Literature DB >> 4572991

Nuclear relaxation and kinetic studies of the role of Mn 2+ in the mechanism of enolase.

T Nowak, A S Mildvan, G L Kenyon.   

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Year:  1973        PMID： 4572991     DOI： 10.1021/bi00733a005

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  Calorimetric studies of the role of magnesium ions in yeast enolase catalysis.

Authors:  L D Faller; A M Johnson
Journal:  Proc Natl Acad Sci U S A       Date:  1974-04       Impact factor: 11.205

Review 2.  Unraveling the Structure and Mechanism of the MST(ery) Enzymes.

Authors:  Catherine L Shelton; Audrey L Lamb
Journal:  Trends Biochem Sci       Date:  2018-03-21       Impact factor: 13.807

3.  The active site of staphylococcal nuclease: paramagnetic relaxation of bound nucleotide inhibitor nuclei by lanthanide ions.

Authors:  B Furie; J H Griffin; R J Feldmann; E A Sokoloski; A N Schechter
Journal:  Proc Natl Acad Sci U S A       Date:  1974-07       Impact factor: 11.205

4.  The role of Mg2+ and Mn2+ in the enzyme-catalysed activation of nitrogenase Fe protein from Rhodospirillum rubrum.

Authors:  J H Guth; R H Burris
Journal:  Biochem J       Date:  1983-09-01       Impact factor: 3.857

5.  Phosphonomethyl analogues of phosphate ester glycolytic intermediates.

Authors:  H B Dixon; M J Sparkes
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857
  5 in total

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