181 related articles for article (PubMed ID: 27531751)
1. Ligand-bound Structures and Site-directed Mutagenesis Identify the Acceptor and Secondary Binding Sites of Streptomyces coelicolor Maltosyltransferase GlgE.
Syson K; Stevenson CE; Miah F; Barclay JE; Tang M; Gorelik A; Rashid AM; Lawson DM; Bornemann S
J Biol Chem; 2016 Oct; 291(41):21531-21540. PubMed ID: 27531751
[TBL] [Abstract][Full Text] [Related]
2. Structure of Streptomyces maltosyltransferase GlgE, a homologue of a genetically validated anti-tuberculosis target.
Syson K; Stevenson CEM; Rejzek M; Fairhurst SA; Nair A; Bruton CJ; Field RA; Chater KF; Lawson DM; Bornemann S
J Biol Chem; 2011 Nov; 286(44):38298-38310. PubMed ID: 21914799
[TBL] [Abstract][Full Text] [Related]
3. Structural insight into how Streptomyces coelicolor maltosyl transferase GlgE binds α-maltose 1-phosphate and forms a maltosyl-enzyme intermediate.
Syson K; Stevenson CE; Rashid AM; Saalbach G; Tang M; Tuukkanen A; Svergun DI; Withers SG; Lawson DM; Bornemann S
Biochemistry; 2014 Apr; 53(15):2494-504. PubMed ID: 24689960
[TBL] [Abstract][Full Text] [Related]
4. Mycobacterium tuberculosis maltosyltransferase GlgE, a genetically validated antituberculosis target, is negatively regulated by Ser/Thr phosphorylation.
Leiba J; Syson K; Baronian G; Zanella-Cléon I; Kalscheuer R; Kremer L; Bornemann S; Molle V
J Biol Chem; 2013 Jun; 288(23):16546-16556. PubMed ID: 23609448
[TBL] [Abstract][Full Text] [Related]
5. Crystal structures of Mycobacterium tuberculosis GlgE and complexes with non-covalent inhibitors.
Lindenberger JJ; Veleti SK; Wilson BN; Sucheck SJ; Ronning DR
Sci Rep; 2015 Aug; 5():12830. PubMed ID: 26245983
[TBL] [Abstract][Full Text] [Related]
6. Structure of Mycobacterium thermoresistibile GlgE defines novel conformational states that contribute to the catalytic mechanism.
Mendes V; Blaszczyk M; Maranha A; Empadinhas N; Blundell TL
Sci Rep; 2015 Nov; 5():17144. PubMed ID: 26616850
[TBL] [Abstract][Full Text] [Related]
7. Modeling of a new tubercular maltosyl transferase, GlgE, study of its binding sites and virtual screening.
Sengupta S; Roy D; Bandyopadhyay S
Mol Biol Rep; 2014 Jun; 41(6):3549-60. PubMed ID: 24820953
[TBL] [Abstract][Full Text] [Related]
8. Synthesis of 2-deoxy-2,2-difluoro-α-maltosyl fluoride and its X-ray structure in complex with Streptomyces coelicolor GlgEI-V279S.
Thanna S; Lindenberger JJ; Gaitonde VV; Ronning DR; Sucheck SJ
Org Biomol Chem; 2015 Jul; 13(27):7542-50. PubMed ID: 26072729
[TBL] [Abstract][Full Text] [Related]
9. Developmental delay in a Streptomyces venezuelae glgE null mutant is associated with the accumulation of α-maltose 1-phosphate.
Miah F; Bibb MJ; Barclay JE; Findlay KC; Bornemann S
Microbiology (Reading); 2016 Jul; 162(7):1208-1219. PubMed ID: 27121970
[TBL] [Abstract][Full Text] [Related]
10. Synthesis of a poly-hydroxypyrolidine-based inhibitor of Mycobacterium tuberculosis GlgE.
Veleti SK; Lindenberger JJ; Thanna S; Ronning DR; Sucheck SJ
J Org Chem; 2014 Oct; 79(20):9444-50. PubMed ID: 25137149
[TBL] [Abstract][Full Text] [Related]
11. Synthesis of a C-phosphonate mimic of maltose-1-phosphate and inhibition studies on Mycobacterium tuberculosis GlgE.
Veleti SK; Lindenberger JJ; Ronning DR; Sucheck SJ
Bioorg Med Chem; 2014 Feb; 22(4):1404-11. PubMed ID: 24461562
[TBL] [Abstract][Full Text] [Related]
12. Zwitterionic pyrrolidene-phosphonates: inhibitors of the glycoside hydrolase-like phosphorylase Streptomyces coelicolor GlgEI-V279S.
Veleti SK; Petit C; Lindenberger JJ; Ronning DR; Sucheck SJ
Org Biomol Chem; 2017 May; 15(18):3884-3891. PubMed ID: 28422240
[TBL] [Abstract][Full Text] [Related]
13. Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
Uitdehaag JC; van Alebeek GJ; van Der Veen BA; Dijkhuizen L; Dijkstra BW
Biochemistry; 2000 Jul; 39(26):7772-80. PubMed ID: 10869182
[TBL] [Abstract][Full Text] [Related]
14. α-Glucan biosynthesis and the GlgE pathway in Mycobacterium tuberculosis.
Bornemann S
Biochem Soc Trans; 2016 Feb; 44(1):68-73. PubMed ID: 26862190
[TBL] [Abstract][Full Text] [Related]
15. A temperature-sensitive Mycobacterium smegmatis glgE mutation leads to a loss of GlgE enzyme activity and thermostability and the accumulation of α-maltose-1-phosphate.
Syson K; Batey SFD; Schindler S; Kalscheuer R; Bornemann S
Biochim Biophys Acta Gen Subj; 2021 Feb; 1865(2):129783. PubMed ID: 33166604
[TBL] [Abstract][Full Text] [Related]
16. Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway.
Kalscheuer R; Syson K; Veeraraghavan U; Weinrick B; Biermann KE; Liu Z; Sacchettini JC; Besra G; Bornemann S; Jacobs WR
Nat Chem Biol; 2010 May; 6(5):376-84. PubMed ID: 20305657
[TBL] [Abstract][Full Text] [Related]
17. Effects of essential carbohydrate/aromatic stacking interaction with Tyr100 and Phe259 on substrate binding of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp. 1011.
Haga K; Kanai R; Sakamoto O; Aoyagi M; Harata K; Yamane K
J Biochem; 2003 Dec; 134(6):881-91. PubMed ID: 14769878
[TBL] [Abstract][Full Text] [Related]
18. The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity.
Roujeinikova A; Raasch C; Burke J; Baker PJ; Liebl W; Rice DW
J Mol Biol; 2001 Sep; 312(1):119-31. PubMed ID: 11545590
[TBL] [Abstract][Full Text] [Related]
19. Crystal structure and characterization of the glycoside hydrolase family 62 α-L-arabinofuranosidase from Streptomyces coelicolor.
Maehara T; Fujimoto Z; Ichinose H; Michikawa M; Harazono K; Kaneko S
J Biol Chem; 2014 Mar; 289(11):7962-72. PubMed ID: 24482228
[TBL] [Abstract][Full Text] [Related]
20. Conversion of cyclodextrin glycosyltransferase into a starch hydrolase by directed evolution: the role of alanine 230 in acceptor subsite +1.
Leemhuis H; Rozeboom HJ; Wilbrink M; Euverink GJ; Dijkstra BW; Dijkhuizen L
Biochemistry; 2003 Jun; 42(24):7518-26. PubMed ID: 12809508
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]