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PDBsum entry 1j10
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structures of beta-Amylase from bacillus cereus var mycoides in complexes with substrate analogs and affinity-Labeling reagents.
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Authors
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T.Oyama,
H.Miyake,
M.Kusunoki,
Y.Nitta.
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Ref.
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J Biochem (tokyo), 2003,
133,
467-474.
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PubMed id
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Abstract
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The crystal structures of beta-amylase from Bacillus cereus var. mycoides in
complexes with five inhibitors were solved. The inhibitors used were three
substrate analogs, i.e. glucose, maltose (product), and a synthesized compound,
O-alpha-D-glucopyranosyl-(1-->4)-O-alpha-D-glucopyranosyl-(1-->4)-D-xylopyranose
(GGX), and two affinity-labeling reagents with an epoxy alkyl group at the
reducing end of glucose. For all inhibitors, one molecule was bound at the
active site cleft and the non-reducing end glucose of the four inhibitors except
GGX was located at subsite 1, accompanied by a large conformational change of
the flexible loop (residues 93-97), which covered the bound inhibitor. In
addition, another molecule of maltose or GGX was bound about 30 A away from the
active site. A large movement of residues 330 and 331 around subsite 3 was also
observed upon the binding of GGX at subsites 3 to 5. Two affinity-labeling
reagents, alpha-EPG and alpha-EBG, were covalently bound to a catalytic residue
(Glu-172). A substrate recognition mechanism for the beta-amylase was discussed
based on the modes of binding of these inhibitors in the active site cleft.
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Secondary reference #1
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Title
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Crystal structure of beta-Amylase from bacillus cereus var. Mycoides at 2.2 a resolution.
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Authors
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T.Oyama,
M.Kusunoki,
Y.Kishimoto,
Y.Takasaki,
Y.Nitta.
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Ref.
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J Biochem (tokyo), 1999,
125,
1120-1130.
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PubMed id
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Secondary reference #2
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Title
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Kinetic study of active site structure of beta-Amylase from bacillus cereus var. Mycoides
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Authors
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Y.Nitta,
M.Shirakawa,
Y.Takasaki.
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Ref.
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biosci biotechnol biochem, 1996,
60,
823.
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