메뉴 건너뛰기




Volumn 64, Issue 7, 2012, Pages 649-658

Lyase activity of glycogen synthase: Is an elimination/addition mechanism a possible reaction pathway for retaining glycosyltransferases?

Author keywords

1,5 anhydro D fructose; catalytic mechanism; glycogen synthase; protein structure; retaining glycosyltransferase

Indexed keywords

CARBON; FRUCTOSE; GLUCOSE; GLYCOGEN SYNTHASE; GLYCOSYLTRANSFERASE; LYASE; OXYGEN; PHOSPHATE; URIDINE DIPHOSPHATE;

EID: 84862563880     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1048     Document Type: Article
Times cited : (11)

References (43)
  • 5
    • 33845584643 scopus 로고    scopus 로고
    • Chemical rescue of α3-galactosyltransferase: Implications in the mechanism of retaining glycosyltransferases
    • Monegal, A., and, Planas, A., (2006) Chemical rescue of α3-galactosyltransferase: implications in the mechanism of retaining glycosyltransferases. J. Am. Chem. Soc. 128, 16030-16031.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16030-16031
    • Monegal, A.1    Planas, A.2
  • 6
    • 3142615417 scopus 로고    scopus 로고
    • Intermediate trapping on a mutant retaining α-galactosyltransferase identifies an unexpected aspartate residue
    • Lairson, L. L., Chiu, C. P. C., Ly, H. D., He, S., Wakarchuk, W. W., Strynadka, N. C. J., and, Withers, S. G., (2004) Intermediate trapping on a mutant retaining α-galactosyltransferase identifies an unexpected aspartate residue. J. Biol. Chem. 279, 28339-28344.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28339-28344
    • Lairson, L.L.1    Chiu, C.P.C.2    Ly, H.D.3    He, S.4    Wakarchuk, W.W.5    Strynadka, N.C.J.6    Withers, S.G.7
  • 7
    • 79953884100 scopus 로고    scopus 로고
    • Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases
    • Soya, N., Fang, Y., Palcic, M. M., and, Klassen, J. S., (2010) Trapping and characterization of covalent intermediates of mutant retaining glycosyltransferases. Glycobiology 21, 547-552.
    • (2010) Glycobiology , vol.21 , pp. 547-552
    • Soya, N.1    Fang, Y.2    Palcic, M.M.3    Klassen, J.S.4
  • 8
    • 0037161293 scopus 로고    scopus 로고
    • Mechanistic studies of a retaining α-galactosyltransferase from Neisseria meningitidis
    • Ly, H. D., Lougheed, B., Wakarchuk, W. W., and, Withers, S. G., (2002) Mechanistic studies of a retaining α-galactosyltransferase from Neisseria meningitidis. Biochemistry 41, 5075-5085.
    • (2002) Biochemistry , vol.41 , pp. 5075-5085
    • Ly, H.D.1    Lougheed, B.2    Wakarchuk, W.W.3    Withers, S.G.4
  • 9
    • 0001403866 scopus 로고
    • Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethanol
    • Sinnott, M. L., and, Jencks, W. P., (1980) Solvolysis of D-glucopyranosyl derivatives in mixtures of ethanol and 2,2,2-trifluoroethanol. J. Am. Chem. Soc. 102: 2026-2032.
    • (1980) J. Am. Chem. Soc. , vol.102 , pp. 2026-2032
    • Sinnott, M.L.1    Jencks, W.P.2
  • 10
    • 0022517513 scopus 로고
    • Mechanism of the phosphorylase reaction. Utilization of D-gluco-hept-1-enitol in the absence of primer
    • Klein, H. W., Im, M. J., and, Palm, D., (1986) Mechanism of the phosphorylase reaction. Utilization of D-gluco-hept-1-enitol in the absence of primer. Eur. J. Biochem. 157, 107-114.
    • (1986) Eur. J. Biochem. , vol.157 , pp. 107-114
    • Klein, H.W.1    Im, M.J.2    Palm, D.3
  • 11
    • 0025017865 scopus 로고
    • The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis
    • Palm, D., Klein, H. W., Schinzel, R., Buehner, M., and, Helmreich, E. J., (1990) The role of pyridoxal 5'-phosphate in glycogen phosphorylase catalysis. Biochemistry 29, 1099-1107.
    • (1990) Biochemistry , vol.29 , pp. 1099-1107
    • Palm, D.1    Klein, H.W.2    Schinzel, R.3    Buehner, M.4    Helmreich, E.J.5
  • 12
    • 0035150891 scopus 로고    scopus 로고
    • Sweet secrets of synthesis
    • Davies, G. J., (2001) Sweet secrets of synthesis. Nat. Struct. Biol. 8, 98-100.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 98-100
    • Davies, G.J.1
  • 13
    • 0035151023 scopus 로고    scopus 로고
    • Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs
    • Persson, K., Ly, H. D., Dieckelmann, M., Wakarchuk, W. W., Withers, S. G., and, Strynadka, N. C., (2001) Crystal structure of the retaining galactosyltransferase LgtC from Neisseria meningitidis in complex with donor and acceptor sugar analogs. Nat. Struct. Biol. 8, 166-175.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 166-175
    • Persson, K.1    Ly, H.D.2    Dieckelmann, M.3    Wakarchuk, W.W.4    Withers, S.G.5    Strynadka, N.C.6
  • 14
    • 1542268957 scopus 로고    scopus 로고
    • Molecular modeling insights into the catalytic mechanism of the retaining galactosyltransferase LgtC
    • Tvaroska, I., (2004) Molecular modeling insights into the catalytic mechanism of the retaining galactosyltransferase LgtC. Carbohydr. Res. 339, 1007-1014.
    • (2004) Carbohydr. Res. , vol.339 , pp. 1007-1014
    • Tvaroska, I.1
  • 16
    • 0036909547 scopus 로고    scopus 로고
    • Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA
    • Gibson, R. P., Turkenburg, J. P., Charnock, S. J., Lloyd, R., and, Davies, G. J., (2002) Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA. Chem. Biol. 9, 1337-1346.
    • (2002) Chem. Biol. , vol.9 , pp. 1337-1346
    • Gibson, R.P.1    Turkenburg, J.P.2    Charnock, S.J.3    Lloyd, R.4    Davies, G.J.5
  • 18
    • 70350538953 scopus 로고    scopus 로고
    • Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate
    • Goedl, C., and, Nidetzky, B., (2009) Sucrose phosphorylase harbouring a redesigned, glycosyltransferase-like active site exhibits retaining glucosyl transfer in the absence of a covalent intermediate. Chem. BioChem. 10, 2333-2337.
    • (2009) Chem. BioChem. , vol.10 , pp. 2333-2337
    • Goedl, C.1    Nidetzky, B.2
  • 19
    • 80053917641 scopus 로고    scopus 로고
    • The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications
    • Zheng, Y., Anderson, S., Zhang, Y., and, Garavito, R. M., (2011) The structure of sucrose synthase-1 from Arabidopsis thaliana and its functional implications. J. Biol. Chem. 286, 36108-36118.
    • (2011) J. Biol. Chem. , vol.286 , pp. 36108-36118
    • Zheng, Y.1    Anderson, S.2    Zhang, Y.3    Garavito, R.M.4
  • 20
    • 80855133537 scopus 로고    scopus 로고
    • The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: Evidence for a short-lived oxocarbenium-like species
    • Ardèvol, A., and, Rovira, C., (2011) The molecular mechanism of enzymatic glycosyl transfer with retention of configuration: evidence for a short-lived oxocarbenium-like species. Angew. Chem. Int. Ed. Engl. 50, 10897-10901.
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 10897-10901
    • Ardèvol, A.1    Rovira, C.2
  • 21
  • 22
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: Homologous enzymes catalyze glycogen synthesis and degradation
    • Buschiazzo, A., Ugalde, J. E., Guerin, M. E., Shepard, W., Ugalde, R. A., and, Alzari, P. M., (2004) Crystal structure of glycogen synthase: homologous enzymes catalyze glycogen synthesis and degradation. EMBO J. 23, 3196-3205.
    • (2004) EMBO J. , vol.23 , pp. 3196-3205
    • Buschiazzo, A.1    Ugalde, J.E.2    Guerin, M.E.3    Shepard, W.4    Ugalde, R.A.5    Alzari, P.M.6
  • 23
    • 33646338642 scopus 로고    scopus 로고
    • Crystal structure of an archaeal glycogen synthase: Insights into oligomerization and substrate binding of eukaryotic glycogen synthases
    • Horcajada, C., Guinovart, J. J., Fita, I., and, Ferrer, J. C., (2006) Crystal structure of an archaeal glycogen synthase: insights into oligomerization and substrate binding of eukaryotic glycogen synthases. J. Biol. Chem. 281, 2923-2931.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2923-2931
    • Horcajada, C.1    Guinovart, J.J.2    Fita, I.3    Ferrer, J.C.4
  • 24
    • 67650516761 scopus 로고    scopus 로고
    • The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase
    • Sheng, F., Jia, X., Yep, A., Preiss, J., and, Geiger, J. H., (2009) The crystal structures of the open and catalytically competent closed conformation of Escherichia coli glycogen synthase. J. Biol. Chem. 284, 17796-17807.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17796-17807
    • Sheng, F.1    Jia, X.2    Yep, A.3    Preiss, J.4    Geiger, J.H.5
  • 25
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763.
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 26
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P., and, Cowtan, K., (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126-2132.
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 27
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and, Thornton, J. M., (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26, 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 30
    • 33846231909 scopus 로고    scopus 로고
    • Analysis of sugars in environmental samples by gas chromatography-mass spectrometry
    • Medeiros, P. M., Simoneit, B. R., (2007) Analysis of sugars in environmental samples by gas chromatography-mass spectrometry. J. Chromatogr. A. 1141, 271-278.
    • (2007) J. Chromatogr. A. , vol.1141 , pp. 271-278
    • Medeiros, P.M.1    Simoneit, B.R.2
  • 31
    • 59649093199 scopus 로고    scopus 로고
    • The anhydrofructose pathway of glycogen catabolism
    • Yu, S., (2008) The anhydrofructose pathway of glycogen catabolism. IUBMB Life 60, 798-809.
    • (2008) IUBMB Life , vol.60 , pp. 798-809
    • Yu, S.1
  • 32
    • 0037071150 scopus 로고    scopus 로고
    • 1,5-Anhydro-D-fructose; A versatile chiral building block: Biochemistry and chemistry
    • Andersen, S. M., Lundt, I., Marcussen, J., and, Yu, S., (2002) 1,5-Anhydro-D-fructose; a versatile chiral building block: biochemistry and chemistry. Carbohydr. Res. 337, 873-890.
    • (2002) Carbohydr. Res. , vol.337 , pp. 873-890
    • Andersen, S.M.1    Lundt, I.2    Marcussen, J.3    Yu, S.4
  • 33
    • 76349106696 scopus 로고    scopus 로고
    • Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors
    • Martinez-,.
    • Errey, J. C., Lee, S. S., Gibson, R. P., Martinez-, Fleites, C., Barry, C. S., Jung, P. M., O'Sullivan, A. C., Davis, B. G., and, Davies, G. J., (2010) Mechanistic insight into enzymatic glycosyl transfer with retention of configuration through analysis of glycomimetic inhibitors. Angew. Chem. Int. Ed. Engl. 49, 1234-1237.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 1234-1237
    • Errey, J.C.1    Lee, S.S.2    Gibson, R.P.3    Fleites, C.4    Barry, C.S.5    Jung, P.M.6    O'Sullivan, A.C.7    Davis, B.G.8    Davies, G.J.9
  • 34
    • 84855926382 scopus 로고    scopus 로고
    • Ni reaction of α-D-glucopyranosyl fluoride: Mechanistic implications for retaining glycosyltransferases
    • Ni reaction of α-D-glucopyranosyl fluoride: mechanistic implications for retaining glycosyltransferases. J. Am. Chem. Soc. 134, 1212-1220.
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 1212-1220
    • Chan, J.1    Tang, A.2    Bennet, A.J.3
  • 35
    • 0030700684 scopus 로고    scopus 로고
    • Eliminations in the reactions catalyzed by UDP-N-acetylglucosamine 2-epimerase
    • Morgan, P. M., Sala, R. F., and, Tanner, M. E., (1997) Eliminations in the reactions catalyzed by UDP-N-acetylglucosamine 2-epimerase. J. Am. Chem. Soc. 119, 10269-10277.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 10269-10277
    • Morgan, P.M.1    Sala, R.F.2    Tanner, M.E.3
  • 36
    • 0034642186 scopus 로고    scopus 로고
    • The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases
    • Campbell, R. E., Mosimann, S. C., Tanner, M. E., and, Strynadka, N. C., (2000) The structure of UDP-N-acetylglucosamine 2-epimerase reveals homology to phosphoglycosyl transferases. Biochemistry 39, 14993-15001.
    • (2000) Biochemistry , vol.39 , pp. 14993-15001
    • Campbell, R.E.1    Mosimann, S.C.2    Tanner, M.E.3    Strynadka, N.C.4
  • 38
    • 0025917139 scopus 로고
    • Lyase activity of nucleoside 2-deoxyribosyltransferase: Transient generation of ribal and its use in the synthesis of 2'-deoxynucleosides
    • Smar, M., Short, S. A., and, Wolfenden, R., (1991) Lyase activity of nucleoside 2-deoxyribosyltransferase: transient generation of ribal and its use in the synthesis of 2'-deoxynucleosides. Biochemistry 30, 7908-7912.
    • (1991) Biochemistry , vol.30 , pp. 7908-7912
    • Smar, M.1    Short, S.A.2    Wolfenden, R.3
  • 39
    • 0029959892 scopus 로고    scopus 로고
    • Active site amino acids that participate in the catalytic mechanism of nucleoside 2'-deoxyribosyltransferase
    • Short, S. A., Armstrong, S. R., Ealick, S. E., and, Porter, D. J. T., (1996) Active site amino acids that participate in the catalytic mechanism of nucleoside 2'-deoxyribosyltransferase. J. Biol. Chem. 271, 4978-4987.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4978-4987
    • Short, S.A.1    Armstrong, S.R.2    Ealick, S.E.3    Porter, D.J.T.4
  • 40
    • 79952260308 scopus 로고    scopus 로고
    • Turnover is rate-limited by deglycosylation for Micromonospora viridifaciens sialidase-catalyzed hydrolyses: Conformational implications for the Michaelis complex
    • Chan, J., Lu, A., and, Bennet, A. J., (2011) Turnover is rate-limited by deglycosylation for Micromonospora viridifaciens sialidase-catalyzed hydrolyses: conformational implications for the Michaelis complex J. Am. Chem. Soc. 133, 2989-2997.
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 2989-2997
    • Chan, J.1    Lu, A.2    Bennet, A.J.3
  • 41
    • 0020488546 scopus 로고
    • General acid-base catalysis of alpha-glucan phosphorylases: Stereospecific glucosyl transfer from D-glucal is a pyridoxal 5'-phosphate and orthophosphate (arsenate) dependent reaction
    • Klein, H. W., Palm, D., and, Helmreich, E. J., (1982) General acid-base catalysis of alpha-glucan phosphorylases: stereospecific glucosyl transfer from D-glucal is a pyridoxal 5'-phosphate and orthophosphate (arsenate) dependent reaction. Biochemistry 21, 6675-6684.
    • (1982) Biochemistry , vol.21 , pp. 6675-6684
    • Klein, H.W.1    Palm, D.2    Helmreich, E.J.3
  • 42
    • 0242585466 scopus 로고    scopus 로고
    • Sialic acid biosynthesis: Stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase
    • Chou, W. K., Hinderlich, S., Reutter, W., and, Tanner, M. E., (2003) Sialic acid biosynthesis: stereochemistry and mechanism of the reaction catalyzed by the mammalian UDP-N-acetylglucosamine 2-epimerase. J. Am. Chem. Soc. 125, 2455-2461.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2455-2461
    • Chou, W.K.1    Hinderlich, S.2    Reutter, W.3    Tanner, M.E.4
  • 43
    • 79956305481 scopus 로고    scopus 로고
    • Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site
    • Díaz, A., Martínez-Pons, C., Fita, I., Ferrer, J. C., and, Guinovart, J. J., (2011) Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site. J. Biol. Chem. 286, 18505-18514.
    • (2011) J. Biol. Chem. , vol.286 , pp. 18505-18514
    • Díaz, A.1    Martínez-Pons, C.2    Fita, I.3    Ferrer, J.C.4    Guinovart, J.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.