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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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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S.Bozonnet,
M.T.Jensen,
M.M.Nielsen,
N.Aghajari,
M.H.Jensen,
B.Kramhøft,
M.Willemoës,
S.Tranier,
R.Haser,
and
B.Svensson
(2007).
The 'pair of sugar tongs' site on the non-catalytic domain C of barley alpha-amylase participates in substrate binding and activity.
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FEBS J, 274,
5055-5067.
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PDB codes:
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S.A.van Hijum,
S.Kralj,
L.K.Ozimek,
L.Dijkhuizen,
and
I.G.van Geel-Schutten
(2006).
Structure-function relationships of glucansucrase and fructansucrase enzymes from lactic acid bacteria.
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Microbiol Mol Biol Rev, 70,
157-176.
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Z.Wang,
Q.Qi,
and
P.G.Wang
(2006).
Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production.
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Appl Environ Microbiol, 72,
1873-1877.
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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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H.W.Choe,
K.S.Park,
J.Labahn,
J.Granzin,
C.J.Kim,
and
G.Büldt
(2003).
Crystallization and preliminary X-ray diffraction studies of alpha-cyclodextrin glucanotransferase isolated from Bacillus macerans.
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Acta Crystallogr D Biol Crystallogr, 59,
348-349.
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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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N.Pinotsis,
D.D.Leonidas,
E.D.Chrysina,
N.G.Oikonomakos,
and
I.M.Mavridis
(2003).
The binding of beta- and gamma-cyclodextrins to glycogen phosphorylase b: kinetic and crystallographic studies.
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Protein Sci, 12,
1914-1924.
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PDB codes:
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D.Zhang,
X.Li,
and
L.H.Zhang
(2002).
Isomaltulose synthase from Klebsiella sp. strain LX3: gene cloning and characterization and engineering of thermostability.
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Appl Environ Microbiol, 68,
2676-2682.
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G.Parsiegla,
A.Belaïch,
J.P.Belaïch,
and
R.Haser
(2002).
Crystal structure of the cellulase Cel9M enlightens structure/function relationships of the variable catalytic modules in glycoside hydrolases.
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Biochemistry, 41,
11134-11142.
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PDB codes:
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N.Rashid,
J.Cornista,
S.Ezaki,
T.Fukui,
H.Atomi,
and
T.Imanaka
(2002).
Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain.
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J Bacteriol, 184,
777-784.
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S.Kralj,
G.H.van Geel-Schutten,
H.Rahaoui,
R.J.Leer,
E.J.Faber,
M.J.van der Maarel,
and
L.Dijkhuizen
(2002).
Molecular characterization of a novel glucosyltransferase from Lactobacillus reuteri strain 121 synthesizing a unique, highly branched glucan with alpha-(1-->4) and alpha-(1-->6) glucosidic bonds.
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Appl Environ Microbiol, 68,
4283-4291.
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M.Hemker,
A.Stratmann,
K.Goeke,
W.Schröder,
J.Lenz,
W.Piepersberg,
and
H.Pape
(2001).
Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.
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J Bacteriol, 183,
4484-4492.
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T.Yokota,
T.Tonozuka,
S.Kamitori,
and
Y.Sakano
(2001).
The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 alpha-amylases: effects of domain N on activity, specificity, stability and dimerization.
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Biosci Biotechnol Biochem, 65,
401-408.
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T.Yokota,
T.Tonozuka,
Y.Shimura,
K.Ichikawa,
S.Kamitori,
and
Y.Sakano
(2001).
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
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Biosci Biotechnol Biochem, 65,
619-626.
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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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J.C.Uitdehaag,
G.J.van Alebeek,
B.A.van Der Veen,
L.Dijkhuizen,
and
B.W.Dijkstra
(2000).
Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
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Biochemistry, 39,
7772-7780.
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PDB codes:
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N.Ichikawa,
R.Fujisaka,
and
R.Kuribayashi
(2000).
Requirement for lysine-19 of the yeast mitochondrial ATPase inhibitor for the stability of the inactivated inhibitor-F1Fo complex at higher pH.
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Biosci Biotechnol Biochem, 64,
89-95.
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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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B.Mikami,
M.Adachi,
T.Kage,
E.Sarikaya,
T.Nanmori,
R.Shinke,
and
S.Utsumi
(1999).
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose.
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Biochemistry, 38,
7050-7061.
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PDB codes:
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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.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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K.Funane,
N.Libessart,
D.Stewart,
T.Michishita,
and
J.Preiss
(1998).
Analysis of essential histidine residues of maize branching enzymes by chemical modification and site-directed mutagenesis.
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J Protein Chem, 17,
579-590.
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R.Mosi,
H.Sham,
J.C.Uitdehaag,
R.Ruiterkamp,
B.W.Dijkstra,
and
S.G.Withers
(1998).
Reassessment of acarbose as a transition state analogue inhibitor of cyclodextrin glycosyltransferase.
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Biochemistry, 37,
17192-17198.
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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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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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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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686 a.a.
_CA
