005) Plant Biol. , vol.7 , pp. 15-22
    • Hagemann, M.1    Vinnemeier, J.2    Oberpichler, I.3    Boldt, R.4    Bauwe, H.5
  • 7
    • 0016194812 scopus 로고
    • Mechanism of the reversible glycine cleavage reaction in Arthrobacter globiformis. I. Purification and function of protein components required for the reaction
    • Kochi H., and Kikuchi G. Mechanism of the reversible glycine cleavage reaction in Arthrobacter globiformis. I. Purification and function of protein components required for the reaction. J. Biochem. 75 (1974) 1113-1127
    • (1974) J. Biochem. , vol.75 , pp. 1113-1127
    • Kochi, H.1    Kikuchi, G.2
  • 8
    • 0001339036 scopus 로고
    • Interaction between the component enzymes of the glycine decarboxylase multienzyme complex
    • Oliver D.J., Neuburger M., Bourguignon J., and Douce R. Interaction between the component enzymes of the glycine decarboxylase multienzyme complex. Plant Physiol. 94 (1990) 833-839
    • (1990) Plant Physiol. , vol.94 , pp. 833-839
    • Oliver, D.J.1    Neuburger, M.2    Bourguignon, J.3    Douce, R.4
  • 9
    • 0019333289 scopus 로고
    • The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein
    • Hiraga K., and Kikuchi G. The mitochondrial glycine cleavage system. Functional association of glycine decarboxylase and aminomethyl carrier protein. J. Biol. Chem. 255 (1980) 11671-11676
    • (1980) J. Biol. Chem. , vol.255 , pp. 11671-11676
    • Hiraga, K.1    Kikuchi, G.2
  • 10
    • 0034681906 scopus 로고    scopus 로고
    • Combined structural and biochemical analysis of the H-T complex in the glycine decarboxylase cycle: evidence for a destabilization mechanism of the H-protein
    • Guilhaudis L., Simorre J.P., Blackledge M., Marion D., Gans P., Neuburger M., and Douce R. Combined structural and biochemical analysis of the H-T complex in the glycine decarboxylase cycle: evidence for a destabilization mechanism of the H-protein. Biochemistry 39 (2000) 4259-4266
    • (2000) Biochemistry , vol.39 , pp. 4259-4266
    • Guilhaudis, L.1    Simorre, J.P.2    Blackledge, M.3    Marion, D.4    Gans, P.5    Neuburger, M.6    Douce, R.7
  • 11
    • 0007390697 scopus 로고    scopus 로고
    • Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies
    • Neuburger M., Polidori A.M., Pietre E., Faure M., Jourdain A., Bourguignon J., Pucci B., and Douce R. Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 1. Biochemical studies. Eur. J. Biochem. 267 (2000) 2882-2889
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2882-2889
    • Neuburger, M.1    Polidori, A.M.2    Pietre, E.3    Faure, M.4    Jourdain, A.5    Bourguignon, J.6    Pucci, B.7    Douce, R.8
  • 12
    • 0027975343 scopus 로고
    • X-ray structure determination at 2.6-Å resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves
    • Pares S., Cohen-Addad C., Sieker L., Neuburger M., and Douce R. X-ray structure determination at 2.6-Å resolution of a lipoate-containing protein: the H-protein of the glycine decarboxylase complex from pea leaves. Proc. Natl. Acad. Sci. USA 91 (1994) 4850-4853
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4850-4853
    • Pares, S.1    Cohen-Addad, C.2    Sieker, L.3    Neuburger, M.4    Douce, R.5
  • 13
    • 0034113956 scopus 로고    scopus 로고
    • Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 2. Crystal structures of H- and L-proteins
    • Faure M., Bourguignon J., Neuburger M., Macherel D., Sieker L., Ober R., Kahn R., Cohen-Addad C., and Douce R. Interaction between the lipoamide-containing H-protein and the lipoamide dehydrogenase (L-protein) of the glycine decarboxylase multienzyme system. 2. Crystal structures of H- and L-proteins. Eur. J. Biochem. 267 (2000) 2890-2898
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2890-2898
    • Faure, M.1    Bourguignon, J.2    Neuburger, M.3    Macherel, D.4    Sieker, L.5    Ober, R.6    Kahn, R.7    Cohen-Addad, C.8    Douce, R.9
  • 14
    • 23644451998 scopus 로고    scopus 로고
    • Crystal structure of human T-protein of glycine cleavage system at 2.0 Å resolution and its implication for understanding non-ketotic hyperglycinemia
    • Okamura-Ikeda K., Hosaka H., Yoshimura M., Yamashita E., Toma S., Nakagawa A., Fujiwara K., Motokawa Y., and Taniguchi H. Crystal structure of human T-protein of glycine cleavage system at 2.0 Å resolution and its implication for understanding non-ketotic hyperglycinemia. J. Mol. Biol. 351 (2005) 1146-1159
    • (2005) J. Mol. Biol. , vol.351 , pp. 1146-1159
    • Okamura-Ikeda, K.1    Hosaka, H.2    Yoshimura, M.3    Yamashita, E.4    Toma, S.5    Nakagawa, A.6    Fujiwara, K.7    Motokawa, Y.8    Taniguchi, H.9
  • 15
    • 18444417376 scopus 로고    scopus 로고
    • Structure of P-protein of the glycine cleavage system: implications for non-ketotic hyperglycinemia
    • Nakai T., Nakagawa N., Maoka N., Masui R., Kuramitsu S., and Kamiya N. Structure of P-protein of the glycine cleavage system: implications for non-ketotic hyperglycinemia. EMBO J. 24 (2005) 1536
    • (2005) EMBO J. , vol.24 , pp. 1536
    • Nakai, T.1    Nakagawa, N.2    Maoka, N.3    Masui, R.4    Kuramitsu, S.5    Kamiya, N.6
  • 16
    • 0037126071 scopus 로고    scopus 로고
    • Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus
    • Martin W., Rujan T., Richly E., Hansen A., Cornelsen S., Lins T., Leister D., Stoebe B., Hasegawa M., and Penny D. Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus. Proc. Natl. Acad. Sci. USA 99 (2002) 12246-12251
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12246-12251
    • Martin, W.1    Rujan, T.2    Richly, E.3    Hansen, A.4    Cornelsen, S.5    Lins, T.6    Leister, D.7    Stoebe, B.8    Hasegawa, M.9    Penny, D.10
  • 18
    • 0030614762 scopus 로고    scopus 로고
    • The stpA gene from Synechocystis sp. strain PCC 6803 encodes the glucosylglycerol-phosphate phosphatase involved in cyanobacterial osmotic response to salt shock
    • Hagemann M., Schoor A., Jeanjean R., Zuther E., and Joset F. The stpA gene from Synechocystis sp. strain PCC 6803 encodes the glucosylglycerol-phosphate phosphatase involved in cyanobacterial osmotic response to salt shock. J. Bacteriol. 179 (1997) 1727-1733
    • (1997) J. Bacteriol. , vol.179 , pp. 1727-1733
    • Hagemann, M.1    Schoor, A.2    Jeanjean, R.3    Zuther, E.4    Joset, F.5
  • 19
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 20
    • 0014010076 scopus 로고
    • Glycine metabolism. I. Properties of the system catalyzing the exchange of bicarbonate with the carboxyl-group of glycine in Peptococcus glycinophilus
    • Klein S.M., and Sagers R.D. Glycine metabolism. I. Properties of the system catalyzing the exchange of bicarbonate with the carboxyl-group of glycine in Peptococcus glycinophilus. J. Biol. Chem. 241 (1966) 197-205
    • (1966) J. Biol. Chem. , vol.241 , pp. 197-205
    • Klein, S.M.1    Sagers, R.D.2
  • 21
    • 23244450781 scopus 로고    scopus 로고
    • Monitoring cytosolic pH of carboxysome-deficient cells of Synechocystis sp PCC 6803 using fluorescence analysis
    • Berry S., Fischer J.H., Kruip J., Hauser M., and Wildner G.F. Monitoring cytosolic pH of carboxysome-deficient cells of Synechocystis sp PCC 6803 using fluorescence analysis. Plant Biol. 7 (2005) 342-347
    • (2005) Plant Biol. , vol.7 , pp. 342-347
    • Berry, S.1    Fischer, J.H.2    Kruip, J.3    Hauser, M.4    Wildner, G.F.5
  • 22
    • 0019333268 scopus 로고
    • The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria
    • Hiraga K., and Kikuchi G. The mitochondrial glycine cleavage system. Purification and properties of glycine decarboxylase from chicken liver mitochondria. J. Biol. Chem. 255 (1980) 11664-11670
    • (1980) J. Biol. Chem. , vol.255 , pp. 11664-11670
    • Hiraga, K.1    Kikuchi, G.2
  • 23
    • 0016265459 scopus 로고
    • Glycine metabolism by rat liver mitochondria: reconstitution of the reversible glycine cleavage system with partially purified protein components
    • Motokawa Y., and Kikuchi G. Glycine metabolism by rat liver mitochondria: reconstitution of the reversible glycine cleavage system with partially purified protein components. Arch. Biochem. Biophys. 164 (1974) 624-633
    • (1974) Arch. Biochem. Biophys. , vol.164 , pp. 624-633
    • Motokawa, Y.1    Kikuchi, G.2
  • 24
    • 0004672691 scopus 로고
    • Extraction and partial characterization of the glycine decarboxylase multienzyme complex from pea leaf mitochondria
    • Sarojini G., and Oliver D.J. Extraction and partial characterization of the glycine decarboxylase multienzyme complex from pea leaf mitochondria. Plant Physiol. 72 (1983) 194-199
    • (1983) Plant Physiol. , vol.72 , pp. 194-199
    • Sarojini, G.1    Oliver, D.J.2
  • 25
    • 0017280254 scopus 로고
    • Mechanism of reversible glycine cleavage reaction in Arthrobacter globiformis - function of lipoic acid in cleavage and synthesis of glycine
    • Kochi H., and Kikuchi G. Mechanism of reversible glycine cleavage reaction in Arthrobacter globiformis - function of lipoic acid in cleavage and synthesis of glycine. Arch. Biochem. Biophys. 173 (1976) 71-81
    • (1976) Arch. Biochem. Biophys. , vol.173 , pp. 71-81
    • Kochi, H.1    Kikuchi, G.2
  • 26
    • 0029915259 scopus 로고    scopus 로고
    • Expression, lipoylation and structure determination of recombinant pea H-protein in Escherichia coli
    • Macherel D., Bourguignon J., Forest E., Faure M., Cohen-Addad C., and Douce R. Expression, lipoylation and structure determination of recombinant pea H-protein in Escherichia coli. Eur. J. Biochem. 236 (1996) 27-33
    • (1996) Eur. J. Biochem. , vol.236 , pp. 27-33
    • Macherel, D.1    Bourguignon, J.2    Forest, E.3    Faure, M.4    Cohen-Addad, C.5    Douce, R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.