-
1
-
-
28244442802
-
Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligosaccharides provide new insight into the mechanism for recognizing substrates with α-(1,6) glycosidic linkages
-
Abe A., Yoshida H., Tonozuka T., Sakano Y. & Kamitori S. 2005. Complexes of Thermoactinomyces vulgaris R-47 α-amylase 1 and pullulan model oligosaccharides provide new insight into the mechanism for recognizing substrates with α-(1, 6) glycosidic linkages. FEBS J. 272: 6145-6153.
-
(2005)
FEBS J.
, vol.272
, pp. 6145-6153
-
-
Abe, A.1
Yoshida, H.2
Tonozuka, T.3
Sakano, Y.4
Kamitori, S.5
-
2
-
-
9144235528
-
Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase
-
Albenne C., Skov L. K., Mirza O., Gajhede M., Feller G., D'Amico S., André G., Potocki-Véronèse G., van der Veen B. A., Monsan P. & Remaud-Simeon M. 2004. Molecular basis of the amylose-like polymer formation catalyzed by Neisseria polysaccharea amylosucrase. J. Biol. Chem. 279: 726-734.
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 726-734
-
-
Albenne, C.1
Skov, L.K.2
Mirza, O.3
Gajhede, M.4
Feller, G.5
D'Amico, S.6
André, G.7
Potocki-Véronèse, G.8
van der Veen, B.A.9
Monsan, P.10
Remaud-Simeon, M.11
-
3
-
-
80053177304
-
Multiple glycogen binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen
-
Baskaran S., Chikwana V. M., Contreras C. J., Davis K. D., Wilson W. A., Depaoli-Roach A. A., Roach P. J. & Hurley T. D. 2011. Multiple glycogen binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen. J. Biol. Chem. 286: 33999-34006.
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 33999-34006
-
-
Baskaran, S.1
Chikwana, V.M.2
Contreras, C.J.3
Davis, K.D.4
Wilson, W.A.5
Depaoli-Roach, A.A.6
Roach, P.J.7
Hurley, T.D.8
-
4
-
-
34748886064
-
The 'pair of sugar tongs' on the noncatalytic domain C of barley α-amylase participates in substrate binding and activity
-
Bozonnet S., Jensen M. T., Nielsen M. M., Aghajari N., Jensen M. H., Kramhøft B., Willemoës M., Tranier S., Haser R. & Svensson B. 2007. The 'pair of sugar tongs' on the noncatalytic domain C of barley α-amylase participates in substrate binding and activity. FEBS J. 274: 5055-5067.
-
(2007)
FEBS J.
, vol.274
, pp. 5055-5067
-
-
Bozonnet, S.1
Jensen, M.T.2
Nielsen, M.M.3
Aghajari, N.4
Jensen, M.H.5
Kramhøft, B.6
Willemoës, M.7
Tranier, S.8
Haser, R.9
Svensson, B.10
-
5
-
-
84880926719
-
The structure of Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding-mode
-
Caner S., Nguyen N., Aguda A., Zhang R., Pan Y. T., Withers S. G. & Brayer G. 2013. The structure of Mycobacterium smegmatis trehalose synthase reveals an unusual active site configuration and acarbose-binding-mode. Glycobiology 23: 1075-1083.
-
(2013)
Glycobiology
, vol.23
, pp. 1075-1083
-
-
Caner, S.1
Nguyen, N.2
Aguda, A.3
Zhang, R.4
Pan, Y.T.5
Withers, S.G.6
Brayer, G.7
-
6
-
-
58149200943
-
The Carbohydrate-Active enzymes database (CAZy): an expert resource for glycogenomics
-
Cantarel B. L., Coutinho P. M., Rancurel C., Bernard T., Lombard V. & Henrissat B. 2009. The Carbohydrate-Active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res. 37: D233-D238.
-
(2009)
Nucleic Acids Res.
, vol.37
-
-
Cantarel, B.L.1
Coutinho, P.M.2
Rancurel, C.3
Bernard, T.4
Lombard, V.5
Henrissat, B.6
-
7
-
-
84864758794
-
Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose
-
Chaen K., Noguchi J., Omori T., Kakuta Y. & Kimura M. 2012. Crystal structure of the rice branching enzyme I (BEI) in complex with maltopentaose. Biochem. Biophys. Res. Commun. 424: 508-511.
-
(2012)
Biochem. Biophys. Res. Commun.
, vol.424
, pp. 508-511
-
-
Chaen, K.1
Noguchi, J.2
Omori, T.3
Kakuta, Y.4
Kimura, M.5
-
8
-
-
84887979987
-
Surface binding sites in carbohydrate active enzymes: an emerging picture of structural and functional diversity
-
P. Rauter and T. Lindhorst (Eds.), Cambridge, United Kingdom: Royal Society of Chemistry
-
Cockburn D. & Svensson B. 2013. Surface binding sites in carbohydrate active enzymes: an emerging picture of structural and functional diversity, pp. 204-221. In: Rauter P. & Lindhorst T. (eds), Carbohydrate Chemistry vol. 39, Royal Society of Chemistry, Cambridge, United Kingdom.
-
(2013)
Carbohydrate Chemistry Vol. 39
, pp. 204-221
-
-
Cockburn, D.1
Svensson, B.2
-
9
-
-
84878311729
-
Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity
-
Cuesta-Seijo J. A., Nielsen M. M., Marri L., Tanaka H., Beeren S. R. & Palcic M. M. 2013. Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity. Acta Crystallogr. D Biol, Crystallogr. 69: 1013-1025.
-
(2013)
Acta Crystallogr. D Biol, Crystallogr.
, vol.69
, pp. 1013-1025
-
-
Cuesta-Seijo, J.A.1
Nielsen, M.M.2
Marri, L.3
Tanaka, H.4
Beeren, S.R.5
Palcic, M.M.6
-
10
-
-
80054916704
-
Isothermal titration calorimetry and surface plasmon resonance allow quantifying substrate binding to different binding sites of Bacillus subtilis xylanase
-
Cuyvers S., Dornez E., Abou Hachem M., Svensson B., Horhorn M., Chory J., Delcour J. A. & Courtin C. M. 2012. Isothermal titration calorimetry and surface plasmon resonance allow quantifying substrate binding to different binding sites of Bacillus subtilis xylanase. Anal. Biochem. 420: 90-92.
-
(2012)
Anal. Biochem.
, vol.420
, pp. 90-92
-
-
Cuyvers, S.1
Dornez, E.2
Abou Hachem, M.3
Svensson, B.4
Horhorn, M.5
Chory, J.6
Delcour, J.A.7
Courtin, C.M.8
-
11
-
-
80054923047
-
Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases
-
Cuyvers S., Dornez E., Delcour J. A. & Courtin C. M. 2012. Occurrence and functional significance of secondary carbohydrate binding sites in glycoside hydrolases. Crit. Rev. Biotechnol. 32: 93-107.
-
(2012)
Crit. Rev. Biotechnol.
, vol.32
, pp. 93-107
-
-
Cuyvers, S.1
Dornez, E.2
Delcour, J.A.3
Courtin, C.M.4
-
12
-
-
0033614827
-
X-ray structure of Novamyl, the five-domain "maltogenic" α-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7 Å resolution
-
Dauter Z., Dauter M., Brzozowski A. M., Christensen S., Borchert T. V., Beier L., Wilson K. S. & Davies G. J. 1999. X-ray structure of Novamyl, the five-domain "maltogenic" α-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1. 7 Å resolution. Biochemistry 38: 8385-8392.
-
(1999)
Biochemistry
, vol.38
, pp. 8385-8392
-
-
Dauter, Z.1
Dauter, M.2
Brzozowski, A.M.3
Christensen, S.4
Borchert, T.V.5
Beier, L.6
Wilson, K.S.7
Davies, G.J.8
-
13
-
-
79956305481
-
Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogenbinding site
-
Diaz A., Martínez-Pons C., Fita I., Ferrer J. C. & Guinovart J. J. 2011. Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogenbinding site. J. Biol. Chem. 286: 18505-18514.
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 18505-18514
-
-
Diaz, A.1
Martínez-Pons, C.2
Fita, I.3
Ferrer, J.C.4
Guinovart, J.J.5
-
14
-
-
84865528641
-
Binding interactions between α-glucans from Lactobacillus reuteri and milk proteins characterized by surface plasmon resonance
-
Diemer S. K., Svensson B., Babol L. N., Cockburn D., Grijpstra P., Dijkhuizen L., Folkenberg D. M., Garrigues C. & Ipsen R. H. 2012. Binding interactions between α-glucans from Lactobacillus reuteri and milk proteins characterized by surface plasmon resonance. Food Biophys. 7: 220-226.
-
(2012)
Food Biophys.
, vol.7
, pp. 220-226
-
-
Diemer, S.K.1
Svensson, B.2
Babol, L.N.3
Cockburn, D.4
Grijpstra, P.5
Dijkhuizen, L.6
Folkenberg, D.M.7
Garrigues, C.8
Ipsen, R.H.9
-
15
-
-
84899833506
-
Structure, function and specificity of branching enzyme
-
S. Janecek (Ed.)
-
th Symposium on the Alpha-Amylase Family, Programme and Abstracts, 20-24 October 2013, Smolenice Castle, Slovakia.
-
(2013)
th Symposium on the Alpha-Amylase Family, Programme and Abstracts, 20-24 October 2013, Smolenice Castle, Slovakia
, pp. 27
-
-
Fawaz, R.1
Feng, L.2
Hovde, S.3
Mort, A.4
Geiger, J.H.5
-
16
-
-
0017158856
-
Structure of glycogen phosphorylase at 3.0-Å-resolution and its ligand binding sites at 6-Å
-
Fletterick R. J., Sygusch J., Semple H. & Madsen N. B. 1976. Structure of glycogen phosphorylase at 3. 0-Å-resolution and its ligand binding sites at 6-Å. J. Biol. Chem. 251: 6142-6146.
-
(1976)
J. Biol. Chem.
, vol.251
, pp. 6142-6146
-
-
Fletterick, R.J.1
Sygusch, J.2
Semple, H.3
Madsen, N.B.4
-
17
-
-
26844434953
-
Use of random mutageneses to improve the properties of Thermus aquaticus amylomaltase for efficient production of cycloamyloses
-
Fujii K., Minagawa H., Terada Y., Takaha T., Kuriki T., Shimada J. & Kaneko H. 2005. Use of random mutageneses to improve the properties of Thermus aquaticus amylomaltase for efficient production of cycloamyloses. Appl. Environ. Microbiol. 71: 5823-5827.
-
(2005)
Appl. Environ. Microbiol.
, vol.71
, pp. 5823-5827
-
-
Fujii, K.1
Minagawa, H.2
Terada, Y.3
Takaha, T.4
Kuriki, T.5
Shimada, J.6
Kaneko, H.7
-
18
-
-
33947134880
-
Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase
-
Fujii K., Minagawa H., Terada Y., Takaha T., Kuriki T., Shimada J. & Kaneko H. 2007. Function of second glucan binding site including tyrosines 54 and 101 in Thermus aquaticus amylomaltase. J. Biosci. Bioeng. 103: 167-173.
-
(2007)
J. Biosci. Bioeng.
, vol.103
, pp. 167-173
-
-
Fujii, K.1
Minagawa, H.2
Terada, Y.3
Takaha, T.4
Kuriki, T.5
Shimada, J.6
Kaneko, H.7
-
19
-
-
77950511400
-
Catalytic mechanism of human α-galactosidase
-
Guce A. I., Clark N. E., Salgado E. N., Ivanen D. R., Kulminskaya A. A., Brumer H. & Garman S. C. 2010. Catalytic mechanism of human α-galactosidase. J. Biol. Chem. 285: 3625-2632.
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 2632-3625
-
-
Guce, A.I.1
Clark, N.E.2
Salgado, E.N.3
Ivanen, D.R.4
Kulminskaya, A.A.5
Brumer, H.6
Garman, S.C.7
-
20
-
-
70449955237
-
Lafora disease: insights into neurodegeneration from plant metabolism
-
Gentry M. S., Dixon J. E. & Worby C. A. 2009. Lafora disease: insights into neurodegeneration from plant metabolism. Trends Biochem. Sci. 34: 628-639.
-
(2009)
Trends Biochem. Sci.
, vol.34
, pp. 628-639
-
-
Gentry, M.S.1
Dixon, J.E.2
Worby, C.A.3
-
21
-
-
80054683038
-
Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding from microbes, plant and animals
-
Janecek S., Svensson B. & MacGregor E. A. 2011. Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding from microbes, plant and animals. Enzyme Microb. Technol. 49: 429-440.
-
(2011)
Enzyme Microb. Technol.
, vol.49
, pp. 429-440
-
-
Janecek, S.1
Svensson, B.2
MacGregor, E.A.3
-
22
-
-
84899863334
-
α-Amylase -an enzyme specificity found in various families of glycoside hydrolases
-
Janecek S., Svensson B. & MacGregor E. A. 2014. α-Amylase -an enzyme specificity found in various families of glycoside hydrolases. Cell. Mol. Life Sci. 71: 1149-1170.
-
(2014)
Cell. Mol. Life Sci.
, vol.71
, pp. 1149-1170
-
-
Janecek, S.1
Svensson, B.2
MacGregor, E.A.3
-
23
-
-
0030250653
-
Overexpression, purification, and characterization of recombinant barley α-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris
-
Juge N., Andersen J. S., Tull D., Roepstorff P. & Svensson B. 1996. Overexpression, purification, and characterization of recombinant barley α-amylases 1 and 2 secreted by the methylotrophic yeast Pichia pastoris. Protein Expr. Purif. 8: 204-214.
-
(1996)
Protein Expr. Purif.
, vol.8
, pp. 204-214
-
-
Juge, N.1
Andersen, J.S.2
Tull, D.3
Roepstorff, P.4
Svensson, B.5
-
24
-
-
33644530353
-
The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase
-
Juge N., Nøhr J., Le Gal-Coëffet M.-F., Kramhøft B., Furniss C. S. M., Planchot V., Archer D. B., Williamson G. & Svensson B. 2006. The activity of barley α-amylase on starch granules is enhanced by fusion of a starch binding domain from Aspergillus niger glucoamylase. Biochim. Biophys. Acta 1764: 275-284.
-
(2006)
Biochim. Biophys. Acta
, vol.1764
, pp. 275-284
-
-
Juge, N.1
Nøhr, J.2
Le Gal-Coëffet, M.-F.3
Kramhøft, B.4
Furniss, C.S.M.5
Planchot, V.6
Archer, D.B.7
Williamson, G.8
Svensson, B.9
-
25
-
-
75849119359
-
SusG: a unique cellmembrane-associated α-amylase from a prominent human gut symbiont targets complex starch molecules
-
Koropatkin N. M. & Smith T. J. 2010. SusG: a unique cellmembrane-associated α-amylase from a prominent human gut symbiont targets complex starch molecules. Structure 18: 200-215.
-
(2010)
Structure
, vol.18
, pp. 200-215
-
-
Koropatkin, N.M.1
Smith, T.J.2
-
26
-
-
13544266212
-
Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylase by barley α-amylase
-
Kramhøft B., Bak-Jensen K. S., Mori H., Juge N., Nøhr J. & Svensson B. 2005. Involvement of individual subsites and secondary substrate binding sites in multiple attack on amylase by barley α-amylase. Biochemistry 44: 1824-1832.
-
(2005)
Biochemistry
, vol.44
, pp. 1824-1832
-
-
Kramhøft, B.1
Bak-Jensen, K.S.2
Mori, H.3
Juge, N.4
Nøhr, J.5
Svensson, B.6
-
27
-
-
84872202291
-
Threedimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications
-
Leemhuis H., Pijning T., Dobruchowska J. M., Leeuwen S. S., Kralj S., Dijkstra B. W. & Dijkhuizen L. 2013. Threedimensional structures, reactions, mechanism, α-glucan analysis and their implications in biotechnology and food applications. J. Biotechnol. 163: 250-272.
-
(2013)
J. Biotechnol.
, vol.163
, pp. 250-272
-
-
Leemhuis, H.1
Pijning, T.2
Dobruchowska, J.M.3
Leeuwen, S.S.4
Kralj, S.5
Dijkstra, B.W.6
Dijkhuizen, L.7
-
28
-
-
0037984394
-
Differential regulation of a hyperthermophilic α-amylase with a novel (Ca,Zn) two-metal center by zinc
-
Linden A., Mayans O., Meyer-Klaucke W., Antranikian G. & Wilmanns M. 2003. Differential regulation of a hyperthermophilic α-amylase with a novel (Ca, Zn) two-metal center by zinc. J. Biol. Chem. 278: 9875-9884.
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 9875-9884
-
-
Linden, A.1
Mayans, O.2
Meyer-Klaucke, W.3
Antranikian, G.4
Wilmanns, M.5
-
29
-
-
34548853710
-
A secondary xylan-binding site enhances the catalytic activity of a single-domain family 11 glycoside hydrolase
-
Ludwiczek M. L., Heller M., Kantner T. & McIntosh L. P. 2007. A secondary xylan-binding site enhances the catalytic activity of a single-domain family 11 glycoside hydrolase. J. Mol. Biol. 373: 337-354.
-
(2007)
J. Mol. Biol.
, vol.373
, pp. 337-354
-
-
Ludwiczek, M.L.1
Heller, M.2
Kantner, T.3
McIntosh, L.P.4
-
30
-
-
33748517440
-
Structure of Bacillus halmapalus α-amylase crystallized with and without the substrate analogue acarbose and maltose. Acta Crystallogr
-
Lyhne-Iversen L., Hobley T. J., Kaasgaard S. G. & Harris P. 2006 Structure of Bacillus halmapalus α-amylase crystallized with and without the substrate analogue acarbose and maltose. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62: 849-854.
-
(2006)
Sect. F Struct. Biol. Cryst. Commun.
, vol.62
, pp. 849-854
-
-
Lyhne-Iversen, L.1
Hobley, T.J.2
Kaasgaard, S.G.3
Harris, P.4
-
31
-
-
84880938887
-
Structure of the Arabidopsis glucan phosphatase LIKE SEX FOUR2 reveals a unique mechanism for starch dephosphorylation
-
Meekins D. A., Guo H. F., Husodo S., Paasch B. C., Bridges T. M., Santelia D., Kottin O., Vander Kooi C. W. & Gentry M. S. 2013. Structure of the Arabidopsis glucan phosphatase LIKE SEX FOUR2 reveals a unique mechanism for starch dephosphorylation. Plant Cell 25: 2301-2314.
-
(2013)
Plant Cell
, vol.25
, pp. 2301-2314
-
-
Meekins, D.A.1
Guo, H.F.2
Husodo, S.3
Paasch, B.C.4
Bridges, T.M.5
Santelia, D.6
Kottin, O.7
Vander Kooi, C.W.8
Gentry, M.S.9
-
32
-
-
84866003063
-
Degradation of the starch components amylopectin and amylose by barley α-amylase 1: role of surface binding site 2
-
Nielsen J. W., Kramhøft B., Bozonnet S., Abou Hachem M., Stipp S. L. S., Svensson B. & Willemoës M. 2012. Degradation of the starch components amylopectin and amylose by barley α-amylase 1: role of surface binding site 2. Arch. Biochem. Biophys. 528: 1-6.
-
(2012)
Arch. Biochem. Biophys.
, vol.528
, pp. 1-6
-
-
Nielsen, J.W.1
Kramhøft, B.2
Bozonnet, S.3
Abou Hachem, M.4
Stipp, S.L.S.5
Svensson, B.6
Willemoës, M.7
-
33
-
-
68849101644
-
Two secondary carbohydrate binding sites on the surface of barley α-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules
-
Nielsen M. M., Bozonnet S., Seo E.-S., Mótyán J. A., Andersen J. M., Dilokpimol A., Abou Hachem M., Gyémánt G., Naested H., Kandra L., Sigurskjold B. W. & Svensson B. 2009. Two secondary carbohydrate binding sites on the surface of barley α-amylase 1 have distinct functions and display synergy in hydrolysis of starch granules. Biochemistry 48: 7686-7697.
-
(2009)
Biochemistry
, vol.48
, pp. 7686-7697
-
-
Nielsen, M.M.1
Bozonnet, S.2
Seo, E.-S.3
Mótyán, J.A.4
Andersen, J.M.5
Dilokpimol, A.6
Abou Hachem, M.7
Gyémánt, G.8
Naested, H.9
Kandra, L.10
Sigurskjold, B.W.11
Svensson, B.12
-
34
-
-
46949096331
-
Multi-site substrate binding and interplay in barley α-amylase 1
-
Nielsen M. M., Seo E. S., Bozonnet S., Aghajari N., Robert X., Haser R. & Svensson B. 2008. Multi-site substrate binding and interplay in barley α-amylase 1. FEBS Lett. 582: 2567-2571.
-
(2008)
FEBS Lett
, vol.582
, pp. 2567-2571
-
-
Nielsen, M.M.1
Seo, E.S.2
Bozonnet, S.3
Aghajari, N.4
Robert, X.5
Haser, R.6
Svensson, B.7
-
35
-
-
0141815501
-
Mechanism of barley α-amylase. Inhibition of amylose, maltodextrin and maltoheptaose hydrolysis by acarbose and cyclodextrin
-
Oudjeriouat N., Moreau Y., Santimone M., Svensson B., Marchis-Mouren G. & Desseaux V. 2003. Mechanism of barley α-amylase. Inhibition of amylose, maltodextrin and maltoheptaose hydrolysis by acarbose and cyclodextrin. Eur. J. Biochem. 270: 3871-3879.
-
(2003)
Eur. J. Biochem.
, vol.270
, pp. 3871-3879
-
-
Oudjeriouat, N.1
Moreau, Y.2
Santimone, M.3
Svensson, B.4
Marchis-Mouren, G.5
Desseaux, V.6
-
36
-
-
0042011174
-
The binding of β- and γ-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies
-
Pinotsis N., Leonidas D. D., Chrysina E. D., Oikonomakos N. G. & Mavridis I. M. 2003. The binding of β- and γ-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies. Protein Sci. 12: 1914-1924.
-
(2003)
Protein Sci.
, vol.12
, pp. 1914-1924
-
-
Pinotsis, N.1
Leonidas, D.D.2
Chrysina, E.D.3
Oikonomakos, N.G.4
Mavridis, I.M.5
-
37
-
-
0033694762
-
X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus - Implications for the synthesis of large cyclic glucans
-
Przylas I., Terada Y., Fujii K., Takaha T., Saenger W. & Strater, N. 2000. X-ray structure of acarbose bound to amylomaltase from Thermus aquaticus - Implications for the synthesis of large cyclic glucans. Eur. J. Biochem. 267: 6903-6913.
-
(2000)
Eur. J. Biochem.
, vol.267
, pp. 6903-6913
-
-
Przylas, I.1
Terada, Y.2
Fujii, K.3
Takaha, T.4
Saenger, W.5
Strater, N.6
-
38
-
-
0028966756
-
Carbohydrate-binding sites in a pancreatic α-amylase-substrate complex derived from X-ray structure analysis at 2.1 Å resolution
-
Qian M. X., Haser R. & Payan F. 1995. Carbohydrate-binding sites in a pancreatic α-amylase-substrate complex derived from X-ray structure analysis at 2. 1 Å resolution. Protein Sci. 4: 747-755.
-
(1995)
Protein Sci.
, vol.4
, pp. 747-755
-
-
Qian, M.X.1
Haser, R.2
Payan, F.3
-
39
-
-
56949098309
-
Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary α-amylase in substrate hydrolysis and bacterial binding
-
Ragunath C., Manuel S. G., Venkataraman V., Sait H. B. R., Kasinathan C. & Ramasubbu N. 2008. Probing the role of aromatic residues at the secondary saccharide-binding sites of human salivary α-amylase in substrate hydrolysis and bacterial binding. J. Mol. Biol. 384: 1232-1248.
-
(2008)
J. Mol. Biol.
, vol.384
, pp. 1232-1248
-
-
Ragunath, C.1
Manuel, S.G.2
Venkataraman, V.3
Sait, H.B.R.4
Kasinathan, C.5
Ramasubbu, N.6
-
40
-
-
0041663295
-
The structure of barley α-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding. A pair of sugar tongs
-
Robert X., Haser R., Gottschalk T., Ratajczek F., Driguez H., Svensson B. & Aghajari N. 2003. The structure of barley α-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding. A pair of sugar tongs. Structure 11: 973-984.
-
(2003)
Structure
, vol.11
, pp. 973-984
-
-
Robert, X.1
Haser, R.2
Gottschalk, T.3
Ratajczek, F.4
Driguez, H.5
Svensson, B.6
Aghajari, N.7
-
41
-
-
25444484215
-
Oligosaccharide binding to barley α-amylase 1
-
Robert X., Haser R., Mori H., Svensson B. & Aghajari N. 2005. Oligosaccharide binding to barley α-amylase 1. J. Biol. Chem. 280: 32968-32978.
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 32968-32978
-
-
Robert, X.1
Haser, R.2
Mori, H.3
Svensson, B.4
Aghajari, N.5
-
42
-
-
0014140609
-
Multiple attack hypothesis of α-amylase action: action of porcine pancreatic, human salivary, and Aspergillus oryzae α-amylases
-
Robyt J. F. & French D. 1967. Multiple attack hypothesis of α-amylase action: action of porcine pancreatic, human salivary, and Aspergillus oryzae α-amylases. Arch. Biochem. Biophys. 122: 8-16.
-
(1967)
Arch. Biochem. Biophys.
, vol.122
, pp. 8-16
-
-
Robyt, J.F.1
French, D.2
-
43
-
-
84885158803
-
A simple bacterial glucanotransferase can complement Arabidopsis mutants defective in cytosolic maltose metabolism
-
Ruzanski C., Smirnova J., Rejzek M., Cockburn D., Pedersen H. L., Pike M., Willats W. G. T., Svensson B., Steup M., Smith A. M. & Field R. A. 2013 A simple bacterial glucanotransferase can complement Arabidopsis mutants defective in cytosolic maltose metabolism. J. Biol. Chem. 288: 28581-28598.
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 28581-28598
-
-
Ruzanski, C.1
Smirnova, J.2
Rejzek, M.3
Cockburn, D.4
Pedersen, H.L.5
Pike, M.6
Willats, W.G.T.7
Svensson, B.8
Steup, M.9
Smith, A.M.10
Field, R.A.11
-
44
-
-
84876202428
-
New insight into structure/function relationships in plant α-amylase family GH13 members
-
Seo E. S., Andersen J. M., Nielsen M. M., Vester-Christensen M. B., Christiansen C., Jensen J. M., Mótyán J. A., Glaring M. A., Blennow A., Kandra L., Gyémánt G., Janeček Š., Haser R., Aghajari N., Abou Hachem M. & Svensson B. 2010. New insight into structure/function relationships in plant α-amylase family GH13 members. J. Appl. Glycosci. 57: 157-162.
-
(2010)
J. Appl. Glycosci.
, vol.57
, pp. 157-162
-
-
Seo, E.S.1
Andersen, J.M.2
Nielsen, M.M.3
Vester-Christensen, M.B.4
Christiansen, C.5
Jensen, J.M.6
Mótyán, J.A.7
Glaring, M.A.8
Blennow, A.9
Kandra, L.10
Gyémánt, G.11
Janeček12
Haser, R.13
Aghajari, N.14
Abou Hachem, M.15
Svensson, B.16
-
45
-
-
57349153333
-
An enzyme family reunion - similarities, differences and eccentricities in actions on α-glucans
-
Seo E. S., Christiansen C., Abou Hachem M., Nielsen M. M., Fukuda K., Bozonnet S., Blennow A., Aghajari N., Haser R. & Svensson B. 2008. An enzyme family reunion - similarities, differences and eccentricities in actions on α-glucans. Biologia 63: 967-979.
-
(2008)
Biologia
, vol.63
, pp. 967-979
-
-
Seo, E.S.1
Christiansen, C.2
Abou Hachem, M.3
Nielsen, M.M.4
Fukuda, K.5
Bozonnet, S.6
Blennow, A.7
Aghajari, N.8
Haser, R.9
Svensson, B.10
-
46
-
-
0033013902
-
The starch-binding domain from glucoamylase disrupts the structure of starch
-
Southall S. M., Simpson P. J., Gilbert H. J., Williamson G. & Williamson M. P. 1999. The starch-binding domain from glucoamylase disrupts the structure of starch. FEBS Lett. 447: 58-60.
-
(1999)
FEBS Lett.
, vol.447
, pp. 58-60
-
-
Southall, S.M.1
Simpson, P.J.2
Gilbert, H.J.3
Williamson, G.4
Williamson, M.P.5
-
47
-
-
33845665889
-
Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins
-
Stam M. R., Danchin E. G. J., Rancurel C., Coutinho P. M. & Henrissat B. 2006. Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng. Des. Sel. 19: 555-562.
-
(2006)
Protein Eng. Des. Sel.
, vol.19
, pp. 555-562
-
-
Stam, M.R.1
Danchin, E.G.J.2
Rancurel, C.3
Coutinho, P.M.4
Henrissat, B.5
-
48
-
-
84899864505
-
Binding, catalysis and regulation of the anti-TB target GH13 3 GlgE
-
S. Janecek (Ed.)
-
th Symposium on the Alpha-Amylase Family, Programme and Abstracts, 20-24 October 2013, Smolenice Castle, Slovakia.
-
(2013)
th Symposium on the Alpha-Amylase Family, Programme and Abstracts, 20-24 October 2013, Smolenice Castle, Slovakia
, pp. 22
-
-
Syson, K.1
Stevenson, C.E.M.2
Rashid, A.3
Leiba, J.4
Tuukkanen, A.5
Svergun, D.I.6
Molle, V.7
Lawson, D.8
Bornemann, S.9
-
49
-
-
41949118483
-
Crystal structure of the polyextremophilic α-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch
-
Tan T. C., Mijts B. N., Swaminathan K., Patel B. K. C. & Divne C. 2008. Crystal structure of the polyextremophilic α-amylase AmyB from Halothermothrix orenii: details of a productive enzyme-substrate complex and an N domain with a role in binding raw starch. J. Mol. Biol. 378: 850-868.
-
(2008)
J. Mol. Biol.
, vol.378
, pp. 850-868
-
-
Tan, T.C.1
Mijts, B.N.2
Swaminathan, K.3
Patel, B.K.C.4
Divne, C.5
-
50
-
-
15244339423
-
Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides
-
Timmins J., Leiros H.-K. S., Leonard G., Leiros, I. & McSweeney S. 2005. Crystal structure of maltooligosyltrehalose trehalohydrolase from Deinococcus radiodurans in complex with disaccharides. J. Mol. Biol. 347: 949-963.
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 949-963
-
-
Timmins, J.1
Leiros, H.-K.S.2
Leonard, G.3
Leiros, I.4
McSweeney, S.5
-
51
-
-
33747177331
-
Monoclinic crystal form of Aspergillus niger α-amylase in complex with maltose at 1.8 Å resolution
-
Vujicic-Žagar A. & Dijkstra B. W. 2006. Monoclinic crystal form of Aspergillus niger α-amylase in complex with maltose at 1. 8 Å resolution. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 62: 716-721.
-
(2006)
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
, vol.62
, pp. 716-721
-
-
Vujicic-Žagar, A.1
Dijkstra, B.W.2
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