Crystal Structure of Holo Inorganic Pyrophosphatase from Escherichia coli at 1.9 Å Resolution. Mechanism of Hydrolysis-Reference-Cited by-同舟云学术

Crystal Structure of Holo Inorganic Pyrophosphatase from Escherichia coli at 1.9 Å Resolution. Mechanism of Hydrolysis

Published:1997-06-01 Issue:25 Volume:36 Page:7754-7760
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Harutyunyan Emil H.¹,Oganessyan Vaheh Yu.¹,Oganessyan Natalya N.¹,Avaeva Svetlana M.¹,Nazarova Tatyana I.¹,Vorobyeva Natalya N.¹,Kurilova Svetlana A.¹,Huber Robert¹,Mather Timothy¹

Affiliation:

1. Shubnikov Institute of Crystallography, Russian Academy of Sciences, Leninski pr. 59, 117333 Moscow, Russian Federation, A. N. Belozersky Institute of Physico-Chemical Biology, Moscow State University, 119899, Moscow, Russian Federation, and Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18A, 82152, Martinsried, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi962637u

Reference21 articles.

1. Mg2+ activation of Escherichia coli inorganic pyrophosphatase

2. Two pathways of pyrophosphate hydrolysis and synthesis by yeast inorganic pyrophosphatase

3. Kinetics and thermodynamics of catalysis by the inorganic pyrophosphatase of Escherichia coli in both directions

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