Literature references that cite this PDB file's
key reference
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PubMed id
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Reference
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H.Leemhuis,
R.M.Kelly,
and
L.Dijkhuizen
(2010).
Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications.
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Appl Microbiol Biotechnol, 85,
823-835.
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C.Christiansen,
M.Abou Hachem,
S.Janecek,
A.Viksø-Nielsen,
A.Blennow,
and
B.Svensson
(2009).
The carbohydrate-binding module family 20--diversity, structure, and function.
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FEBS J, 276,
5006-5029.
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Y.H.Liu,
F.P.Lu,
Y.Li,
J.L.Wang,
and
C.Gao
(2008).
Acid stabilization of Bacillus licheniformis alpha amylase through introduction of mutations.
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Appl Microbiol Biotechnol, 80,
795-803.
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Y.H.Liu,
F.P.Lu,
Y.Li,
X.B.Yin,
Y.Wang,
and
C.Gao
(2008).
Characterisation of mutagenised acid-resistant alpha-amylase expressed in Bacillus subtilis WB600.
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Appl Microbiol Biotechnol, 78,
85-94.
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Q.Qi,
and
W.Zimmermann
(2005).
Cyclodextrin glucanotransferase: from gene to applications.
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Appl Microbiol Biotechnol, 66,
475-485.
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J.E.Nielsen,
and
J.A.McCammon
(2003).
Calculating pKa values in enzyme active sites.
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Protein Sci, 12,
1894-1901.
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H.Mori,
K.S.Bak-Jensen,
and
B.Svensson
(2002).
Barley alpha-amylase Met53 situated at the high-affinity subsite -2 belongs to a substrate binding motif in the beta-->alpha loop 2 of the catalytic (beta/alpha)8-barrel and is critical for activity and substrate specificity.
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Eur J Biochem, 269,
5377-5390.
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A.M.Brzozowski,
D.M.Lawson,
J.P.Turkenburg,
H.Bisgaard-Frantzen,
A.Svendsen,
T.V.Borchert,
Z.Dauter,
K.S.Wilson,
and
G.J.Davies
(2000).
Structural analysis of a chimeric bacterial alpha-amylase. High-resolution analysis of native and ligand complexes.
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Biochemistry, 39,
9099-9107.
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PDB codes:
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B.A.van der Veen,
G.J.van Alebeek,
J.C.Uitdehaag,
B.W.Dijkstra,
and
L.Dijkhuizen
(2000).
The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms.
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Eur J Biochem, 267,
658-665.
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N.Ishii,
K.Haga,
K.Yamane,
and
K.Harata
(2000).
Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 determined at 1.9 A resolution.
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J Mol Recognit, 13,
35-43.
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PDB code:
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E.H.Rydberg,
G.Sidhu,
H.C.Vo,
J.Hewitt,
H.C.Côte,
Y.Wang,
S.Numao,
R.T.MacGillivray,
C.M.Overall,
G.D.Brayer,
and
S.G.Withers
(1999).
Cloning, mutagenesis, and structural analysis of human pancreatic alpha-amylase expressed in Pichia pastoris.
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Protein Sci, 8,
635-643.
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PDB code:
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G.P.De Montalk,
M.Remaud-Simeon,
R.M.Willemot,
V.Planchot,
and
P.Monsan
(1999).
Sequence analysis of the gene encoding amylosucrase from Neisseria polysaccharea and characterization of the recombinant enzyme.
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J Bacteriol, 181,
375-381.
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H.D.Ly,
and
S.G.Withers
(1999).
Mutagenesis of glycosidases.
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Annu Rev Biochem, 68,
487-522.
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J.Abe,
C.Ushijima,
and
S.Hizukuri
(1999).
Expression of the isoamylase gene of Flavobacterium odoratum KU in Escherichia coli and identification of essential residues of the enzyme by site-directed mutagenesis.
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Appl Environ Microbiol, 65,
4163-4170.
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J.E.Nielsen,
L.Beier,
D.Otzen,
T.V.Borchert,
H.B.Frantzen,
K.V.Andersen,
and
A.Svendsen
(1999).
Electrostatics in the active site of an alpha-amylase.
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Eur J Biochem, 264,
816-824.
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A.K.Schmidt,
S.Cottaz,
H.Driguez,
and
G.E.Schulz
(1998).
Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin.
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Biochemistry, 37,
5909-5915.
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PDB code:
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R.D.Wind,
J.C.Uitdehaag,
R.M.Buitelaar,
B.W.Dijkstra,
and
L.Dijkhuizen
(1998).
Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.
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J Biol Chem, 273,
5771-5779.
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PDB code:
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K.S.Devulapalle,
S.D.Goodman,
Q.Gao,
A.Hemsley,
and
G.Mooser
(1997).
Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci.
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Protein Sci, 6,
2489-2493.
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R.Mosi,
S.He,
J.Uitdehaag,
B.W.Dijkstra,
and
S.G.Withers
(1997).
Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme.
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Biochemistry, 36,
9927-9934.
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S.Arming,
B.Strobl,
C.Wechselberger,
and
G.Kreil
(1997).
In vitro mutagenesis of PH-20 hyaluronidase from human sperm.
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Eur J Biochem, 247,
810-814.
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B.Strokopytov,
R.M.Knegtel,
D.Penninga,
H.J.Rozeboom,
K.H.Kalk,
L.Dijkhuizen,
and
B.W.Dijkstra
(1996).
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity.
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Biochemistry, 35,
4241-4249.
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PDB codes:
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T.Kuriki,
H.Kaneko,
M.Yanase,
H.Takata,
J.Shimada,
S.Handa,
T.Takada,
H.Umeyama,
and
S.Okada
(1996).
Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center.
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J Biol Chem, 271,
17321-17329.
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A.J.Jacks,
K.Sorimachi,
M.F.Le Gal-Coëffet,
G.Williamson,
D.B.Archer,
and
M.P.Williamson
(1995).
1H and 15N assignments and secondary structure of the starch-binding domain of glucoamylase from Aspergillus niger.
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Eur J Biochem, 233,
568-578.
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R.D.Wind,
W.Liebl,
R.M.Buitelaar,
D.Penninga,
A.Spreinat,
L.Dijkhuizen,
and
H.Bahl
(1995).
Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase.
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Appl Environ Microbiol, 61,
1257-1265.
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R.M.Knegtel,
B.Strokopytov,
D.Penninga,
O.G.Faber,
H.J.Rozeboom,
K.H.Kalk,
L.Dijkhuizen,
and
B.W.Dijkstra
(1995).
Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
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J Biol Chem, 270,
29256-29264.
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PDB codes:
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S.G.Withers,
and
R.Aebersold
(1995).
Approaches to labeling and identification of active site residues in glycosidases.
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Protein Sci, 4,
361-372.
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B.Svensson
(1994).
Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability.
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Plant Mol Biol, 25,
141-157.
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K.W.Rodenburg,
N.Juge,
X.J.Guo,
M.Søgaard,
J.C.Chaix,
and
B.Svensson
(1994).
Domain B protruding at the third beta strand of the alpha/beta barrel in barley alpha-amylase confers distinct isozyme-specific properties.
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Eur J Biochem, 221,
277-284.
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H.M.Jespersen,
E.A.MacGregor,
B.Henrissat,
M.R.Sierks,
and
B.Svensson
(1993).
Starch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.
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J Protein Chem, 12,
791-805.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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684 a.a.
_CA
