Literature DB >> 20443

Allosteric interactions between metal ion and phosphate at the active sites of alkaline phosphatase as determined by 31P NMR and 113Cd NMR.

J F Chlebowski, I M Armitage, J E Coleman.   

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Year:  1977        PMID： 20443

Source DB:  PubMed          Journal:  J Biol Chem        ISSN： 0021-9258            Impact factor:   5.157


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  5 in total

Review 1.  Use of (113)Cd NMR to probe the native metal binding sites in metalloproteins: an overview.

Authors:  Ian M Armitage; Torbjörn Drakenberg; Brian Reilly
Journal:  Met Ions Life Sci       Date:  2013

2.  Cadmium-113 FT NMR-spectra of rabbit liver metallothioneins.

Authors:  K T Suzuki; T Maitani
Journal:  Experientia       Date:  1978-11-15

3.  Isotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization.

Authors:  Logan D Andrews; Hua Deng; Daniel Herschlag
Journal:  J Am Chem Soc       Date:  2011-07-13       Impact factor: 15.419

4.  A phoA structural gene mutation that conditionally affects formation of the enzyme bacterial alkaline phosphatase.

Authors:  D K Agrawal; B L Wanner
Journal:  J Bacteriol       Date:  1990-06       Impact factor: 3.490

5.  Phosphate binding in the active site of alkaline phosphatase and the interactions of 2-nitrosoacetophenone with alkaline phosphatase-induced small structural changes.

Authors:  Le Zhang; René Buchet; Gérard Azzar
Journal:  Biophys J       Date:  2004-06       Impact factor: 4.033
  5 in total

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