Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1 (Q27748894)

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

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

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Thermoanaerobacterium thermosulfurigenes

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Thermoanaerobacterium thermosulfurigenes

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Lubbert Dijkhuizen

object named as

L Dijkhuizen

5

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author name string

R D Wind

1

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J C Uitdehaag

2

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R M Buitelaar

3

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B W Dijkstra

4

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publication date

6 March 1998

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Journal of Biological Chemistry

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273

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10

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5771-9

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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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Crystal structure at 2.3 A resolution and revised nucleotide sequence of the thermostable cyclodextrin glycosyltransferase from Thermonanaerobacterium thermosulfurigenes EM1

1 reference

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X-ray structure of cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011. Comparison of two independent molecules at 1.8 A resolution.

1 reference

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

1 reference

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

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Structures and mechanisms of glycosyl hydrolases

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

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

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

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Catalytic center of cyclodextrin glycosyltransferase derived from X-ray structure analysis combined with site-directed mutagenesis

1 reference

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Assessment of phase accuracy by cross validation: the free R value. Methods and applications

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

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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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Automated refinement of protein models

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

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Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors

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DNA sequencing with chain-terminating inhibitors

1 reference

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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.

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

1 reference

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STEREOCHEMISTRY AND THE MECHANISM OF ENZYMATIC REACTIONS

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Accurate bond and angle parameters for X-ray protein structure refinement

1 reference

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

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Effect of mutation of an amino acid residue near the catalytic site on the activity of Bacillus stearothermophilus alpha-amylase

1 reference

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Arytetralin lignans from Linum catharticum L.

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Repeating use of Chalara paradoxa amylase by alpha-cyclodextrin affinity column

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10.1074/JBC.273.10.5771

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