메뉴 건너뛰기




Volumn 275, Issue 5, 2008, Pages 903-913

The phosphate site of trehalose phosphorylase from Schizophyllum commune probed by site-directed mutagenesis and chemical rescue studies

Author keywords

retaining glucosyl transfer; Catalytic mechanism; Chemical rescue; Family GT 4; Glycosyltransferase

Indexed keywords

PHOSPHORYLASE; TREHALOSE PHOSPHORYLASE; UNCLASSIFIED DRUG; VANADIC ACID;

EID: 38949126913     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06254.x     Document Type: Article
Times cited : (13)

References (43)
  • 1
    • 0037466315 scopus 로고    scopus 로고
    • An evolving hierarchical family classification for glycosyltransferases
    • Coutinho PM, Deleury E, Davies GJ Henrissat B (2003) An evolving hierarchical family classification for glycosyltransferases. J Mol Biol 328, 307 317.
    • (2003) J Mol Biol , vol.328 , pp. 307-317
    • Coutinho, P.M.1    Deleury, E.2    Davies, G.J.3    Henrissat, B.4
  • 3
    • 0033199576 scopus 로고    scopus 로고
    • Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: Answers to a long outstanding question
    • Watson KA, McCleverty C, Geremia S, Cottaz S, Driguez H Johnson LN (1999) Phosphorylase recognition and phosphorolysis of its oligosaccharide substrate: answers to a long outstanding question. EMBO J 18, 4619 4632.
    • (1999) EMBO J , vol.18 , pp. 4619-4632
    • Watson, K.A.1    McCleverty, C.2    Geremia, S.3    Cottaz, S.4    Driguez, H.5    Johnson, L.N.6
  • 5
    • 0025017865 scopus 로고
    • The role of pyridoxal 5′-phosphate in glycogen phosphorylase catalysis
    • Palm D, Klein HW, Schinzel R, Buehner M Helmreich EJ (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
  • 6
    • 0036384359 scopus 로고    scopus 로고
    • Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase
    • Geremia S, Campagnolo M, Schinzel R Johnson LN (2002) Enzymatic catalysis in crystals of Escherichia coli maltodextrin phosphorylase. J Mol Biol 322, 413 423.
    • (2002) J Mol Biol , vol.322 , pp. 413-423
    • Geremia, S.1    Campagnolo, M.2    Schinzel, R.3    Johnson, L.N.4
  • 7
    • 9144219793 scopus 로고    scopus 로고
    • Mechanistic analogies amongst carbohydrate modifying enzymes
    • Lairson LL Withers SG (2004) Mechanistic analogies amongst carbohydrate modifying enzymes. Chem Commun 20, 2243 2248.
    • (2004) Chem Commun , vol.20 , pp. 2243-2248
    • Lairson, L.L.1    Withers, S.G.2
  • 8
    • 0033559148 scopus 로고    scopus 로고
    • Recent insights into inhibition, structure and mechanism of configuration-retaining glycosidases
    • Heightman TD Vasella AT (1999) Recent insights into inhibition, structure and mechanism of configuration-retaining glycosidases. Angew Chem Int Ed 38, 750 770.
    • (1999) Angew Chem Int Ed , vol.38 , pp. 750-770
    • Heightman, T.D.1    Vasella, A.T.2
  • 9
    • 0032882011 scopus 로고    scopus 로고
    • Mutagenesis of glycosidases
    • Ly HD Withers SG (1999) Mutagenesis of glycosidases. Annu Rev Biochem 68, 487 522.
    • (1999) Annu Rev Biochem , vol.68 , pp. 487-522
    • Ly, H.D.1    Withers, S.G.2
  • 10
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel DL Withers SG (2000) Glycosidase mechanisms: anatomy of a finely tuned catalyst. Acc Chem Res 33, 11 18.
    • (2000) Acc Chem Res , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 11
    • 17644368570 scopus 로고    scopus 로고
    • Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: The role of histidine-334 examined through kinetic characterization of site-directed mutants
    • Schwarz A, Pierfederici FM Nidetzky B (2005) Catalytic mechanism of α-retaining glucosyl transfer by Corynebacterium callunae starch phosphorylase: the role of histidine-334 examined through kinetic characterization of site-directed mutants. Biochem J 387, 437 445.
    • (2005) Biochem J , vol.387 , pp. 437-445
    • Schwarz, A.1    Pierfederici, F.M.2    Nidetzky, B.3
  • 12
    • 0036909547 scopus 로고    scopus 로고
    • Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA
    • Gibson RP, Turkenburg JP, Charnock SJ, Lloyd R Davies GJ (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
  • 13
    • 1642307849 scopus 로고    scopus 로고
    • The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases
    • Yep A, Ballicora MA Preiss J (2004) The active site of the Escherichia coli glycogen synthase is similar to the active site of retaining GT-B glycosyltransferases. Biochem Biophys Res Commun 316, 960 966.
    • (2004) Biochem Biophys Res Commun , vol.316 , pp. 960-966
    • Yep, A.1    Ballicora, M.A.2    Preiss, J.3
  • 14
    • 0029953209 scopus 로고    scopus 로고
    • Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states
    • Mitchell EP, Withers SG, Ermert P, Vasella AT, Garman EF, Oikonomakos NG Johnson LN (1996) Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states. Biochemistry 35, 7341 7355.
    • (1996) Biochemistry , vol.35 , pp. 7341-7355
    • Mitchell, E.P.1    Withers, S.G.2    Ermert, P.3    Vasella, A.T.4    Garman, E.F.5    Oikonomakos, N.G.6    Johnson, L.N.7
  • 15
    • 0037008717 scopus 로고    scopus 로고
    • Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, α-1,3-galactosyltransferase
    • Boix E, Zhang Y, Swaminathan GJ, Brew K Acharya KR (2002) Structural basis of ordered binding of donor and acceptor substrates to the retaining glycosyltransferase, α-1,3-galactosyltransferase. J Biol Chem 277, 28310 28318.
    • (2002) J Biol Chem , vol.277 , pp. 28310-28318
    • Boix, E.1    Zhang, Y.2    Swaminathan, G.J.3    Brew, K.4    Acharya, K.R.5
  • 16
    • 33746882419 scopus 로고    scopus 로고
    • Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases
    • Goedl C, Griessler R, Schwarz A Nidetzky B (2006) Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases. Biochem J 397, 491 500.
    • (2006) Biochem J , vol.397 , pp. 491-500
    • Goedl, C.1    Griessler, R.2    Schwarz, A.3    Nidetzky, B.4
  • 17
    • 0035875365 scopus 로고    scopus 로고
    • Fungal trehalose phosphorylase: Kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune
    • Eis C, Watkins M, Prohaska T Nidetzky B (2001) Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune. Biochem J 356, 757 767.
    • (2001) Biochem J , vol.356 , pp. 757-767
    • Eis, C.1    Watkins, M.2    Prohaska, T.3    Nidetzky, B.4
  • 18
    • 0035893762 scopus 로고    scopus 로고
    • α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: Mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors
    • Nidetzky B Eis C (2001) α-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors. Biochem J 360, 727 736.
    • (2001) Biochem J , vol.360 , pp. 727-736
    • Nidetzky, B.1    Eis, C.2
  • 19
    • 0037090699 scopus 로고    scopus 로고
    • Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors
    • Eis C Nidetzky B (2002) Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors. Biochem J 363, 335 340.
    • (2002) Biochem J , vol.363 , pp. 335-340
    • Eis, C.1    Nidetzky, B.2
  • 21
    • 0035930576 scopus 로고    scopus 로고
    • Structure of UDP complex of UDP-galactose: β-galactoside-α-1, 3-galactosyltransferase at 1.53-Å resolution reveals a conformational change in the catalytically important C terminus
    • Boix E, Swaminathan GJ, Zhang Y, Natesh R, Brew K Acharya KR (2001) Structure of UDP complex of UDP-galactose: β-galactoside-α-1,3- galactosyltransferase at 1.53-Å resolution reveals a conformational change in the catalytically important C terminus. J Biol Chem 276, 48608 48614.
    • (2001) J Biol Chem , vol.276 , pp. 48608-48614
    • Boix, E.1    Swaminathan, G.J.2    Zhang, Y.3    Natesh, R.4    Brew, K.5    Acharya, K.R.6
  • 22
    • 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 HD, Dieckelmann M, Wakarchuk WW, Withers SG Strynadka NC (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
  • 24
    • 33750974777 scopus 로고    scopus 로고
    • Insights into the synthesis of lipopolysaccharides and antibiotics through structures of two retaining glycosyltransferases from family GT-4
    • Martinez-Fleites C, Proctor M, Roberts S, Bolam DN, Gilbert HJ Davies GJ (2006) Insights into the synthesis of lipopolysaccharides and antibiotics through structures of two retaining glycosyltransferases from family GT-4. Chem Biol 13, 1143 1152.
    • (2006) Chem Biol , vol.13 , pp. 1143-1152
    • Martinez-Fleites, C.1    Proctor, M.2    Roberts, S.3    Bolam, D.N.4    Gilbert, H.J.5    Davies, G.J.6
  • 25
    • 23944471080 scopus 로고    scopus 로고
    • Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase
    • Lariviere L, Sommer N Morera S (2005) Structural evidence of a passive base-flipping mechanism for AGT, an unusual GT-B glycosyltransferase. J Mol Biol 352, 139 150.
    • (2005) J Mol Biol , vol.352 , pp. 139-150
    • Lariviere, L.1    Sommer, N.2    Morera, S.3
  • 26
    • 4444373841 scopus 로고    scopus 로고
    • Crystal structure of glycogen synthase: Homologous enzymes catalyze glycogen synthesis and degradation
    • Buschiazzo A, Ugalde JE, Guerin ME, Shepard W, Ugalde RA Alzari PM (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
  • 27
    • 0034623162 scopus 로고    scopus 로고
    • Regulation of glycogen synthase. Identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation
    • Pederson BA, Cheng C, Wilson WA Roach PJ (2000) Regulation of glycogen synthase. Identification of residues involved in regulation by the allosteric ligand glucose-6-P and by phosphorylation. J Biol Chem 275, 27753 27761.
    • (2000) J Biol Chem , vol.275 , pp. 27753-27761
    • Pederson, B.A.1    Cheng, C.2    Wilson, W.A.3    Roach, P.J.4
  • 28
    • 34248657555 scopus 로고    scopus 로고
    • Conformational changes induced by binding UDP-2F-galactose to α-1,3 galactosyltransferase - Implications for catalysis
    • Jamaluddin H, Tumbale P, Withers SG, Acharya KR Brew K (2007) Conformational changes induced by binding UDP-2F-galactose to α-1,3 galactosyltransferase - implications for catalysis. J Mol Biol 369, 1270 1281.
    • (2007) J Mol Biol , vol.369 , pp. 1270-1281
    • Jamaluddin, H.1    Tumbale, P.2    Withers, S.G.3    Acharya, K.R.4    Brew, K.5
  • 29
    • 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 JJ, Fita I Ferrer JC (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
  • 30
    • 0034704103 scopus 로고    scopus 로고
    • Identification of essential amino acids in the bacterial α-mannosyltransferase AceA
    • Abdian PL, Lellouch AC, Gautier C, Ielpi L Geremia RA (2000) Identification of essential amino acids in the bacterial α- mannosyltransferase AceA. J Biol Chem 275, 40568 40575.
    • (2000) J Biol Chem , vol.275 , pp. 40568-40575
    • Abdian, P.L.1    Lellouch, A.C.2    Gautier, C.3    Ielpi, L.4    Geremia, R.A.5
  • 31
    • 0025900497 scopus 로고
    • The phosphate recognition site of Escherichia coli maltodextrin phosphorylase
    • Schinzel R Drueckes P (1991) The phosphate recognition site of Escherichia coli maltodextrin phosphorylase. FEBS Lett 286, 125 128.
    • (1991) FEBS Lett , vol.286 , pp. 125-128
    • Schinzel, R.1    Drueckes, P.2
  • 32
    • 0034702818 scopus 로고    scopus 로고
    • Role of arginine 277 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate binding and transition state stabilization
    • Lehoux IE Mitra B (2000) Role of arginine 277 in (S)-mandelate dehydrogenase from Pseudomonas putida in substrate binding and transition state stabilization. Biochemistry 39, 10055 10065.
    • (2000) Biochemistry , vol.39 , pp. 10055-10065
    • Lehoux, I.E.1    Mitra, B.2
  • 33
    • 0030445397 scopus 로고    scopus 로고
    • Chemical rescue by guanidine derivatives of an arginine-substituted site-directed mutant of Escherichia coli ornithine transcarbamylase
    • Rynkiewicz MJ Seaton BA (1996) Chemical rescue by guanidine derivatives of an arginine-substituted site-directed mutant of Escherichia coli ornithine transcarbamylase. Biochemistry 35, 16174 16179.
    • (1996) Biochemistry , vol.35 , pp. 16174-16179
    • Rynkiewicz, M.J.1    Seaton, B.A.2
  • 34
    • 29244467407 scopus 로고    scopus 로고
    • Guanidine derivatives rescue the Arg418Ala mutation of Tritrichomonas foetus IMP dehydrogenase
    • Guillen Schlippe YV Hedstrom L (2005) Guanidine derivatives rescue the Arg418Ala mutation of Tritrichomonas foetus IMP dehydrogenase. Biochemistry 44, 16695 16700.
    • (2005) Biochemistry , vol.44 , pp. 16695-16700
    • Guillen Schlippe, Y.V.1    Hedstrom, L.2
  • 35
    • 0027049221 scopus 로고
    • Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127
    • Phillips MA, Hedstrom L Rutter WJ (1992) Guanidine derivatives restore activity to carboxypeptidase lacking arginine-127. Protein Sci 1, 517 521.
    • (1992) Protein Sci , vol.1 , pp. 517-521
    • Phillips, M.A.1    Hedstrom, L.2    Rutter, W.J.3
  • 36
    • 0034623991 scopus 로고    scopus 로고
    • Chemical rescue of a mutant protein-tyrosine kinase
    • Williams DM, Wang D Cole PA (2000) Chemical rescue of a mutant protein-tyrosine kinase. J Biol Chem 275, 38127 38130.
    • (2000) J Biol Chem , vol.275 , pp. 38127-38130
    • Williams, D.M.1    Wang, D.2    Cole, P.A.3
  • 37
    • 0025786892 scopus 로고
    • Active site lysine promotes catalytic function of pyridoxal 5′-phosphate in α-glucan phosphorylases
    • Schinzel R (1991) Active site lysine promotes catalytic function of pyridoxal 5′-phosphate in α-glucan phosphorylases. J Biol Chem 266, 9428 9431.
    • (1991) J Biol Chem , vol.266 , pp. 9428-9431
    • Schinzel, R.1
  • 38
    • 0024478059 scopus 로고
    • Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines
    • Toney MD Kirsch JF (1989) Direct Brønsted analysis of the restoration of activity to a mutant enzyme by exogenous amines. Science 243, 1485 1488.
    • (1989) Science , vol.243 , pp. 1485-1488
    • Toney, M.D.1    Kirsch, J.F.2
  • 39
    • 22644437239 scopus 로고    scopus 로고
    • Electrostatic stabilization in a pre-organized polar active site: The catalytic role of Lys-80 in Candida tenuis xylose reductase (AKR2B5) probed by site-directed mutagenesis and functional complementation studies
    • Kratzer R Nidetzky B (2005) Electrostatic stabilization in a pre-organized polar active site: the catalytic role of Lys-80 in Candida tenuis xylose reductase (AKR2B5) probed by site-directed mutagenesis and functional complementation studies. Biochem J 389, 507 515.
    • (2005) Biochem J , vol.389 , pp. 507-515
    • Kratzer, R.1    Nidetzky, B.2
  • 40
    • 0034719113 scopus 로고    scopus 로고
    • Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue
    • Zheng R Blanchard JS (2000) Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue. Biochemistry 39, 16244 16251.
    • (2000) Biochemistry , vol.39 , pp. 16244-16251
    • Zheng, R.1    Blanchard, J.S.2
  • 41
    • 0026647925 scopus 로고
    • Pyridoxal 5′-phosphate as a 31P reporter observing functional changes in the active site of Escherichia coli maltodextrin phosphorylase after site-directed mutagenesis
    • Schinzel R, Palm D Schnackerz KD (1992) Pyridoxal 5′-phosphate as a 31P reporter observing functional changes in the active site of Escherichia coli maltodextrin phosphorylase after site-directed mutagenesis. Biochemistry 31, 4128 4133.
    • (1992) Biochemistry , vol.31 , pp. 4128-4133
    • Schinzel, R.1    Palm, D.2    Schnackerz, K.D.3
  • 42
    • 0025154906 scopus 로고
    • Escherichia coli maltodextrin phosphorylase: Contribution of active site residues glutamate-637 and tyrosine-538 to the phosphorolytic cleavage of α-glucans
    • Schinzel R Palm D (1990) Escherichia coli maltodextrin phosphorylase: contribution of active site residues glutamate-637 and tyrosine-538 to the phosphorolytic cleavage of α-glucans. Biochemistry 29, 9956 9962.
    • (1990) Biochemistry , vol.29 , pp. 9956-9962
    • Schinzel, R.1    Palm, D.2
  • 43
    • 0033565384 scopus 로고    scopus 로고
    • Characterization of trehalose phosphorylase from Schizophyllum commune
    • Eis C Nidetzky B (1999) Characterization of trehalose phosphorylase from Schizophyllum commune. Biochem J 341, 385 393.
    • (1999) Biochem J , vol.341 , pp. 385-393
    • Eis, C.1    Nidetzky, B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.