Escherichia coli β-Galactosidase Recognizes a High-Energy Conformation of C-Lactose, a Nonhydrolizable Substrate Analogue. NMR and Modeling Studies of the Molecular Complex-Reference-Cited by-同舟云学术

Escherichia coli β-Galactosidase Recognizes a High-Energy Conformation of C-Lactose, a Nonhydrolizable Substrate Analogue. NMR and Modeling Studies of the Molecular Complex

Published:1998-02-01 Issue:6 Volume:120 Page:1309-1318
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Espinosa J. F.¹,Montero E.¹,Vian A.¹,García J. L.¹,Dietrich H.¹,Schmidt R. R.¹,Martín-Lomas M.¹,Imberty A.¹,Cañada F. J.¹,Jiménez-Barbero J.¹

Affiliation:

1. Contribution from the Departmento Química Orgánica Biológica, Instituto Química Orgánica, CSIC, Juan de la Cierva 3, 28006 Madrid, Spain, CIBCSIC, Velazquez, 28006 Madrid, Spain, Fak. Chemie, University Konstanz, Germany, Instituto de Investigaciones Químicas, CSIC, Isla de la Cartuja, Sevilla, Spain, and CERMAVCNRS, Grenoble, France

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/ja972291q

Reference47 articles.

1. Catalytic mechanism of enzymic glycosyl transfer

2. The active site and mechanism of the β-galactosidase from Escherichia coli

3. Correction: A map of a collisionally evolving dust disk around Fomalhaut

4. Symposium on Three-Dimensional Structure of Macromolecules of Biological Origin. by Invitation of the Committee on Arrangements for the Autumn Meeting. Presented before the Academy on October 19, 1966. Chairman, Walter Kauzmann: THE HEN EGG-WHITE LYSOZYME MOLECULE

5. Author Index

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