-
1
-
-
84891763855
-
The carbohydrate-active enzymes database (CAZy) in 2013
-
1 Lombard, V., Golaconda Ramulu, H., Drula, E., Coutinho, P.M., Henrissat, B., The carbohydrate-active enzymes database (CAZy) in 2013. Nucleic Acids Res 42 (2014), 490–495.
-
(2014)
Nucleic Acids Res
, vol.42
, pp. 490-495
-
-
Lombard, V.1
Golaconda Ramulu, H.2
Drula, E.3
Coutinho, P.M.4
Henrissat, B.5
-
2
-
-
84922718832
-
Structure–function relationships of starch components
-
2 Vamadevan, V., Bertoft, E., Structure–function relationships of starch components. Starch - Stärke 67 (2015), 55–68.
-
(2015)
Starch - Stärke
, vol.67
, pp. 55-68
-
-
Vamadevan, V.1
Bertoft, E.2
-
3
-
-
84982077839
-
The structural biology of glucan phosphatases
-
(this volume)
-
3 Gentry, M.S., The structural biology of glucan phosphatases. Curr Opin Struct Biol, 40, 2016 (this volume).
-
(2016)
Curr Opin Struct Biol
, vol.40
-
-
Gentry, M.S.1
-
4
-
-
84907289294
-
A family of starch-active polysaccharide monooxygenases
-
Discovery and characterization of starch-active LPMO subsequently assigned into AA13.
-
4• Vu, V.V., Beeson, W.T., Span, E.A., Farquhar, E.R., Marletta, M.A., A family of starch-active polysaccharide monooxygenases. Proc Natl Acad Sci U S A 111 (2014), 13822–13827 Discovery and characterization of starch-active LPMO subsequently assigned into AA13.
-
(2014)
Proc Natl Acad Sci U S A
, vol.111
, pp. 13822-13827
-
-
Vu, V.V.1
Beeson, W.T.2
Span, E.A.3
Farquhar, E.R.4
Marletta, M.A.5
-
5
-
-
84955324784
-
Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase
-
First crystal structure of a starch-active LPMO, a representative of the new AA13 family showing a shallow groove leading to the active site.
-
5•• Lo Leggio, L., Simmons, T.J., Poulsen, J.-C.N., Frandsen, K.E.H., Hemsworth, G.R., Stringer, M.A., von Freiesleben, P., Tovborg, M., Johansen, K.S., De Maria, L., et al. Structure and boosting activity of a starch-degrading lytic polysaccharide monooxygenase. Nat Commun, 6, 2015, 5961 First crystal structure of a starch-active LPMO, a representative of the new AA13 family showing a shallow groove leading to the active site.
-
(2015)
Nat Commun
, vol.6
, pp. 5961
-
-
Lo Leggio, L.1
Simmons, T.J.2
Poulsen, J.-C.N.3
Frandsen, K.E.H.4
Hemsworth, G.R.5
Stringer, M.A.6
von Freiesleben, P.7
Tovborg, M.8
Johansen, K.S.9
De Maria, L.10
-
6
-
-
84899860464
-
Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review
-
6 Cockburn, D., Wilkens, C., Ruzanski, C., Andersen, S., Willum Nielsen, J., Smith, A., Field, R., Willemoës, M., Abou Hachem, M., Svensson, B., Analysis of surface binding sites (SBSs) in carbohydrate active enzymes with focus on glycoside hydrolase families 13 and 77 — a mini-review. Biologia (Bratisl) 69 (2014), 705–712.
-
(2014)
Biologia (Bratisl)
, vol.69
, pp. 705-712
-
-
Cockburn, D.1
Wilkens, C.2
Ruzanski, C.3
Andersen, S.4
Willum Nielsen, J.5
Smith, A.6
Field, R.7
Willemoës, M.8
Abou Hachem, M.9
Svensson, B.10
-
7
-
-
84923013262
-
Surface binding sites in amylase have distinct roles in recognition of starch structure motifs and degradation
-
7 Cockburn, D., Nielsen, M.M., Christiansen, C., Andersen, J.M., Rannes, J.B., Blennow, A., Svensson, B., Surface binding sites in amylase have distinct roles in recognition of starch structure motifs and degradation. Int J Biol Macromol 75 (2015), 338–345.
-
(2015)
Int J Biol Macromol
, vol.75
, pp. 338-345
-
-
Cockburn, D.1
Nielsen, M.M.2
Christiansen, C.3
Andersen, J.M.4
Rannes, J.B.5
Blennow, A.6
Svensson, B.7
-
8
-
-
84878311729
-
Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity
-
8 Cuesta-Seijo, J.A., Nielsen, M.M., Marri, L., Tanaka, H., Beeren, S.R., Palcic, M.M., Structure of starch synthase I from barley: insight into regulatory mechanisms of starch synthase activity. Acta Crystallogr Sect D Biol Crystallogr 69 (2013), 1013–1025.
-
(2013)
Acta Crystallogr Sect 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
-
9
-
-
84907510438
-
Selectivity of the surface binding site (SBS) on barley starch synthase I
-
9 Wilkens, C., Cuesta-Seijo, J.a., Palcic, M., Svensson, B., Selectivity of the surface binding site (SBS) on barley starch synthase I. Biologia (Bratisl) 69 (2014), 1118–1121.
-
(2014)
Biologia (Bratisl)
, vol.69
, pp. 1118-1121
-
-
Wilkens, C.1
Cuesta-Seijo, J.A.2
Palcic, M.3
Svensson, B.4
-
10
-
-
80053177304
-
Multiple glycogen-binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen
-
10 Baskaran, S., Chikwana, V.M., Contreras, C.J., Davis, K.D., Wilson, W.A., DePaoli-Roach, A.A., Roach, P.J., Hurley, T.D., Multiple glycogen-binding sites in eukaryotic glycogen synthase are required for high catalytic efficiency toward glycogen. J Biol Chem 286 (2011), 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
-
11
-
-
79956305481
-
Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site
-
11 Díaz, A., Martínez-Pons, C., Fita, I., Ferrer, J.C., Guinovart, J.J., Processivity and subcellular localization of glycogen synthase depend on a non-catalytic high affinity glycogen-binding site. J Biol Chem 286 (2011), 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
-
12
-
-
84899863334
-
α-Amylase: an enzyme specificity found in various families of glycoside hydrolases
-
12 Janeček, Š., Svensson, B., MacGregor, E.A., α-Amylase: an enzyme specificity found in various families of glycoside hydrolases. Cell Mol Life Sci 71 (2014), 1149–1170.
-
(2014)
Cell Mol Life Sci
, vol.71
, pp. 1149-1170
-
-
Janeček, Š.1
Svensson, B.2
MacGregor, E.A.3
-
13
-
-
84965052610
-
Structure and function of α-glucan debranching enzymes
-
13 Møller, M.S., Henriksen, A., Svensson, B., Structure and function of α-glucan debranching enzymes. Cell Mol Life Sci 73 (2016), 2619–2641.
-
(2016)
Cell Mol Life Sci
, vol.73
, pp. 2619-2641
-
-
Møller, M.S.1
Henriksen, A.2
Svensson, B.3
-
14
-
-
33845665889
-
Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins
-
14 Stam, M.R., Danchin, E.G.J., Rancurel, C., Coutinho, P.M., Henrissat, B., Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng Des Sel 19 (2006), 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
-
15
-
-
84921745976
-
Three-dimensional structure of a variant ‘Termamyl-like’ Geobacillus stearothermophilus α-amylase at 1.9 Å resolution
-
15 Offen, W.A., Viksoe-Nielsen, A., Borchert, T.V., Wilson, K.S., Davies, G.J., Three-dimensional structure of a variant ‘Termamyl-like’ Geobacillus stearothermophilus α-amylase at 1.9 Å resolution. Acta Crystallogr Sect F Struct Biol Commun 71 (2015), 66–70.
-
(2015)
Acta Crystallogr Sect F Struct Biol Commun
, vol.71
, pp. 66-70
-
-
Offen, W.A.1
Viksoe-Nielsen, A.2
Borchert, T.V.3
Wilson, K.S.4
Davies, G.J.5
-
16
-
-
84925618282
-
Crystal structure of α-amylase from Oryza sativa: molecular insights into enzyme activity and thermostability
-
8-barrel catalytic domain an SBS present in barley α-amylase is conserved.
-
8-barrel catalytic domain an SBS present in barley α-amylase is conserved.
-
(2014)
Biosci Biotechnol Biochem
, vol.78
, pp. 989-997
-
-
Ochiai, A.1
Sugai, H.2
Harada, K.3
Tanaka, S.4
Ishiyama, Y.5
Ito, K.6
Tanaka, T.7
Uchiumi, T.8
Taniguchi, M.9
Mitsui, T.10
-
17
-
-
84902470011
-
Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04
-
Crystal structure of a Pyrococcus exo-type maltose-forming amylase of family GH57 with preference for α-1,6-bonds and dual α-1,4-/α-1,6-bond specificity amenable to rational engineering.
-
17• Park, K.H., Jung, J.H., Park, S.G., Lee, M.E., Holden, J.F., Park, C.S., Woo, E.J., Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04. Acta Crystallogr Sect D Biol Crystallogr 70 (2014), 1659–1668 Crystal structure of a Pyrococcus exo-type maltose-forming amylase of family GH57 with preference for α-1,6-bonds and dual α-1,4-/α-1,6-bond specificity amenable to rational engineering.
-
(2014)
Acta Crystallogr Sect D Biol Crystallogr
, vol.70
, pp. 1659-1668
-
-
Park, K.H.1
Jung, J.H.2
Park, S.G.3
Lee, M.E.4
Holden, J.F.5
Park, C.S.6
Woo, E.J.7
-
18
-
-
13144305048
-
Activation of Bacillus licheniformis α-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium–sodium–calcium metal triad
-
18 Machius, M., Declerck, N., Huber, R., Wiegand, G., Activation of Bacillus licheniformis α-amylase through a disorder→order transition of the substrate-binding site mediated by a calcium–sodium–calcium metal triad. Structure 6 (1998), 281–292.
-
(1998)
Structure
, vol.6
, pp. 281-292
-
-
Machius, M.1
Declerck, N.2
Huber, R.3
Wiegand, G.4
-
19
-
-
0034622588
-
Structural analysis of a chimeric bacterial α-amylase. High-resolution analysis of native and ligand complexes
-
19 Brzozowski, A.M., Lawson, D.M., Turkenburg, J.P., Bisgaard-Frantzen, H., Svendsen, A., Borchert, T.V., Dauter, Z., Wilson, K.S., Davies, G.J., Structural analysis of a chimeric bacterial α-amylase. High-resolution analysis of native and ligand complexes. Biochemistry 39 (2000), 9099–9107.
-
(2000)
Biochemistry
, vol.39
, pp. 9099-9107
-
-
Brzozowski, A.M.1
Lawson, D.M.2
Turkenburg, J.P.3
Bisgaard-Frantzen, H.4
Svendsen, A.5
Borchert, T.V.6
Dauter, Z.7
Wilson, K.S.8
Davies, G.J.9
-
20
-
-
0035050561
-
Crystal structure of Bacillus stearothermophilus α-amylase: possible factors determining thermostability
-
20 Suvd, D., Fujimoto, Z., Takase, K., Matsumura, M., Mizuno, H., Crystal structure of Bacillus stearothermophilus α-amylase: possible factors determining thermostability. J Biochem 129 (2001), 461–468.
-
(2001)
J Biochem
, vol.129
, pp. 461-468
-
-
Suvd, D.1
Fujimoto, Z.2
Takase, K.3
Matsumura, M.4
Mizuno, H.5
-
21
-
-
8344244671
-
Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707
-
21 Kanai, R., Haga, K., Akiba, T., Yamane, K., Harata, K., Biochemical and crystallographic analyses of maltohexaose-producing amylase from alkalophilic Bacillus sp. 707. Biochemistry 43 (2004), 14047–14056.
-
(2004)
Biochemistry
, vol.43
, pp. 14047-14056
-
-
Kanai, R.1
Haga, K.2
Akiba, T.3
Yamane, K.4
Harata, K.5
-
22
-
-
21444452111
-
Structure of a Bacillus halmapalus family 13 α-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 Å resolution
-
22 Davies, G.J., Marek Brzozowski, A., Dauter, Z., Rasmussen, M.D., Borchert, T.V., Wilson, K.S., Structure of a Bacillus halmapalus family 13 α-amylase, BHA, in complex with an acarbose-derived nonasaccharide at 2.1 Å resolution. Acta Crystallogr Sect D Biol Crystallogr 61 (2005), 190–193.
-
(2005)
Acta Crystallogr Sect D Biol Crystallogr
, vol.61
, pp. 190-193
-
-
Davies, G.J.1
Marek Brzozowski, A.2
Dauter, Z.3
Rasmussen, M.D.4
Borchert, T.V.5
Wilson, K.S.6
-
23
-
-
33846218264
-
Ancestral sequence evolutionary trace and crystal structure analyses of alkaline α-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins
-
23 Shirai, T., Igarashi, K., Ozawa, T., Hagihara, H., Kobayashi, T., Ozaki, K., Ito, S., Ancestral sequence evolutionary trace and crystal structure analyses of alkaline α-amylase from Bacillus sp. KSM-1378 to clarify the alkaline adaptation process of proteins. Proteins Struct Funct Bioinforma 66 (2007), 600–610.
-
(2007)
Proteins Struct Funct Bioinforma
, vol.66
, pp. 600-610
-
-
Shirai, T.1
Igarashi, K.2
Ozawa, T.3
Hagihara, H.4
Kobayashi, T.5
Ozaki, K.6
Ito, S.7
-
24
-
-
76349122941
-
Structure of Bacillus amyloliquefaciens α-amylase at high resolution: implications for thermal stability
-
24 Alikhajeh, J., Khajeh, K., Ranjbar, B., Naderi-Manesh, H., Lin, Y.H., Liu, E., Guan, H.H., Hsieh, Y.C., Chuankhayan, P., Huang, Y.C., et al. Structure of Bacillus amyloliquefaciens α-amylase at high resolution: implications for thermal stability. Acta Crystallogr Sect F Struct Biol Cryst Commun 66 (2010), 121–129.
-
(2010)
Acta Crystallogr Sect F Struct Biol Cryst Commun
, vol.66
, pp. 121-129
-
-
Alikhajeh, J.1
Khajeh, K.2
Ranjbar, B.3
Naderi-Manesh, H.4
Lin, Y.H.5
Liu, E.6
Guan, H.H.7
Hsieh, Y.C.8
Chuankhayan, P.9
Huang, Y.C.10
-
25
-
-
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
-
25 Robert, X., Haser, R., Gottschalk, T., Ratajczak, F., Driguez, H., Svensson, B., Aghajari, N., 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 (2003), 973–984.
-
(2003)
Structure
, vol.11
, pp. 973-984
-
-
Robert, X.1
Haser, R.2
Gottschalk, T.3
Ratajczak, F.4
Driguez, H.5
Svensson, B.6
Aghajari, N.7
-
26
-
-
25444484215
-
Oligosaccharide binding to barley α-amylase 1
-
26 Robert, X., Haser, R., Mori, H., Svensson, B., Aghajari, N., Oligosaccharide binding to barley α-amylase 1. J Biol Chem 280 (2005), 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
-
27
-
-
34748886064
-
The “pair of sugar tongs” site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity
-
27 Bozonnet, S., Jensen, M.T., Nielsen, M.M., Aghajari, N., Jensen, M.H., Kramhøft, B., Willemoës, M., Tranier, S., Haser, R., Svensson, B., The “pair of sugar tongs” site on the non-catalytic domain C of barley α-amylase participates in substrate binding and activity. FEBS J 274 (2007), 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
-
28
-
-
46949096331
-
Multi-site substrate binding and interplay in barley α-amylase 1
-
28 Nielsen, M.M., Seo, E.S., Bozonnet, S., Aghajari, N., Robert, X., Haser, R., Svensson, B., Multi-site substrate binding and interplay in barley α-amylase 1. FEBS Lett 582 (2008), 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
-
29
-
-
0028229326
-
Crystal and molecular structure of barley α-amylase
-
29 Kadziola, A., Abe, J., Svensson, B., Haser, R., Crystal and molecular structure of barley α-amylase. J Mol Biol 239 (1994), 104–121.
-
(1994)
J Mol Biol
, vol.239
, pp. 104-121
-
-
Kadziola, A.1
Abe, J.2
Svensson, B.3
Haser, R.4
-
30
-
-
0032562777
-
Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis
-
30 Kadziola, A., Søgaard, M., Svensson, B., Haser, R., Molecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysis. J Mol Biol 278 (1998), 205–217.
-
(1998)
J Mol Biol
, vol.278
, pp. 205-217
-
-
Kadziola, A.1
Søgaard, M.2
Svensson, B.3
Haser, R.4
-
31
-
-
70949096336
-
The rice α-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids
-
31 Kitajima, A., Asatsuma, S., Okada, H., Hamada, Y., Kaneko, K., Nanjo, Y., Kawagoe, Y., Toyooka, K., Matsuoka, K., Takeuchi, M., et al. The rice α-amylase glycoprotein is targeted from the Golgi apparatus through the secretory pathway to the plastids. Plant Cell 21 (2009), 2844–2858.
-
(2009)
Plant Cell
, vol.21
, pp. 2844-2858
-
-
Kitajima, A.1
Asatsuma, S.2
Okada, H.3
Hamada, Y.4
Kaneko, K.5
Nanjo, Y.6
Kawagoe, Y.7
Toyooka, K.8
Matsuoka, K.9
Takeuchi, M.10
-
32
-
-
84905180510
-
Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus α-amylase
-
32 Ranjani, V., Janeček, S., Chai, K.P., Shahir, S., Abdul Rahman, R.N.Z.R., Chan, K.-G., Goh, K.M., Protein engineering of selected residues from conserved sequence regions of a novel Anoxybacillus α-amylase. Sci Rep 4 (2014), 5850–5858.
-
(2014)
Sci Rep
, vol.4
, pp. 5850-5858
-
-
Ranjani, V.1
Janeček, S.2
Chai, K.P.3
Shahir, S.4
Abdul Rahman, R.N.Z.R.5
Chan, K.-G.6
Goh, K.M.7
-
33
-
-
84960959631
-
Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass
-
33 Chai, K.P., Othman, N.F.B., Teh, A.-H., Ho, K.L., Chan, K.-G., Shamsir, M.S., Goh, K.M., Ng, C.L., Crystal structure of Anoxybacillus α-amylase provides insights into maltose binding of a new glycosyl hydrolase subclass. Sci Rep, 6, 2016, 23126.
-
(2016)
Sci Rep
, vol.6
, pp. 23126
-
-
Chai, K.P.1
Othman, N.F.B.2
Teh, A.-H.3
Ho, K.L.4
Chan, K.-G.5
Shamsir, M.S.6
Goh, K.M.7
Ng, C.L.8
-
34
-
-
84863473157
-
Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose
-
34 Chai, Y.Y., Rahman RNZRA, Illias, R.M., Goh, K.M., Cloning and characterization of two new thermostable and alkalitolerant α-amylases from the Anoxybacillus species that produce high levels of maltose. J Ind Microbiol Biotechnol 39 (2012), 731–741.
-
(2012)
J Ind Microbiol Biotechnol
, vol.39
, pp. 731-741
-
-
Chai, Y.Y.1
RNZRA, R.2
Illias, R.M.3
Goh, K.M.4
-
35
-
-
84878018073
-
Crystal structure of a compact α-amylase from Geobacillus thermoleovorans
-
35 Mok, S.C., Teh, A.H., Saito, J.A., Najimudin, N., Alam, M., Crystal structure of a compact α-amylase from Geobacillus thermoleovorans. Enzyme Microb Technol 53 (2013), 46–54.
-
(2013)
Enzyme Microb Technol
, vol.53
, pp. 46-54
-
-
Mok, S.C.1
Teh, A.H.2
Saito, J.A.3
Najimudin, N.4
Alam, M.5
-
36
-
-
84879595690
-
Molecular basis for the recognition of long-chain substrates by plant α-glucosidases
-
36 Tagami, T., Yamashita, K., Okuyama, M., Mori, H., Yao, M., Kimura, A., Molecular basis for the recognition of long-chain substrates by plant α-glucosidases. J Biol Chem 288 (2013), 19296–19303.
-
(2013)
J Biol Chem
, vol.288
, pp. 19296-19303
-
-
Tagami, T.1
Yamashita, K.2
Okuyama, M.3
Mori, H.4
Yao, M.5
Kimura, A.6
-
37
-
-
84931038861
-
Structural analysis of the α-glucosidase HaG provides new insights into substrate specificity and catalytic mechanism
-
8-barrel catalytic domain this GH13 α-glucosidase showed strict disaccharide specificity.
-
8-barrel catalytic domain this GH13 α-glucosidase showed strict disaccharide specificity.
-
(2015)
Acta Crystallogr Sect D Biol Crystallogr
, vol.71
, pp. 1382-1391
-
-
Shen, X.1
Saburi, W.2
Gai, Z.3
Kato, K.4
Ojima-Kato, T.5
Yu, J.6
Komoda, K.7
Kido, Y.8
Matsui, H.9
Mori, H.10
-
38
-
-
0007553835
-
Substrate specificity of an α-glucosidase in sugar beet seeds
-
38 Matsui, H., Chiba, S., Shimomura, T., Substrate specificity of an α-glucosidase in sugar beet seeds. Agric Biol Chem 42 (1978), 1855–1860.
-
(1978)
Agric Biol Chem
, vol.42
, pp. 1855-1860
-
-
Matsui, H.1
Chiba, S.2
Shimomura, T.3
-
39
-
-
0028886770
-
Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues
-
39 Im, H., Henson, C.A., Characterization of high pI α-glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues. Carbohydr Res 277 (1995), 145–159.
-
(1995)
Carbohydr Res
, vol.277
, pp. 145-159
-
-
Im, H.1
Henson, C.A.2
-
40
-
-
84922230719
-
Structural advantage of sugar beet α-glucosidase to stabilize the Michaelis complex with long-chain substrate
-
Crystal structure of sugar beet GH31 α-glucosidase in complex with acarviosyl-maltooligosaccharides accommodated at the active site and via substrate self-stabilisation contributing to the interaction in particular with distant subsites.
-
40•• Tagami, T., Yamashita, K., Okuyama, M., Mori, H., Yao, M., Kimura, A., Structural advantage of sugar beet α-glucosidase to stabilize the Michaelis complex with long-chain substrate. J Biol Chem 290 (2015), 1796–1803 Crystal structure of sugar beet GH31 α-glucosidase in complex with acarviosyl-maltooligosaccharides accommodated at the active site and via substrate self-stabilisation contributing to the interaction in particular with distant subsites.
-
(2015)
J Biol Chem
, vol.290
, pp. 1796-1803
-
-
Tagami, T.1
Yamashita, K.2
Okuyama, M.3
Mori, H.4
Yao, M.5
Kimura, A.6
-
41
-
-
77958500768
-
Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins
-
41 Vester-Christensen, M.B., Abou Hachem, M., Svensson, B., Henriksen, A., Crystal structure of an essential enzyme in seed starch degradation: barley limit dextrinase in complex with cyclodextrins. J Mol Biol 403 (2010), 739–750.
-
(2010)
J Mol Biol
, vol.403
, pp. 739-750
-
-
Vester-Christensen, M.B.1
Abou Hachem, M.2
Svensson, B.3
Henriksen, A.4
-
42
-
-
84865724994
-
Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21
-
42 Møller, M.S., Abou Hachem, M., Svensson, B., Henriksen, A., Structure of the starch-debranching enzyme barley limit dextrinase reveals homology of the N-terminal domain to CBM21. Acta Crystallogr Sect F Struct Biol Cryst Commun 68 (2012), 1008–1012.
-
(2012)
Acta Crystallogr Sect F Struct Biol Cryst Commun
, vol.68
, pp. 1008-1012
-
-
Møller, M.S.1
Abou Hachem, M.2
Svensson, B.3
Henriksen, A.4
-
43
-
-
84924120262
-
Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase
-
Crystal structure of a catalytic residue mutated debranching enzyme in the first complex with a natural limit dextrin substrate.
-
43•• Møller, M.S., Windahl, M.S., Sim, L., Bøjstrup, M., Abou Hachem, M., Hindsgaul, O., Palcic, M., Svensson, B., Henriksen, A., Oligosaccharide and substrate binding in the starch debranching enzyme barley limit dextrinase. J Mol Biol 427 (2015), 1263–1277 Crystal structure of a catalytic residue mutated debranching enzyme in the first complex with a natural limit dextrin substrate.
-
(2015)
J Mol Biol
, vol.427
, pp. 1263-1277
-
-
Møller, M.S.1
Windahl, M.S.2
Sim, L.3
Bøjstrup, M.4
Abou Hachem, M.5
Hindsgaul, O.6
Palcic, M.7
Svensson, B.8
Henriksen, A.9
-
44
-
-
84906323670
-
Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11
-
Crystal structure of a remarkably thermostable pullulanase in complex with two oligosaccharides at the catalytic domain in parallel binding mode and another interacting with the N-terminal starch binding family CBM68 domain.
-
44•• Xu, J., Ren, F., Huang, C.-H., Zheng, Y., Zhen, J., Sun, H., Ko, T.-P., He, M., Chen, C.-C., Chan, H.-C., et al. Functional and structural studies of pullulanase from Anoxybacillus sp. LM18-11. Proteins Struct Funct Bioinforma 82 (2014), 1685–1693 Crystal structure of a remarkably thermostable pullulanase in complex with two oligosaccharides at the catalytic domain in parallel binding mode and another interacting with the N-terminal starch binding family CBM68 domain.
-
(2014)
Proteins Struct Funct Bioinforma
, vol.82
, pp. 1685-1693
-
-
Xu, J.1
Ren, F.2
Huang, C.-H.3
Zheng, Y.4
Zhen, J.5
Sun, H.6
Ko, T.-P.7
He, M.8
Chen, C.-C.9
Chan, H.-C.10
-
45
-
-
0036348660
-
Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue
-
45 Nakamura, Y., Towards a better understanding of the metabolic system for amylopectin biosynthesis in plants: rice endosperm as a model tissue. Plant Cell Physiol 43 (2002), 718–725.
-
(2002)
Plant Cell Physiol
, vol.43
, pp. 718-725
-
-
Nakamura, Y.1
-
46
-
-
0034003526
-
Update on biochemistry recent progress toward understanding biosynthesis of the amylopectin crystal
-
46 Myers, A.M., Morell, M.K., James, M.G., Ball, S.G., Update on biochemistry recent progress toward understanding biosynthesis of the amylopectin crystal. Plant Physiol 122 (2000), 989–997.
-
(2000)
Plant Physiol
, vol.122
, pp. 989-997
-
-
Myers, A.M.1
Morell, M.K.2
James, M.G.3
Ball, S.G.4
-
47
-
-
77958165867
-
Starch biosynthesis in cereal endosperm
-
47 Jeon, J.-S., Ryoo, N., Hahn, T.-R., Walia, H., Nakamura, Y., Starch biosynthesis in cereal endosperm. Plant Physiol Biochem 48 (2010), 383–392.
-
(2010)
Plant Physiol Biochem
, vol.48
, pp. 383-392
-
-
Jeon, J.-S.1
Ryoo, N.2
Hahn, T.-R.3
Walia, H.4
Nakamura, Y.5
-
48
-
-
84905991993
-
Crystal structure of the Chlamydomonas starch debranching enzyme isoamylase ISA1 reveals insights into the mechanism of branch trimming and complex assembly
-
Crystal structure of isoamylase in complex with maltoheptaose revealing details about the mechanism of branch binding, suggesting a role in trimming of misplaced branches during amylopectin synthesis, and containing two surface binding sites.
-
48•• Sim, L., Beeren, S.R., Findinier, J., Dauvillée, D., Ball, S., Henriksen, A., Palcic, M.M., Crystal structure of the Chlamydomonas starch debranching enzyme isoamylase ISA1 reveals insights into the mechanism of branch trimming and complex assembly. J Biol Chem 289 (2014), 22991–23003 Crystal structure of isoamylase in complex with maltoheptaose revealing details about the mechanism of branch binding, suggesting a role in trimming of misplaced branches during amylopectin synthesis, and containing two surface binding sites.
-
(2014)
J Biol Chem
, vol.289
, pp. 22991-23003
-
-
Sim, L.1
Beeren, S.R.2
Findinier, J.3
Dauvillée, D.4
Ball, S.5
Henriksen, A.6
Palcic, M.M.7
-
49
-
-
84947770599
-
The framework of polysaccharide monooxygenase structure and chemistry
-
49 Span, E.A., Marletta, M.A., The framework of polysaccharide monooxygenase structure and chemistry. Curr Opin Struct Biol 35 (2015), 93–99.
-
(2015)
Curr Opin Struct Biol
, vol.35
, pp. 93-99
-
-
Span, E.A.1
Marletta, M.A.2
-
50
-
-
84966702119
-
Starch-degrading polysaccharide monooxygenases
-
50 Vu, V.V., Marletta, M.A., Starch-degrading polysaccharide monooxygenases. Cell Mol Life Sci 73 (2016), 2809–2819.
-
(2016)
Cell Mol Life Sci
, vol.73
, pp. 2809-2819
-
-
Vu, V.V.1
Marletta, M.A.2
-
51
-
-
77957727454
-
An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides
-
51 Vaaje-Kolstad, G., Westereng, B., Horn, S.J., Liu, Z., Zhai, H., Sørlie, M., Eijsink, V.G.H., An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides. Science 330 (2010), 219–222.
-
(2010)
Science
, vol.330
, pp. 219-222
-
-
Vaaje-Kolstad, G.1
Westereng, B.2
Horn, S.J.3
Liu, Z.4
Zhai, H.5
Sørlie, M.6
Eijsink, V.G.H.7
-
52
-
-
77950948151
-
Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family
-
52 Harris, P.V., Welner, D., McFarland, K.C., Re, E., Navarro Poulsen, J.C., Brown, K., Salbo, R., Ding, H., Vlasenko, E., Merino, S., et al. Stimulation of lignocellulosic biomass hydrolysis by proteins of glycoside hydrolase family 61: structure and function of a large, enigmatic family. Biochemistry 49 (2010), 3305–3316.
-
(2010)
Biochemistry
, vol.49
, pp. 3305-3316
-
-
Harris, P.V.1
Welner, D.2
McFarland, K.C.3
Re, E.4
Navarro Poulsen, J.C.5
Brown, K.6
Salbo, R.7
Ding, H.8
Vlasenko, E.9
Merino, S.10
-
53
-
-
84861862587
-
Starch in the Arabidopsis plant
-
53 Smith, A.M., Starch in the Arabidopsis plant. Starch - Stärke 64 (2012), 421–434.
-
(2012)
Starch - Stärke
, vol.64
, pp. 421-434
-
-
Smith, A.M.1
-
54
-
-
84940676089
-
Structural basis for the interconversion of maltodextrins by MalQ, the amylomaltase of Escherichia coli
-
54 Weiss, S.C., Skerra, A., Schiefner, A., Structural basis for the interconversion of maltodextrins by MalQ, the amylomaltase of Escherichia coli. J Biol Chem 290 (2015), 21352–21364.
-
(2015)
J Biol Chem
, vol.290
, pp. 21352-21364
-
-
Weiss, S.C.1
Skerra, A.2
Schiefner, A.3
-
55
-
-
84949636198
-
Structural dissection of the maltodextrin disproportionation cycle of the Arabidopsis plastidial enzyme DPE1
-
Crystal structures of DPE1 plastidial disproportionating enzyme in complex with different ligands are trapped in conformational states that allow definition of a structural basis for the catalytic mechanism.
-
55•• O'Neill, E.C., Stevenson, C.E.M., Tantanarat, K., Latousakis, D., Donaldson, M.I., Rejzek, M., Nepogodiev, S.A., Limpaseni, T., Field, R.A., Lawson, D.M., Structural dissection of the maltodextrin disproportionation cycle of the Arabidopsis plastidial enzyme DPE1. J Biol Chem 290 (2015), 29834–29853 Crystal structures of DPE1 plastidial disproportionating enzyme in complex with different ligands are trapped in conformational states that allow definition of a structural basis for the catalytic mechanism.
-
(2015)
J Biol Chem
, vol.290
, pp. 29834-29853
-
-
O'Neill, E.C.1
Stevenson, C.E.M.2
Tantanarat, K.3
Latousakis, D.4
Donaldson, M.I.5
Rejzek, M.6
Nepogodiev, S.A.7
Limpaseni, T.8
Field, R.A.9
Lawson, D.M.10
-
56
-
-
84888616193
-
Sugar-coated sensor chip and nanoparticle surfaces for the in vitro enzymatic synthesis of starch-like materials
-
Crystal structure of the Arabidopsis phosphorylase AtPHS2 in complex with maltotriose and acarbose bound at the surface of the enzyme.
-
56• O'Neill, E.C., Rashid, A.M., Stevenson, C.E.M., Hetru, A.-C., Gunning, A.P., Rejzek, M., Nepogodiev, S.A., Bornemann, S., Lawson, D.M., Field, R.A., Sugar-coated sensor chip and nanoparticle surfaces for the in vitro enzymatic synthesis of starch-like materials. Chem Sci 5 (2014), 341–350 Crystal structure of the Arabidopsis phosphorylase AtPHS2 in complex with maltotriose and acarbose bound at the surface of the enzyme.
-
(2014)
Chem Sci
, vol.5
, pp. 341-350
-
-
O'Neill, E.C.1
Rashid, A.M.2
Stevenson, C.E.M.3
Hetru, A.-C.4
Gunning, A.P.5
Rejzek, M.6
Nepogodiev, S.A.7
Bornemann, S.8
Lawson, D.M.9
Field, R.A.10
-
57
-
-
0026033985
-
Structural mechanism for glycogen-phosphorylase control by phosphorylation and AMP
-
57 Barford, D., Hu, S.-H., Johnson, L.N., Structural mechanism for glycogen-phosphorylase control by phosphorylation and AMP. J Mol Biol 218 (1991), 233–260.
-
(1991)
J Mol Biol
, vol.218
, pp. 233-260
-
-
Barford, D.1
Hu, S.-H.2
Johnson, L.N.3
-
58
-
-
0034979357
-
Structural relationships among regulated and unregulated phosphorylases
-
58 Buchbinder, J.L., Rath, V.L., Fletterick, R.J., Structural relationships among regulated and unregulated phosphorylases. Annu Rev Biophys Biomol Struct 30 (2001), 191–209.
-
(2001)
Annu Rev Biophys Biomol Struct
, vol.30
, pp. 191-209
-
-
Buchbinder, J.L.1
Rath, V.L.2
Fletterick, R.J.3
-
59
-
-
84939568633
-
The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif
-
Crystal structure of human pancreatic α-amylase in complex with the flavonol glycoside potent inhibitor montbretin A reveals a new inhibitor motif where caffeine and myrecitin phenolics interact resulting in hydrogen bond formation with catalytic acids.
-
59• Williams, L.K., Zhang, X., Caner, S., Tysoe, C., Nguyen, N.T., Wicki, J., Williams, D.E., Coleman, J., McNeill, J.H., Yuen, V., et al. The amylase inhibitor montbretin A reveals a new glycosidase inhibition motif. Nat Chem Biol 11 (2015), 691–696 Crystal structure of human pancreatic α-amylase in complex with the flavonol glycoside potent inhibitor montbretin A reveals a new inhibitor motif where caffeine and myrecitin phenolics interact resulting in hydrogen bond formation with catalytic acids.
-
(2015)
Nat Chem Biol
, vol.11
, pp. 691-696
-
-
Williams, L.K.1
Zhang, X.2
Caner, S.3
Tysoe, C.4
Nguyen, N.T.5
Wicki, J.6
Williams, D.E.7
Coleman, J.8
McNeill, J.H.9
Yuen, V.10
-
60
-
-
85015474592
-
Potent human α-amylase inhibition by the β-defensin-like protein helianthamide
-
Crystal structure of porcine pancreatic α-amylase in a high affinity complex with helianthamide, representing a new type of complex formation with a antimicrobial β-defensin fold being non-immunogenic and having high stability as opposed to other high affinity peptide and proteinaceous inhibitors.
-
60• Tysoe, C., Williams, L.K., Keyzers, R., Nguyen, N.T., Tarling, C., Wicki, J., Goddard-Borger, E.D., Aguda, A.H., Perry, S., Foster, L.J., et al. Potent human α-amylase inhibition by the β-defensin-like protein helianthamide. ACS Cent Sci 2 (2016), 154–161 Crystal structure of porcine pancreatic α-amylase in a high affinity complex with helianthamide, representing a new type of complex formation with a antimicrobial β-defensin fold being non-immunogenic and having high stability as opposed to other high affinity peptide and proteinaceous inhibitors.
-
(2016)
ACS Cent Sci
, vol.2
, pp. 154-161
-
-
Tysoe, C.1
Williams, L.K.2
Keyzers, R.3
Nguyen, N.T.4
Tarling, C.5
Wicki, J.6
Goddard-Borger, E.D.7
Aguda, A.H.8
Perry, S.9
Foster, L.J.10
-
61
-
-
0029111443
-
The structure of human pancreatic α-amylase at 1.8 Å resolution and comparisons with related enzymes
-
61 Brayer, G.D., Luo, Y., Withers, S.G., The structure of human pancreatic α-amylase at 1.8 Å resolution and comparisons with related enzymes. Protein Sci 4 (1995), 1730–1742.
-
(1995)
Protein Sci
, vol.4
, pp. 1730-1742
-
-
Brayer, G.D.1
Luo, Y.2
Withers, S.G.3
-
62
-
-
0001631469
-
Structure of human salivary α-amylase at 1.6 Å resolution: implications for its role in the oral cavity
-
62 Ramasubbu, N., Paloth, V., Luo, Y., Brayer, G.D., Levine, M.J., Structure of human salivary α-amylase at 1.6 Å resolution: implications for its role in the oral cavity. Acta Crystallogr Sect D Biol Crystallogr 52 (1996), 435–446.
-
(1996)
Acta Crystallogr Sect D Biol Crystallogr
, vol.52
, pp. 435-446
-
-
Ramasubbu, N.1
Paloth, V.2
Luo, Y.3
Brayer, G.D.4
Levine, M.J.5
-
63
-
-
0032528247
-
A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution
-
63 Strobl, S., Maskos, K., Wiegand, G., Huber, R., Gomis-Rüth, F.X., Glockshuber, R., A novel strategy for inhibition of α-amylases: yellow meal worm α-amylase in complex with the Ragi bifunctional inhibitor at 2.5 Å resolution. Structure 6 (1998), 911–921.
-
(1998)
Structure
, vol.6
, pp. 911-921
-
-
Strobl, S.1
Maskos, K.2
Wiegand, G.3
Huber, R.4
Gomis-Rüth, F.X.5
Glockshuber, R.6
-
64
-
-
84929347435
-
Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal-type inhibitors
-
Crystal structure of the complex of debranching limit dextrinase in complex with an endogenous inhibitor of the cereal-inhibitor family that applies a unique binding mode stabilized by an intermolecular hydrophobic cluster formed adjacent to the catalytic site.
-
64•• Møller, M.S., Vester-Christensen, M.B., Jensen, J.M., Abou Hachem, M., Henriksen, A., Svensson, B., Crystal structure of barley limit dextrinase-limit dextrinase inhibitor (LD-LDI) complex reveals insights into mechanism and diversity of cereal-type inhibitors. J Biol Chem 290 (2015), 12614–12629 Crystal structure of the complex of debranching limit dextrinase in complex with an endogenous inhibitor of the cereal-inhibitor family that applies a unique binding mode stabilized by an intermolecular hydrophobic cluster formed adjacent to the catalytic site.
-
(2015)
J Biol Chem
, vol.290
, pp. 12614-12629
-
-
Møller, M.S.1
Vester-Christensen, M.B.2
Jensen, J.M.3
Abou Hachem, M.4
Henriksen, A.5
Svensson, B.6
-
65
-
-
1042298136
-
Proteinaceous α-amylase inhibitors
-
65 Svensson, B., Fukuda, K., Nielsen, P.K., Bønsager, B.C., Proteinaceous α-amylase inhibitors. Biochim Biophys Acta 1696 (2004), 145–156.
-
(2004)
Biochim Biophys Acta
, vol.1696
, pp. 145-156
-
-
Svensson, B.1
Fukuda, K.2
Nielsen, P.K.3
Bønsager, B.C.4
-
66
-
-
33646770359
-
Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site
-
66 Mikami, B., Iwamoto, H., Malle, D., Yoon, H.-J., Demirkan-Sarikaya, E., Mezaki, Y., Katsuya, Y., Crystal structure of pullulanase: evidence for parallel binding of oligosaccharides in the active site. J Mol Biol 359 (2006), 690–707.
-
(2006)
J Mol Biol
, vol.359
, pp. 690-707
-
-
Mikami, B.1
Iwamoto, H.2
Malle, D.3
Yoon, H.-J.4
Demirkan-Sarikaya, E.5
Mezaki, Y.6
Katsuya, Y.7
-
67
-
-
0031015902
-
Nomenclature for sugar-binding subsites in glycosyl hydrolases
-
67 Davies, G.J., Wilson, K.S., Henrissat, B., Nomenclature for sugar-binding subsites in glycosyl hydrolases. Biochem J Lett 321 (1997), 557–559.
-
(1997)
Biochem J Lett
, vol.321
, pp. 557-559
-
-
Davies, G.J.1
Wilson, K.S.2
Henrissat, B.3
|