The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution (Q27620493)

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English	The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution	scientific article

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The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution (English)

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Lubbert Dijkhuizen

object named as

L Dijkhuizen

4

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author name string

J C Uitdehaag

1

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K H Kalk

2

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B A van Der Veen

3

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B W Dijkstra

5

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language of work or name

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publication date

3 December 1999

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Journal of Biological Chemistry

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274

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49

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34868-76

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Structural and sequence-based classification of glycoside hydrolases

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https://api.crossref.org/works/10.1074%2FJBC.274.49.34868

21 January 2018

alpha-Amylase family: molecular biology and evolution

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21 January 2018

Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability

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Mechanisms of enzymatic glycoside hydrolysis

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X-ray structures along the reaction pathway of cyclodextrin glycosyltransferase elucidate catalysis in the alpha-amylase family

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21 January 2018

Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution

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Structure of cyclodextrin glycosyltransferase refined at 2.0 Å resolution

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Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form

1 reference

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The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251

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Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity

1 reference

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21 January 2018

Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin

1 reference

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21 January 2018

Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products

1 reference

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21 January 2018

X-ray structure of cyclodextrin glycosyltransferase complexed with acarbose. Implications for the catalytic mechanism of glycosidases

1 reference

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21 January 2018

Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1

1 reference

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Improved methods for building protein models in electron density maps and the location of errors in these models

1 reference

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Automated refinement of protein models

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21 January 2018

Errors in protein structures

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https://api.crossref.org/works/10.1074%2FJBC.274.49.34868

21 January 2018

The CCP4 suite: programs for protein crystallography

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PROCHECK: a program to check the stereochemical quality of protein structures

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The active center of a mammalian alpha-amylase. Structure of the complex of a pancreatic alpha-amylase with a carbohydrate inhibitor refined to 2.2-A resolution

1 reference

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21 January 2018

Structure of the Aspergillus oryzae alpha-amylase complexed with the inhibitor acarbose at 2.0 A resolution

1 reference

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21 January 2018

Four aromatic residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of replacements on substrate binding and cyclization characteristics.

1 reference

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21 January 2018

Conformational differences between alpha-cyclodextrin in aqueous solution and in crystalline form. A molecular dynamics study.

1 reference

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21 January 2018

Three histidine residues in the active center of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011: effects of the replacement on pH dependence and transition-state stabilization.

1 reference

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21 January 2018

Site-directed mutations in tyrosine 195 of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 affect activity and product specificity

1 reference

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21 January 2018

Studies of the inhibition by malto-oligosaccharides of the cyclisation reaction catalysed by the cyclodextrin glycosyltransferase from Klebsiella pneumoniae M 5 al with glycogen

1 reference

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21 January 2018

Studies of the mechanism of the cyclisation reaction catalysed by the wildtype and a truncated alpha-cyclodextrin glycosyltransferase from Klebsiella pneumoniae strain M 5 al, and the beta-cyclodextrin glycosyltransferase from Bacillus circulans str

1 reference

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Energy profile of maltooligosaccharide permeation through maltoporin as derived from the structure and from a statistical analysis of saccharide-protein interactions

1 reference

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Analysis of mutations in cyclodextrin glucanotransferase from Bacillus stearothermophilus which affect cyclization characteristics and thermostability.

1 reference

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Substrate binding to a cyclodextrin glycosyltransferase and mutations increasing the gamma-cyclodextrin production

1 reference

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Engineering of factors determining alpha-amylase and cyclodextrin glycosyltransferase specificity in the cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.

1 reference

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Improved Fourier coefficients for maps using phases from partial structures with errors

1 reference

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An amylose antiparallel double helix at atomic resolution

1 reference

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Structure and molecular model refinement of Aspergillus oryzae (TAKA) alpha-amylase: an application of the simulated-annealing method

1 reference

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Thermodynamics of the hydrolysis and cyclization reactions of alpha-, beta-, and gamma-cyclodextrin

1 reference

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Replacement of an amino acid residue of cyclodextrin glucanotransferase of Bacillus ohbensis doubles the production of gamma-cyclodextrin

1 reference

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21 January 2018

Cyclodextrins are not the major cyclic alpha-1,4-glucans produced by the initial action of cyclodextrin glucanotransferase on amylose

1 reference

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The role of histidine residues in the catalytic act of cyclomaltodextrin glucanotransferase from Bacillus circulans var. alkalophilus

1 reference

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21 January 2018

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10.1074/JBC.274.49.34868

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