-
1
-
-
0002339053
-
α-Glucosidases
-
Amylase Research Society of Japan Pergamon Press Oxford, United Kingdom
-
S. Chiba α-Glucosidases Amylase Research Society of Japan Handbook of Amylases and Related Enzymes 1988 Pergamon Press Oxford, United Kingdom 104 116
-
(1988)
Handbook of Amylases and Related Enzymes
, pp. 104-116
-
-
Chiba, S.1
-
2
-
-
0031024312
-
Synthesis of a novel vitamin e derivative, 2-(α-D-glucopyranosyl)methyl-2,5,7,8-tetramethylchroman-6-ol, by α-glucosidase-catalyzed transglycosylation
-
H. Murase, R. Yamauchi, K. Kato, T. Kunieda, and J. Terao Synthesis of a novel vitamin E derivative, 2-(α-D-glucopyranosyl)methyl-2,5,7,8-tetramethylchroman-6-ol, by α-glucosidase-catalyzed transglycosylation Lipids 32 1997 73 78
-
(1997)
Lipids
, vol.32
, pp. 73-78
-
-
Murase, H.1
Yamauchi, R.2
Kato, K.3
Kunieda, T.4
Terao, J.5
-
3
-
-
0034280575
-
Synthesis of α-D-glucosylglycerol by α-glucosidase and some its characteristics
-
F. Takenaka, and H. Uchiyama Synthesis of α-D-glucosylglycerol by α-glucosidase and some its characteristics Biosci. Biotechnol. Biochem. 64 2000 1821 1826
-
(2000)
Biosci. Biotechnol. Biochem.
, vol.64
, pp. 1821-1826
-
-
Takenaka, F.1
Uchiyama, H.2
-
4
-
-
84863230607
-
Characterization of Halomonas sp. Strain H11 α-glucosidase activated by monovalent cations and its application for efficient synthesis of α-D-glycosylglycerol
-
T. Ojima, W. Saburi, T. Yamamoto, and T. Kudo Characterization of Halomonas sp. strain H11 α-glucosidase activated by monovalent cations and its application for efficient synthesis of α-D-glycosylglycerol Appl. Environ. Microbiol. 78 2012 1836 1845
-
(2012)
Appl. Environ. Microbiol.
, vol.78
, pp. 1836-1845
-
-
Ojima, T.1
Saburi, W.2
Yamamoto, T.3
Kudo, T.4
-
5
-
-
84861193146
-
α-Glucosylated 6-gingerol: Chemoenzymatic synthesis using α-glucosidase from Halomonas sp. H11, and its physical properties
-
T. Ojima, K. Aizawa, W. Saburi, and T. Yamamoto α-Glucosylated 6-gingerol: chemoenzymatic synthesis using α-glucosidase from Halomonas sp. H11, and its physical properties Carbohydr. Res. 354 2012 59 64
-
(2012)
Carbohydr. Res.
, vol.354
, pp. 59-64
-
-
Ojima, T.1
Aizawa, K.2
Saburi, W.3
Yamamoto, T.4
-
6
-
-
84857886473
-
Manufacture of oligosaccharides
-
Amylase Research Society of Japan Pergamon Press Oxford, United Kingdom
-
H. Takaku Manufacture of oligosaccharides Amylase Research Society of Japan Handbook of Amylases and Related Enzymes 1988 Pergamon Press Oxford, United Kingdom 212 222
-
(1988)
Handbook of Amylases and Related Enzymes
, pp. 212-222
-
-
Takaku, H.1
-
7
-
-
0006745657
-
Properties of a nigerose and nigerosylmaltooligosaccharides-supplemented syrup
-
T. Yamamoto, T. Unno, M. Sugawara, and T. Goda Properties of a nigerose and nigerosylmaltooligosaccharides-supplemented syrup J. Appl. Glycosci. 46 1999 475 482
-
(1999)
J. Appl. Glycosci.
, vol.46
, pp. 475-482
-
-
Yamamoto, T.1
Unno, T.2
Sugawara, M.3
Goda, T.4
-
8
-
-
0030733350
-
Structural and sequence-based classification of glycoside hydrolases
-
B. Henrrisat, and G. Davies Structural and sequence-based classification of glycoside hydrolases Curr. Opin. Struct. Biol. 7 1997 637 644
-
(1997)
Curr. Opin. Struct. Biol.
, vol.7
, pp. 637-644
-
-
Henrrisat, B.1
Davies, G.2
-
9
-
-
84891763855
-
The carbohydrate-active enzymes database (CAZy) in 2013
-
V. Lombard, H. Golaconda Ramulu, E. Drula, P.M. Coutinho, and B. Henrissat The carbohydrate-active enzymes database (CAZy) in 2013 Nucleic Acids Res. 42 2014 D490 D495
-
(2014)
Nucleic Acids Res.
, vol.42
, pp. D490-D495
-
-
Lombard, V.1
Golaconda Ramulu, H.2
Drula, E.3
Coutinho, P.M.4
Henrissat, B.5
-
10
-
-
0034220797
-
The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric α-glucosidase II belonging to the glycosyl hydrolase family 31
-
S. Kashiwabara, S. Azuma, M. Tsuduki, and Y. Suzuki The primary structure of the subunit in Bacillus thermoamyloliquefaciens KP1071 molecular weight 540,000 homohexameric α-glucosidase II belonging to the glycosyl hydrolase family 31 Biosci. Biotechnol. Biochem. 64 2000 1379 1393
-
(2000)
Biosci. Biotechnol. Biochem.
, vol.64
, pp. 1379-1393
-
-
Kashiwabara, S.1
Azuma, S.2
Tsuduki, M.3
Suzuki, Y.4
-
11
-
-
72649094480
-
The first α-1,3-glucosidase from bacterial origin belonging to glycoside hydrolase family 31
-
M.S. Kan, M. Okuyama, H. Mori, and A. Kimura The first α-1,3-glucosidase from bacterial origin belonging to glycoside hydrolase family 31 Biochimie 91 2009 1434 1442
-
(2009)
Biochimie
, vol.91
, pp. 1434-1442
-
-
Kan, M.S.1
Okuyama, M.2
Mori, H.3
Kimura, A.4
-
12
-
-
70350523401
-
Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application
-
Y.H. Wang, Y. Jiang, Z.Y. Duan, W.L. Shao, and H.Z. Li Expression and characterization of an α-glucosidase from Thermoanaerobacter ethanolicus JW200 with potential for industrial application Biologia 64 2009 1053 1057
-
(2009)
Biologia
, vol.64
, pp. 1053-1057
-
-
Wang, Y.H.1
Jiang, Y.2
Duan, Z.Y.3
Shao, W.L.4
Li, H.Z.5
-
13
-
-
77957840981
-
Novel α-glucosidase from human gut microbiome: Substrate specificities and their switch
-
K. Tan, C. Tesar, R. Wilton, L. Keigher, G. Babnigg, and A. Joachimiak Novel α-glucosidase from human gut microbiome: substrate specificities and their switch FASEB J. 24 2010 3939 3949
-
(2010)
FASEB J.
, vol.24
, pp. 3939-3949
-
-
Tan, K.1
Tesar, C.2
Wilton, R.3
Keigher, L.4
Babnigg, G.5
Joachimiak, A.6
-
14
-
-
0035831255
-
Relationship of sequence and structure to specificity in the α-amylase family of enzymes
-
E.A. MacGregor, Š. Janeček, and B. Svensson Relationship of sequence and structure to specificity in the α-amylase family of enzymes Biochim. Biophys. Acta 1546 2001 1 20
-
(2001)
Biochim. Biophys. Acta
, vol.1546
, pp. 1-20
-
-
MacGregor, E.A.1
Janeček Š.2
Svensson, B.3
-
15
-
-
84855275557
-
Function and structure studies of GH family 31 and 97 α-glycosidases
-
M. Okuyama Function and structure studies of GH family 31 and 97 α-glycosidases Biosci. Biotechnol. Biochem. 75 2011 2269 2277
-
(2011)
Biosci. Biotechnol. Biochem.
, vol.75
, pp. 2269-2277
-
-
Okuyama, M.1
-
16
-
-
2042475521
-
Identification and enzymatic characterization of the maltose inducible α-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis
-
S. Schönert, T. Buder, and M.K. Dahl Identification and enzymatic characterization of the maltose inducible α-glucosidase MalL (sucrase-isomaltase-maltase) of Bacillus subtilis J. Bacteriol. 180 1998 2574 2578
-
(1998)
J. Bacteriol.
, vol.180
, pp. 2574-2578
-
-
Schönert, S.1
Buder, T.2
Dahl, M.K.3
-
17
-
-
33744725575
-
Maltose and maltodextrin utilization by Bacillus subtilis
-
S. Schönert, S. Seitz, H. Krafft, E.A. Feuerbaum, I. Andernach, G. Witz, and M.K. Dahl Maltose and maltodextrin utilization by Bacillus subtilis J. Bacteriol. 188 2006 3911 3922
-
(2006)
J. Bacteriol.
, vol.188
, pp. 3911-3922
-
-
Schönert, S.1
Seitz, S.2
Krafft, H.3
Feuerbaum, E.A.4
Andernach, I.5
Witz, G.6
Dahl, M.K.7
-
18
-
-
71949124513
-
The maltodextrin transport system and metabolism in Lactobacillus acidophilus NCFM and production of novel α-glucosides through reverse phosphorolysis by maltose phosphorylase
-
H. Nakai, M.J. Baumann, B.O. Petersen, Y. Westphal, H. Schols, A. Dilokpimol, M.A. Hachem, S.J. Lahtinen, J.Ø. Duus, and B. Svensson The maltodextrin transport system and metabolism in Lactobacillus acidophilus NCFM and production of novel α-glucosides through reverse phosphorolysis by maltose phosphorylase FEBS J. 276 2009 7353 7365
-
(2009)
FEBS J.
, vol.276
, pp. 7353-7365
-
-
Nakai, H.1
Baumann, M.J.2
Petersen, B.O.3
Westphal, Y.4
Schols, H.5
Dilokpimol, A.6
Hachem, M.A.7
Lahtinen, S.J.8
Duus J.Ø.9
Svensson, B.10
-
19
-
-
0024520745
-
Site-directed mutagenesis by overlap extension using the polymerase chain reaction
-
S.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, and L.R. Pease Site-directed mutagenesis by overlap extension using the polymerase chain reaction Gene 77 1989 51 59
-
(1989)
Gene
, vol.77
, pp. 51-59
-
-
Ho, S.N.1
Hunt, H.D.2
Horton, R.M.3
Pullen, J.K.4
Pease, L.R.5
-
20
-
-
0005365801
-
The partial specific volumes, in aqueous solution, of three proteins
-
M.O. Dayhoff, G.E. Perlmann, and D.A. MacInnes The partial specific volumes, in aqueous solution, of three proteins J. Am. Chem. Soc. 74 1952 2515 2517
-
(1952)
J. Am. Chem. Soc.
, vol.74
, pp. 2515-2517
-
-
Dayhoff, M.O.1
Perlmann, G.E.2
MacInnes, D.A.3
-
21
-
-
84951404090
-
Photometric ninhydrin method for use in the chromatography of amino acids
-
S. Moore, and W.H. Stein Photometric ninhydrin method for use in the chromatography of amino acids J. Biol. Chem. 176 1948 367 388
-
(1948)
J. Biol. Chem.
, vol.176
, pp. 367-388
-
-
Moore, S.1
Stein, W.H.2
-
22
-
-
34248201703
-
ASH structure alignment package: Sensitivity and selectivity in domain classification
-
D.M. Standley, H. Toh, and H. Nakamura ASH structure alignment package: sensitivity and selectivity in domain classification BMC Bioinforma. 8 2007 116
-
(2007)
BMC Bioinforma.
, vol.8
, pp. 116
-
-
Standley, D.M.1
Toh, H.2
Nakamura, H.3
-
23
-
-
63849246525
-
Protein structure prediction on the Web: A case study using the Phyre server
-
L.A. Kelley, and M.J. Sternberg Protein structure prediction on the Web: a case study using the Phyre server Nat. Protoc. 4 2009 363 371
-
(2009)
Nat. Protoc.
, vol.4
, pp. 363-371
-
-
Kelley, L.A.1
Sternberg, M.J.2
-
24
-
-
84871601424
-
Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31
-
J. Larsbrink, A. Izumi, G.R. Hemsworth, G.J. Davies, and H. Brumer Structural enzymology of Cellvibrio japonicus Agd31B protein reveals α-transglucosylase activity in glycoside hydrolase family 31 J. Biol. Chem. 287 2012 43288 43299
-
(2012)
J. Biol. Chem.
, vol.287
, pp. 43288-43299
-
-
Larsbrink, J.1
Izumi, A.2
Hemsworth, G.R.3
Davies, G.J.4
Brumer, H.5
-
25
-
-
0035006850
-
Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe
-
M. Okuyama, A. Okuno, N. Shimizu, H. Mori, A. Kimura, and S. Chiba Carboxyl group of residue Asp647 as possible proton donor in catalytic reaction of α-glucosidase from Schizosaccharomyces pombe Eur. J. Biochem. 268 2001 2270 2280
-
(2001)
Eur. J. Biochem.
, vol.268
, pp. 2270-2280
-
-
Okuyama, M.1
Okuno, A.2
Shimizu, N.3
Mori, H.4
Kimura, A.5
Chiba, S.6
-
26
-
-
12544256784
-
Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate
-
A.L. Lovering, S.S. Lee, Y.W. Kim, S.G. Withers, and N.C. Strynadka Mechanistic and structural analysis of a family 31 α-glycosidase and its glycosyl-enzyme intermediate J. Biol. Chem. 280 2005 2105 2115
-
(2005)
J. Biol. Chem.
, vol.280
, pp. 2105-2115
-
-
Lovering, A.L.1
Lee, S.S.2
Kim, Y.W.3
Withers, S.G.4
Strynadka, N.C.5
-
27
-
-
33745048293
-
Structure of the Sulfolobus solfataricus α-glucosidase: Implications for domain conservation and substrate recognition in GH31
-
H.A. Ernst, L.L. Leggio, M. Willemoës, G. Leonard, P. Blum, and S. Larsen Structure of the Sulfolobus solfataricus α-glucosidase: implications for domain conservation and substrate recognition in GH31 J. Mol. Biol. 358 2006 1106 1124
-
(2006)
J. Mol. Biol.
, vol.358
, pp. 1106-1124
-
-
Ernst, H.A.1
Leggio, L.L.2
Willemoës, M.3
Leonard, G.4
Blum, P.5
Larsen, S.6
-
28
-
-
79957714498
-
Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification
-
J. Larsbrink, A. Izumi, F.M. Ibatullin, A. Nakhai, H.J. Gilbert, G.J. Davies, and H. Brumer Structural and enzymatic characterization of a glycoside hydrolase family 31 α-xylosidase from Cellvibrio japonicus involved in xyloglucan saccharification Biochem. J. 436 2011 567 580
-
(2011)
Biochem. J.
, vol.436
, pp. 567-580
-
-
Larsbrink, J.1
Izumi, A.2
Ibatullin, F.M.3
Nakhai, A.4
Gilbert, H.J.5
Davies, G.J.6
Brumer, H.7
-
29
-
-
84879595690
-
Molecular basis for the recognition of long-chain substrates by plant α-glucosidases
-
T. Tagami, K. Yamashita, M. Okuyama, H. Mori, M. Yao, and A. Kimura 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
-
30
-
-
84884169627
-
Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism
-
H.J. Rozeboom, S. Yu, S. Madrid, K.H. Kalk, R. Zhang, and B.W. Dijkstra Crystal structure of α-1,4-glucan lyase, a unique glycoside hydrolase family member with a novel catalytic mechanism J. Biol. Chem. 288 2013 26764 26774
-
(2013)
J. Biol. Chem.
, vol.288
, pp. 26764-26774
-
-
Rozeboom, H.J.1
Yu, S.2
Madrid, S.3
Kalk, K.H.4
Zhang, R.5
Dijkstra, B.W.6
-
31
-
-
80955157951
-
Structural insight into substrate specificity of human intestinal maltase-glucoamylase
-
L. Ren, X. Qin, X. Cao, L. Wang, F. Bai, G. Bai, and Y. Shen Structural insight into substrate specificity of human intestinal maltase-glucoamylase Protein Cell. 2 2011 827 836
-
(2011)
Protein Cell.
, vol.2
, pp. 827-836
-
-
Ren, L.1
Qin, X.2
Cao, X.3
Wang, L.4
Bai, F.5
Bai, G.6
Shen, Y.7
-
32
-
-
37449009082
-
Human intestinal maltase-glucoamylase: Crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity
-
L. Sim, R. Quezada-Calvillo, E.E. Sterchi, B.L. Nichols, and D.R. Rose Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity J. Mol. Biol. 375 2007 782 792
-
(2007)
J. Mol. Biol.
, vol.375
, pp. 782-792
-
-
Sim, L.1
Quezada-Calvillo, R.2
Sterchi, E.E.3
Nichols, B.L.4
Rose, D.R.5
-
33
-
-
77952939601
-
Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains
-
L. Sim, C. Willemsma, S. Mohan, H.Y. Naim, B.M. Pinto, and D.R. Rose Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains J. Biol. Chem. 285 2010 17763 17770
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 17763-17770
-
-
Sim, L.1
Willemsma, C.2
Mohan, S.3
Naim, H.Y.4
Pinto, B.M.5
Rose, D.R.6
-
34
-
-
0031001295
-
r 540000 homohexameric α-glucosidase with both exo-α-1,4-glucosidase and oligo-1,6-glucosidase activities
-
r 540000 homohexameric α-glucosidase with both exo-α-1,4-glucosidase and oligo-1,6-glucosidase activities Eur. J. Biochem. 245 1997 129 136
-
(1997)
Eur. J. Biochem.
, vol.245
, pp. 129-136
-
-
Suzuki, Y.1
Nobiki, M.2
Matsuda, M.3
Sawai, T.4
-
35
-
-
84883680333
-
Aromatic residue on β→α loop 1 in the catalytic domain is important to the transglycosylation specificity of glycoside hydrolase family 31 α-glucosidase
-
K.M. Song, M. Okuyama, M. Nishimura, T. Tagami, H. Mori, and A. Kimura Aromatic residue on β→α loop 1 in the catalytic domain is important to the transglycosylation specificity of glycoside hydrolase family 31 α-glucosidase Biosci. Biotechnol. Biochem. 77 2013 1759 1765
-
(2013)
Biosci. Biotechnol. Biochem.
, vol.77
, pp. 1759-1765
-
-
Song, K.M.1
Okuyama, M.2
Nishimura, M.3
Tagami, T.4
Mori, H.5
Kimura, A.6
-
36
-
-
84871716252
-
Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates
-
T. Tagami, M. Okuyama, H. Nakai, Y.M. Kim, H. Mori, K. Taguchi, B. Svensson, and A. Kimura Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates Biochim. Biophys. Acta 1834 2013 329 335
-
(2013)
Biochim. Biophys. Acta
, vol.1834
, pp. 329-335
-
-
Tagami, T.1
Okuyama, M.2
Nakai, H.3
Kim, Y.M.4
Mori, H.5
Taguchi, K.6
Svensson, B.7
Kimura, A.8
-
37
-
-
84954871548
-
Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger
-
A. Kita, H. Matsui, A. Somoto, A. Kimura, M. Takata, and S. Chiba Substrate specificity and subsite affinities of crystalline α-glucosidase from Aspergillus niger Agric. Biol. Chem. 55 1991 2327 2335
-
(1991)
Agric. Biol. Chem.
, vol.55
, pp. 2327-2335
-
-
Kita, A.1
Matsui, H.2
Somoto, A.3
Kimura, A.4
Takata, M.5
Chiba, S.6
-
38
-
-
27644512261
-
Glucoamylase originating from Schwanniomyces occidentalis is a typical α-glucosidase
-
F. Sato, M. Okuyama, H. Nakai, H. Mori, A. Kimura, and S. Chiba Glucoamylase originating from Schwanniomyces occidentalis is a typical α-glucosidase Biosci. Biotechnol. Biochem. 69 2005 1905 1913
-
(2005)
Biosci. Biotechnol. Biochem.
, vol.69
, pp. 1905-1913
-
-
Sato, F.1
Okuyama, M.2
Nakai, H.3
Mori, H.4
Kimura, A.5
Chiba, S.6
-
39
-
-
0031886567
-
Molecular characterization of the α-glucosidase gene (malA) from the hyperthermophilic archaeon Sulfolobus solfataricus
-
M. Rolfsmeier, C. Haseltine, E. Bini, A. Clark, and P. Blum Molecular characterization of the α-glucosidase gene (malA) from the hyperthermophilic archaeon Sulfolobus solfataricus J. Bacteriol. 180 1998 1287 1295
-
(1998)
J. Bacteriol.
, vol.180
, pp. 1287-1295
-
-
Rolfsmeier, M.1
Haseltine, C.2
Bini, E.3
Clark, A.4
Blum, P.5
-
40
-
-
0017821899
-
Purification and properties of an α-glucosidase (glucoamylase) in sugar beet seed
-
S. Chiba, S. Inomata, H. Matsui, and T. Shimomura Purification and properties of an α-glucosidase (glucoamylase) in sugar beet seed Agric. Biol. Chem. 42 1978 241 245
-
(1978)
Agric. Biol. Chem.
, vol.42
, pp. 241-245
-
-
Chiba, S.1
Inomata, S.2
Matsui, H.3
Shimomura, T.4
-
41
-
-
79959518480
-
Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase
-
K. Jones, L. Sim, S. Mohan, J. Kumarasamy, H. Liu, S. Avery, H.Y. Naim, R. Quezada-Calvillo, B.L. Nichols, B.M. Pinto, and D.R. Rose Mapping the intestinal alpha-glucogenic enzyme specificities of starch digesting maltase-glucoamylase and sucrase-isomaltase Bioorg. Med. Chem. 19 2011 3929 3934
-
(2011)
Bioorg. Med. Chem.
, vol.19
, pp. 3929-3934
-
-
Jones, K.1
Sim, L.2
Mohan, S.3
Kumarasamy, J.4
Liu, H.5
Avery, S.6
Naim, H.Y.7
Quezada-Calvillo, R.8
Nichols, B.L.9
Pinto, B.M.10
Rose, D.R.11
-
42
-
-
3543078738
-
Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli
-
M. Okuyama, H. Mori, S. Chiba, and A. Kimura Overexpression and characterization of two unknown proteins, YicI and YihQ, originated from Escherichia coli Protein Expr. Purif. 37 2004 170 179
-
(2004)
Protein Expr. Purif.
, vol.37
, pp. 170-179
-
-
Okuyama, M.1
Mori, H.2
Chiba, S.3
Kimura, A.4
-
43
-
-
0028989882
-
α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism
-
S. Yu, T. Ahmad, L. Kenne, and M. Pedersén α-1,4-Glucan lyase, a new class of starch/glycogen degrading enzyme. III. Substrate specificity, mode of action, and cleavage mechanism Biochim. Biophys. Acta 1244 1995 1 9
-
(1995)
Biochim. Biophys. Acta
, vol.1244
, pp. 1-9
-
-
Yu, S.1
Ahmad, T.2
Kenne, L.3
Pedersén, M.4
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