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L. Sim, R. Quezada‐Calvillo, E. Sterchi, B. Nichols, D. Rose (2008)
Human intestinal maltase-glucoamylase: crystal structure of the N-terminal catalytic subunit and basis of inhibition and substrate specificity.Journal of molecular biology, 375 3
T. Kaneko, T. Kohmoto, Hiroe Kikuchi, M. Shiota, H. Iino, T. Mitsuoka (1994)
Effects of Isomaltooligosaccharides with Different Degrees of Polymerization on Human Fecal BifidobacteriaBioscience, Biotechnology, and Biochemistry, 58
T. Tagami, K. Yamashita, M. Okuyama, H. Mori, M. Yao, A. Kimura (2013)
Molecular Basis for the Recognition of Long-chain Substrates by Plant α-GlucosidasesThe Journal of Biological Chemistry, 288
H Takaku (1988)
Handbook of amylases and related enzymes
Kyung‐Mo Song, M. Okuyama, Mariko Nishimura, T. Tagami, H. Mori, A. Kimura (2013)
Aromatic Residue on β→α Loop 1 in the Catalytic Domain Is Important to the Transglycosylation Specificity of Glycoside Hydrolase Family 31 α-GlucosidaseBioscience, Biotechnology, and Biochemistry, 77
D. Kothari, Seema Patel, A. Goyal (2014)
Therapeutic spectrum of nondigestible oligosaccharides: overview of current state and prospect.Journal of food science, 79 8
(2013)
A (2013b) Molecular basis
(1988)
Anomalously linked oligosaccharides mixture. In: The amylase research society
J. Söding, A. Biegert, A. Lupas (2005)
The HHpred interactive server for protein homology detection and structure predictionNucleic Acids Research, 33
K. Tan, C. Tesar, R. Wilton, L. Keigher, G. Babnigg, A. Joachimiak (2010)
Novel α‐glucosidase from human gut microbiome: substrate specificities and their switchThe FASEB Journal, 24
K. Hur, Myung-Shik Lee (2015)
Gut Microbiota and Metabolic DisordersDiabetes & Metabolism Journal, 39
T. Kohmoto, F. Fukui, Hajime Takaku, T. Mitsuoka (1991)
Dose-response Test of Isomaltooligosaccharides for Increasing Fecal BifidobacteriaAgricultural and biological chemistry, 55
A Fersht (1988)
Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding
T. Kohmoto, F. Fukui, Hajime Takaku, Y. Machida, M. Arai, T. Mitsuoka (1988)
Effect of Isomalto-oligosaccharides on Human Fecal FloraBifidobacteria and Microflora, 7
H. Mäkeläinen, Oliver Hasselwander, N. Rautonen, A. Ouwehand (2009)
Panose, a new prebiotic candidateLetters in Applied Microbiology, 49
T. Tagami, M. Okuyama, Hiroyuki Nakai, Young-Min Kim, H. Mori, K. Taguchi, B. Svensson, A. Kimura (2013)
Key aromatic residues at subsites +2 and +3 of glycoside hydrolase family 31 α-glucosidase contribute to recognition of long-chain substrates.Biochimica et biophysica acta, 1834 1
L. Ren, X. Qin, Xiaofang Cao, Lele Wang, Fang Bai, G. Bai, Yuequan Shen (2011)
Structural insight into substrate specificity of human intestinal maltase-glucoamylaseProtein & Cell, 2
T. Kohmoto, K. Tsuji, T. Kaneko, M. Shiota, F. Fukui, Hajime Takaku, Y. Nakagawa, T. Ichikawa, Syuuhei Kobayashi (1992)
Metabolism of (13)C-Isomaltooligosaccharides in Healthy Men.Bioscience, biotechnology, and biochemistry, 56 6
N. Shimba, Mai Shinagawa, Wataru Hoshino, Hideyuki Yamaguchi, N. Yamada, Ei-Ichiro Suzuki (2009)
Monitoring the hydrolysis and transglycosylation activity of alpha-glucosidase from Aspergillus niger by nuclear magnetic resonance spectroscopy and mass spectrometry.Analytical biochemistry, 393 1
A. Fersht (1998)
Structure and mechanism in protein science
T. Tagami, K. Yamashita, M. Okuyama, H. Mori, M. Yao, A. Kimura (2014)
Structural Advantage of Sugar Beet α-Glucosidase to Stabilize the Michaelis Complex with Long-chain SubstrateThe Journal of Biological Chemistry, 290
Aspergillus niger α-glucosidase (ANG), a member of glycoside hydrolase family 31, catalyzes hydrolysis of α-glucosidic linkages at the non-reducing end. In the presence of high concentrations of maltose, the enzyme also catalyzes the formation of α-(1→6)-glucosyl products by transglucosylation and it is used for production of the industrially useful panose and isomaltooligosaccharides. The initial transglucosylation by wild-type ANG in the presence of 100 mM maltose [Glc(α1–4)Glc] yields both α-(1→6)- and α-(1→4)-glucosidic linkages, the latter constituting ~25% of the total transfer reaction product. The maltotriose [Glc(α1–4)Glc(α1–4)Glc], α-(1→4)-glucosyl product disappears quickly, whereas the α-(1→6)-glucosyl products panose [Glc(α1–6)Glc(α1–4)Glc], isomaltose [Glc(α1–6)Glc], and isomaltotriose [Glc(α1–6)Glc(α1–6)Glc] accumulate. To modify the transglucosylation properties of ANG, residue Asn694, which was predicted to be involved in formation of the plus subsites of ANG, was replaced with Ala, Leu, Phe, and Trp. Except for N694A, the mutations enhanced the initial velocity of the α-(1→4)-transfer reaction to produce maltotriose, which was then degraded at a rate similar to that by wild-type ANG. With increasing reaction time, N694F and N694W mutations led to the accumulation of larger amounts of isomaltose and isomaltotriose than achieved with the wild-type enzyme. In the final stage of the reaction, the major product was panose (N694A and N694L) or isomaltose (N694F and N694W).
Applied Microbiology and Biotechnology – Springer Journals
Published: Jul 7, 2017
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