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Volumn 44, Issue , 2016, Pages 68-73

α-Glucan biosynthesis and the GlgE pathway in Mycobacterium tuberculosis

Author keywords

Capsule; GlgE pathway; Glycogen; Mycobacterium tuberculosis; Streptomyces; glucan

Indexed keywords

ALPHA GLUCAN; GLGE PROTEIN; GLUCAN; GLYCOGEN; TRANSFERASE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; GLYCOGEN SYNTHASE;

EID: 84958059900     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20150181     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 85069161983 scopus 로고    scopus 로고
    • Glycogen biosynthesis
    • (Schaechter, M., ed.), Elsevier, Oxford 5, CrossRef
    • Preiss, J. (2009) Glycogen biosynthesis. In The Encyclopedia of Microbiology (Schaechter, M., ed.), pp. 145-158, Elsevier, Oxford 5, CrossRef
    • (2009) The Encyclopedia of Microbiology , pp. 145-158
    • Preiss, J.1
  • 2
    • 79958171834 scopus 로고    scopus 로고
    • Unexpected and widespread connections between bacterial glycogen and trehalose metabolism
    • CrossRef PubMed
    • Chandra, G., Chater, K.F. and Bornemann, S. (2011) Unexpected and widespread connections between bacterial glycogen and trehalose metabolism. Microbiology 157, 1565-1572 CrossRef PubMed
    • (2011) Microbiology , vol.157 , pp. 1565-1572
    • Chandra, G.1    Chater, K.F.2    Bornemann, S.3
  • 3
    • 0014592361 scopus 로고
    • Environmental control of glycogen and lipid content of mycobacterium tuberculosis
    • PubMed
    • Antoine, A.D. and Tepper, B.S. (1969) Environmental control of glycogen and lipid content of Mycobacterium tuberculosis. J. Bacteriol. 100, 538-539 PubMed
    • (1969) J. Bacteriol. , vol.100 , pp. 538-539
    • Antoine, A.D.1    Tepper, B.S.2
  • 4
    • 0029118560 scopus 로고
    • Molecular composition of the outermost capsular material of the tubercle bacillus
    • CrossRef PubMed
    • Ortalo-Magné, A., Dupont, M.A., Lemassu, A., Andersen, A.B., Gounon, P. and Daffé, M. (1995) Molecular composition of the outermost capsular material of the tubercle bacillus. Microbiology 141, 1609-1620 CrossRef PubMed
    • (1995) Microbiology , vol.141 , pp. 1609-1620
    • Ortalo-Magné, A.1    Dupont, M.A.2    Lemassu, A.3    Andersen, A.B.4    Gounon, P.5    Daffé, M.6
  • 5
    • 45749097433 scopus 로고    scopus 로고
    • Comparative structural analyses of the α-glucan and glycogen from mycobacterium bovis
    • CrossRef PubMed
    • Dinadayala, P., Sambou, T., Daffé, M. and Lemassu, A. (2008) Comparative structural analyses of the α-glucan and glycogen from Mycobacterium bovis. Glycobiology 18, 502-508 CrossRef PubMed
    • (2008) Glycobiology , vol.18 , pp. 502-508
    • Dinadayala, P.1    Sambou, T.2    Daffé, M.3    Lemassu, A.4
  • 6
    • 0028097922 scopus 로고
    • Structural features of the exocellular polysaccharides of mycobacterium tuberculosis
    • CrossRef PubMed
    • Lemassu, A. and Daffé, M. (1994) Structural features of the exocellular polysaccharides of Mycobacterium tuberculosis. Biochem. J. 297, 351-357 CrossRef PubMed
    • (1994) Biochem. J. , vol.297 , pp. 351-357
    • Lemassu, A.1    Daffé, M.2
  • 7
    • 0014589473 scopus 로고
    • Characterization of glycogens from mycobacteria
    • CrossRef PubMed
    • Antoine, A.D. and Tepper, B.S. (1969) Characterization of glycogens from mycobacteria. Arch. Biochem. Biophys. 134, 207-213 CrossRef PubMed
    • (1969) Arch. Biochem. Biophys. , vol.134 , pp. 207-213
    • Antoine, A.D.1    Tepper, B.S.2
  • 8
    • 1842582661 scopus 로고    scopus 로고
    • Revisiting the structure of the anti-neoplastic glucans of mycobacterium bovis bacille calmette-guérin - structural analysis of the extracellular and boiling water extract-derived glucans of the vaccine substrains
    • CrossRef PubMed
    • Dinadayala, P., Lemassu, A., Granovski, P., Cérantola, S., Winter, N. and Daffé, M. (2004) Revisiting the structure of the anti-neoplastic glucans of Mycobacterium bovis Bacille Calmette-Guérin - Structural analysis of the extracellular and boiling water extract-derived glucans of the vaccine substrains. J. Biol. Chem. 279, 12369-12378 CrossRef PubMed
    • (2004) J. Biol. Chem. , vol.279 , pp. 12369-12378
    • Dinadayala, P.1    Lemassu, A.2    Granovski, P.3    Cérantola, S.4    Winter, N.5    Daffé, M.6
  • 10
    • 0015577056 scopus 로고
    • Levels of glycogen and trehalose in mycobacterium smegmatis and purification and properties of glycogen synthetase
    • PubMed
    • Elbein, A.D. and Mitchell, M. (1973) Levels of glycogen and trehalose in Mycobacterium smegmatis and purification and properties of glycogen synthetase. J. Bacteriol. 113, 863-873 PubMed
    • (1973) J. Bacteriol. , vol.113 , pp. 863-873
    • Elbein, A.D.1    Mitchell, M.2
  • 11
    • 84928694825 scopus 로고    scopus 로고
    • Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in mycobacterium tuberculosis
    • CrossRef
    • Asención Diez, M.D., Demonte, A.M., Syson, K., Arias, D.G., Gorelik, A., Guerrero, S.A., Bornemann, S. and Iglesias, A.A. (2015) Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis. BBA-Gen. Subjects 1850, 13-21 CrossRef
    • (2015) BBA-Gen. Subjects , vol.1850 , pp. 13-21
    • Asención Diez, M.D.1    Demonte, A.M.2    Syson, K.3    Arias, D.G.4    Gorelik, A.5    Guerrero, S.A.6    Bornemann, S.7    Iglesias, A.A.8
  • 13
    • 14444270344 scopus 로고    scopus 로고
    • Nonopsonic binding of mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent
    • PubMed
    • Cywes, C., Hoppe, H.C., Daffé, M. and Ehlers, M.R.W. (1997) Nonopsonic binding of Mycobacterium tuberculosis to complement receptor type 3 is mediated by capsular polysaccharides and is strain dependent. Infect. Immun. 65, 4258-4266 PubMed
    • (1997) Infect. Immun. , vol.65 , pp. 4258-4266
    • Cywes, C.1    Hoppe, H.C.2    Daffé, M.3    Ehlers, M.R.W.4
  • 14
    • 34447637113 scopus 로고    scopus 로고
    • Cell wall-associated α-glucan is instrumental for mycobacterium tuberculosis to block CD1 molecule expression and disable the function of dendritic cell derived from infected monocyte
    • CrossRef PubMed
    • Gagliardi, M.C., Lemassu, A., Teloni, R., Mariotti, S., Sargentini, V., Pardini, M., Daffé, M. and Nisini, R. (2007) Cell wall-associated α-glucan is instrumental for Mycobacterium tuberculosis to block CD1 molecule expression and disable the function of dendritic cell derived from infected monocyte. Cell Microbiol. 9, 2081-2092 CrossRef PubMed
    • (2007) Cell Microbiol. , vol.9 , pp. 2081-2092
    • Gagliardi, M.C.1    Lemassu, A.2    Teloni, R.3    Mariotti, S.4    Sargentini, V.5    Pardini, M.6    Daffé, M.7    Nisini, R.8
  • 15
    • 77949556108 scopus 로고    scopus 로고
    • Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: Involvement of mycobacterial capsular polysaccharides in host imune modulation
    • CrossRef PubMed
    • Geurtsen, J., Chedammi, S., Mesters, J., Cot, M., Driessen, N.N., Sambou, T., Kakutani, R., Ummels, R., Maaskant, J., Takata, H. et al. (2009) Identification of mycobacterial alpha-glucan as a novel ligand for DC-SIGN: involvement of mycobacterial capsular polysaccharides in host imune modulation. J. Immunol. 183, 5221-5231 CrossRef PubMed
    • (2009) J. Immunol. , vol.183 , pp. 5221-5231
    • Geurtsen, J.1    Chedammi, S.2    Mesters, J.3    Cot, M.4    Driessen, N.N.5    Sambou, T.6    Kakutani, R.7    Ummels, R.8    Maaskant, J.9    Takata, H.10
  • 18
    • 77951245174 scopus 로고    scopus 로고
    • Last step in the conversion of trehalose to glycogen: A mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen
    • CrossRef PubMed
    • Elbein, A.D., Pastuszak, I., Tackett, A.J., Wilson, T. and Pan, Y.T. (2010) Last step in the conversion of trehalose to glycogen: a mycobacterial enzyme that transfers maltose from maltose 1-phosphate to glycogen. J. Biol. Chem. 285, 9803-9812 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 9803-9812
    • Elbein, A.D.1    Pastuszak, I.2    Tackett, A.J.3    Wilson, T.4    Pan, Y.T.5
  • 19
    • 8644245771 scopus 로고    scopus 로고
    • Trehalose synthase of mycobacterium smegmatis - purification, cloning, expression, and properties of the enzyme
    • CrossRef PubMed
    • Pan, Y.T., Edavana, V.K., Jourdian, W.J., Edmondson, R., Carroll, J.D., Pastuszak, I. and Elbein, A.D. (2004) Trehalose synthase of Mycobacterium smegmatis - purification, cloning, expression, and properties of the enzyme. Eur. J. Biochem. 271, 4259-4269 CrossRef PubMed
    • (2004) Eur. J. Biochem. , vol.271 , pp. 4259-4269
    • Pan, Y.T.1    Edavana, V.K.2    Jourdian, W.J.3    Edmondson, R.4    Carroll, J.D.5    Pastuszak, I.6    Elbein, A.D.7
  • 20
    • 0038359368 scopus 로고    scopus 로고
    • Mechanistic study of the intramolecular conversion of maltose to trehalose by thermus caldophilus GK24 trehalose synthase
    • CrossRef PubMed
    • Koh, S., Kim, J., Shin, H.J., Lee, D., Bae, J., Kim, D. and Lee, D.S. (2003) Mechanistic study of the intramolecular conversion of maltose to trehalose by Thermus caldophilus GK24 trehalose synthase. Carbohydr. Res. 338, 1339-1343 CrossRef PubMed
    • (2003) Carbohydr. Res. , vol.338 , pp. 1339-1343
    • Koh, S.1    Kim, J.2    Shin, H.J.3    Lee, D.4    Bae, J.5    Kim, D.6    Lee, D.S.7
  • 21
    • 80053907355 scopus 로고    scopus 로고
    • Mechanistic analysis of trehalose synthase from mycobacterium smegmatis
    • CrossRef PubMed
    • Zhang, R., Pan, Y.T., He, S.M., Lam, M., Brayer, G.D., Elbein, A.D. and Withers, S.G. (2011) Mechanistic analysis of trehalose synthase from Mycobacterium smegmatis. J. Biol. Chem. 286, 35601-35609 CrossRef PubMed
    • (2011) J. Biol. Chem. , vol.286 , pp. 35601-35609
    • Zhang, R.1    Pan, Y.T.2    He, S.M.3    Lam, M.4    Brayer, G.D.5    Elbein, A.D.6    Withers, S.G.7
  • 22
    • 84880926719 scopus 로고    scopus 로고
    • The structure of the mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode
    • CrossRef PubMed
    • Caner, S., Nham, N., Aguda, A., Zhang, R., Pan, Y.T., Withers, S.G. and Brayer, G.D. (2013) The structure of the Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding mode. Glycobiology 23, 1075-1083 CrossRef PubMed
    • (2013) Glycobiology , vol.23 , pp. 1075-1083
    • Caner, S.1    Nham, N.2    Aguda, A.3    Zhang, R.4    Pan, Y.T.5    Withers, S.G.6    Brayer, G.D.7
  • 23
    • 84886522329 scopus 로고    scopus 로고
    • Synthesis of α-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and maltokinase Pep2
    • CrossRef PubMed
    • Roy, R., Usha, V., Kermani, A., Scott, D.J., Hyde, E.I., Besra, G.S., Alderwick, L.J. and Fuetterer, K. (2013) Synthesis of α-glucan in mycobacteria involves a hetero-octameric complex of trehalose synthase TreS and maltokinase Pep2. ACS Chem. Biol. 8, 2245-2255 CrossRef PubMed
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2245-2255
    • Roy, R.1    Usha, V.2    Kermani, A.3    Scott, D.J.4    Hyde, E.I.5    Besra, G.S.6    Alderwick, L.J.7    Fuetterer, K.8
  • 24
    • 84916926032 scopus 로고    scopus 로고
    • Structures of trehalose synthase from deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization
    • CrossRef PubMed
    • Wang, Y.-L., Chow, S.-Y., Lin, Y.-T., Hsieh, Y.-C., Lee, G.-C. and Liaw, S.-H. (2014) Structures of trehalose synthase from Deinococcus radiodurans reveal that a closed conformation is involved in catalysis of the intramolecular isomerization. Acta Crystallogr. D Biol. Crystallogr. 70, 3144-3154 CrossRef PubMed
    • (2014) Acta Crystallogr. D Biol. Crystallogr. , vol.70 , pp. 3144-3154
    • Wang, Y.-L.1    Chow, S.-Y.2    Lin, Y.-T.3    Hsieh, Y.-C.4    Lee, G.-C.5    Liaw, S.-H.6
  • 25
    • 84923045274 scopus 로고    scopus 로고
    • Homotypic dimerization of a maltose kinase for molecular scaffolding
    • Li, J., Guan, X., Shaw, N., Chen, W., Dong, Y., Xu, X., Li, X. and Rao, Z. (2014) Homotypic dimerization of a maltose kinase for molecular scaffolding. Sci. Rep. 4, 1-8
    • (2014) Sci. Rep. , vol.4 , pp. 1-8
    • Li, J.1    Guan, X.2    Shaw, N.3    Chen, W.4    Dong, Y.5    Xu, X.6    Li, X.7    Rao, Z.8
  • 27
    • 0030591439 scopus 로고    scopus 로고
    • Maltokinase (ATP:maltose 1-phosphotransferase) from actinoplanes sp: Demonstration of enzyme activity and characterization of the reaction product
    • CrossRef PubMed
    • Drepper, A., Peitzmann, R. and Pape, H. (1996) Maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes sp: demonstration of enzyme activity and characterization of the reaction product. FEBS Lett. 388, 177-179 CrossRef PubMed
    • (1996) FEBS Lett. , vol.388 , pp. 177-179
    • Drepper, A.1    Peitzmann, R.2    Pape, H.3
  • 28
    • 6344238950 scopus 로고    scopus 로고
    • Isolation of mak1 from actinoplanes missouriensis and evidence that pep2 from streptomyces coelicolor is a maltokinase
    • CrossRef PubMed
    • Jarling, M., Cauvet, T., Grundmeier, M., Kuhnert, K. and Pape, H. (2004) Isolation of mak1 from Actinoplanes missouriensis and evidence that Pep2 from Streptomyces coelicolor is a maltokinase. J. Basic Microbiol. 44, 360-373 CrossRef PubMed
    • (2004) J. Basic Microbiol. , vol.44 , pp. 360-373
    • Jarling, M.1    Cauvet, T.2    Grundmeier, M.3    Kuhnert, K.4    Pape, H.5
  • 29
    • 77952699926 scopus 로고    scopus 로고
    • Biochemical characterization of the maltokinase from mycobacterium bovis BCG
    • CrossRef
    • Mendes, V., Maranha, A., Lamosa, P., da Costa, M.S. and Empadinhas, N. (2010) Biochemical characterization of the maltokinase from Mycobacterium bovis BCG. BMC Biochem 11, CrossRef
    • (2010) BMC Biochem , vol.11
    • Mendes, V.1    Maranha, A.2    Lamosa, P.3    Da Costa, M.S.4    Empadinhas, N.5
  • 30
    • 0141956316 scopus 로고    scopus 로고
    • Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from actinoplanes missouriensis
    • CrossRef PubMed
    • Niehues, B., Jossek, R., Kramer, U., Koch, A., Jarling, M., Schroder, W. and Pape, H. (2003) Isolation and characterization of maltokinase (ATP:maltose 1-phosphotransferase) from Actinoplanes missouriensis. Arch. Microbiol. 180, 233-239 CrossRef PubMed
    • (2003) Arch. Microbiol. , vol.180 , pp. 233-239
    • Niehues, B.1    Jossek, R.2    Kramer, U.3    Koch, A.4    Jarling, M.5    Schroder, W.6    Pape, H.7
  • 31
    • 33751429907 scopus 로고    scopus 로고
    • Expression and characterization of α-(1,4)-glucan branching enzyme Rv1326c of mycobacterium tuberculosis H37Rv
    • CrossRef PubMed
    • Garg, S.K., Alam, M.S., Kishan, K.V. R. and Agrawal, P. (2007) Expression and characterization of α-(1,4)-glucan branching enzyme Rv1326c of Mycobacterium tuberculosis H37Rv. Protein Expr. Purif. 51, 198-208 CrossRef PubMed
    • (2007) Protein Expr. Purif. , vol.51 , pp. 198-208
    • Garg, S.K.1    Alam, M.S.2    Kishan, K.V.R.3    Agrawal, P.4
  • 32
    • 77954240010 scopus 로고    scopus 로고
    • Crystal structure of full length mycobacterium tuberculosis H37Rv glycogen branching enzyme: Insights of N-terminal β-sandwich in substrate specificity and enzymatic activity
    • CrossRef PubMed
    • Pal, K., Kumar, S., Sharma, S., Garg, S.K., Alam, M.S., Xu, H.E., Agrawal, P. and Swaminathan, K. (2010) Crystal structure of full length Mycobacterium tuberculosis H37Rv glycogen branching enzyme: insights of N-terminal β-sandwich in substrate specificity and enzymatic activity. J. Biol. Chem. 285, 20897-20903 CrossRef PubMed
    • (2010) J. Biol. Chem. , vol.285 , pp. 20897-20903
    • Pal, K.1    Kumar, S.2    Sharma, S.3    Garg, S.K.4    Alam, M.S.5    Xu, H.E.6    Agrawal, P.7    Swaminathan, K.8
  • 34
    • 84876459348 scopus 로고    scopus 로고
    • Flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria
    • CrossRef PubMed
    • Miah, F., Koliwer-Brandl, H., Rejzek, M., Field, R.A., Kalscheuer, R. and Bornemann, S. (2013) Flux through trehalose synthase flows from trehalose to the alpha anomer of maltose in mycobacteria. Chem. Biol. 20, 487-492 CrossRef PubMed
    • (2013) Chem. Biol. , vol.20 , pp. 487-492
    • Miah, F.1    Koliwer-Brandl, H.2    Rejzek, M.3    Field, R.A.4    Kalscheuer, R.5    Bornemann, S.6
  • 35
    • 84940709339 scopus 로고    scopus 로고
    • Genetics of mycobacterial trehalose metabolism
    • Kalscheuer, R. and Koliwer-Brandl, H. (2014) Genetics of mycobacterial trehalose metabolism. Microbiol. Spectr. 2, 1-15
    • (2014) Microbiol. Spectr. , vol.2 , pp. 1-15
    • Kalscheuer, R.1    Koliwer-Brandl, H.2
  • 36
    • 79954442657 scopus 로고    scopus 로고
    • The significance of GlgE as a new target for tuberculosis
    • CrossRef PubMed
    • Kalscheuer, R. and Jacobs, W.R. (2010) The significance of GlgE as a new target for tuberculosis. Drug News Perspect. 23, 619-624 CrossRef PubMed
    • (2010) Drug News Perspect. , vol.23 , pp. 619-624
    • Kalscheuer, R.1    Jacobs, W.R.2
  • 37
    • 84893770146 scopus 로고    scopus 로고
    • Synthesis of a C-phosphonate mimic of maltose-1-phosphate and inhibition studies on mycobacterium tuberculosis GlgE
    • CrossRef PubMed
    • Veleti, S.K., Lindenberger, J.J., Ronning, D.R. and Sucheck, S.J. (2014) Synthesis of a C-phosphonate mimic of maltose-1-phosphate and inhibition studies on Mycobacterium tuberculosis GlgE. Bioorg. Med. Chem. 22, 1404-1411 CrossRef PubMed
    • (2014) Bioorg. Med. Chem. , vol.22 , pp. 1404-1411
    • Veleti, S.K.1    Lindenberger, J.J.2    Ronning, D.R.3    Sucheck, S.J.4
  • 38
    • 84908251249 scopus 로고    scopus 로고
    • Synthesis of a poly-hydroxypyrolidine-based inhibitor of mycobacterium tuberculosis GlgE
    • CrossRef PubMed
    • Veleti, S.K., Lindenberger, J.J., Thanna, S., Ronning, D.R. and Sucheck, S.J. (2014) Synthesis of a poly-hydroxypyrolidine-based inhibitor of Mycobacterium tuberculosis GlgE. J. Org. Chem. 79, 9444-9450 CrossRef PubMed
    • (2014) J. Org. Chem. , vol.79 , pp. 9444-9450
    • Veleti, S.K.1    Lindenberger, J.J.2    Thanna, S.3    Ronning, D.R.4    Sucheck, S.J.5
  • 39
    • 84902368566 scopus 로고    scopus 로고
    • Modeling of a new tubercular maltosyl transferase, GlgE, study of its binding sites and virtual screening
    • CrossRef PubMed
    • Sengupta, S., Roy, D. and Bandyopadhyay, S. (2014) Modeling of a new tubercular maltosyl transferase, GlgE, study of its binding sites and virtual screening. Mol. Biol. Rep. 41, 3549-3560 CrossRef PubMed
    • (2014) Mol. Biol. Rep. , vol.41 , pp. 3549-3560
    • Sengupta, S.1    Roy, D.2    Bandyopadhyay, S.3
  • 40
    • 84958040310 scopus 로고    scopus 로고
    • Structural insight into mycobacterium tuberculosis maltosyl transferase inhibitors: Pharmacophore-based virtual screening, docking, and molecular dynamics simulations
    • CrossRef
    • Sengupta, S., Roy, D. and Bandyopadhyay, S. (2015) Structural insight into Mycobacterium tuberculosis maltosyl transferase inhibitors: pharmacophore-based virtual screening, docking, and molecular dynamics simulations. J. Biol. Struct. Dynam. 11, 1-12 CrossRef
    • (2015) J. Biol. Struct. Dynam. , vol.11 , pp. 1-12
    • Sengupta, S.1    Roy, D.2    Bandyopadhyay, S.3
  • 41
    • 84912064647 scopus 로고    scopus 로고
    • Structure-based design of inhibitors against maltosyltransferase GlgE
    • CrossRef
    • Billones, J.B. and Valle, A.M.F. (2014) Structure-based design of inhibitors against maltosyltransferase GlgE. Orient. J. Chem. 30, 1137-1145 CrossRef
    • (2014) Orient. J. Chem. , vol.30 , pp. 1137-1145
    • Billones, J.B.1    Valle, A.M.F.2
  • 42
    • 84920520297 scopus 로고    scopus 로고
    • Discovery of mycobacterium tuberculosis α-1,4-glucan branching enzyme (GlgB) inhibitors by structure- and ligand-based virtual screening
    • CrossRef PubMed
    • Dkhar, H.K., Gopalsamy, A., Loharch, S., Kaur, A., Bhutani, I., Saminathan, K., Bhagyaraj, E., Chandra, V., Swaminathan, K., Agrawal, P. et al. (2015) Discovery of Mycobacterium tuberculosis α-1,4-glucan branching enzyme (GlgB) inhibitors by structure- and ligand-based virtual screening. J. Biol. Chem. 290, 76-89 CrossRef PubMed
    • (2015) J. Biol. Chem. , vol.290 , pp. 76-89
    • Dkhar, H.K.1    Gopalsamy, A.2    Loharch, S.3    Kaur, A.4    Bhutani, I.5    Saminathan, K.6    Bhagyaraj, E.7    Chandra, V.8    Swaminathan, K.9    Agrawal, P.10
  • 43
    • 0038653402 scopus 로고    scopus 로고
    • ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis
    • CrossRef PubMed
    • Ballicora, M.A., Iglesias, A.A. and Preiss, J. (2003) ADP-glucose pyrophosphorylase, a regulatory enzyme for bacterial glycogen synthesis. Microbiol. Mol. Biol. Rev. 67, 213-225 CrossRef PubMed
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 213-225
    • Ballicora, M.A.1    Iglesias, A.A.2    Preiss, J.3
  • 44
    • 84878749203 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated anti-tuberculosis target, is negatively regulated by Ser/Thr phosphorylation
    • CrossRef PubMed
    • Leiba, J., Syson, K., Baronian, G., Zanella-Cleon, I., Kalscheuer, R., Kremer, L., Bornemann, S. and Molle, V. (2013) Mycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated anti-tuberculosis target, is negatively regulated by Ser/Thr phosphorylation. J. Biol. Chem. 288, 16546-16556 CrossRef PubMed
    • (2013) J. Biol. Chem. , vol.288 , pp. 16546-16556
    • Leiba, J.1    Syson, K.2    Baronian, G.3    Zanella-Cleon, I.4    Kalscheuer, R.5    Kremer, L.6    Bornemann, S.7    Molle, V.8
  • 46
    • 84899457053 scopus 로고    scopus 로고
    • Structural insight into how streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate
    • CrossRef PubMed
    • Syson, K., Stevenson, C.E.M., Rashid, A.M., Saalbach, G., Tang, M., Tuukkanen, A., Svergun, D.I., Withers, S.G., Lawson, D.M. and Bornemann, S. (2014) Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate. Biochemistry 53, 2494-2504 CrossRef PubMed
    • (2014) Biochemistry , vol.53 , pp. 2494-2504
    • Syson, K.1    Stevenson, C.E.M.2    Rashid, A.M.3    Saalbach, G.4    Tang, M.5    Tuukkanen, A.6    Svergun, D.I.7    Withers, S.G.8    Lawson, D.M.9    Bornemann, S.10
  • 47
    • 84936853275 scopus 로고    scopus 로고
    • Synthesis of 2-deoxy-2,2-difluoro-α-maltosyl fluoride and its X-ray structure in complex with streptomyces coelicolor GlgEI-V279S
    • CrossRef PubMed
    • Thanna, S., Lindenberger, J.J., Gaitonde, V.V., Ronning, D.R. and Sucheck, S.J. (2015) Synthesis of 2-deoxy-2,2-difluoro-α-maltosyl fluoride and its X-ray structure in complex with Streptomyces coelicolor GlgEI-V279S. Org. Biomol. Chem. 13, 7542-7550 CrossRef PubMed
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 7542-7550
    • Thanna, S.1    Lindenberger, J.J.2    Gaitonde, V.V.3    Ronning, D.R.4    Sucheck, S.J.5
  • 48
    • 84938824086 scopus 로고    scopus 로고
    • Crystal structures of mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors
    • CrossRef
    • Lindenberger, J.J., Kumar Veleti, S., Wilson, B.N., Sucheck, S.J. and Ronning, D.R. (2015) Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors. Sci Rep. 5, CrossRef
    • (2015) Sci Rep. , vol.5
    • Lindenberger, J.J.1    Kumar Veleti, S.2    Wilson, B.N.3    Sucheck, S.J.4    Ronning, D.R.5
  • 49
    • 0014198207 scopus 로고
    • Identification of α,α-trehalose 6,6′-dimannosylphosphate and α-maltose 1-phosphate of mycobacteria
    • PubMed
    • Narumi, K. and Tsumita, T. (1967) Identification of α,α-trehalose 6,6′-dimannosylphosphate and α-maltose 1-phosphate of mycobacteria. J. Biol. Chem. 242, 2233-2239 PubMed
    • (1967) J. Biol. Chem. , vol.242 , pp. 2233-2239
    • Narumi, K.1    Tsumita, T.2
  • 50
    • 4944260924 scopus 로고    scopus 로고
    • Production of maltodextrin 1-phosphate by fibrobacter succinogenes S85
    • CrossRef PubMed
    • Nouaille, R., Matulova, M., Delort, A.M. and Forano, E. (2004) Production of maltodextrin 1-phosphate by Fibrobacter succinogenes S85. FEBS Lett. 576, 226-230 CrossRef PubMed
    • (2004) FEBS Lett. , vol.576 , pp. 226-230
    • Nouaille, R.1    Matulova, M.2    Delort, A.M.3    Forano, E.4
  • 51
    • 18944363557 scopus 로고    scopus 로고
    • Oligosaccharide synthesis in fibrobacter succinogenes S85 and its modulation by the substrate
    • CrossRef PubMed
    • Nouaille, R., Matulova, M., Delort, A.M. and Forano, E. (2005) Oligosaccharide synthesis in Fibrobacter succinogenes S85 and its modulation by the substrate. FEBS J. 272, 2416-2427 CrossRef PubMed
    • (2005) FEBS J. , vol.272 , pp. 2416-2427
    • Nouaille, R.1    Matulova, M.2    Delort, A.M.3    Forano, E.4


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