Literature DB >> 9562560

How do kinases transfer phosphoryl groups?

A Matte1, L W Tari, L T Delbaere.   

Abstract

Understanding how phosphoryl transfer is accomplished by kinases, a ubiquitous group of enzymes, is central to many biochemical processes. Qualitative analysis of the crystal structures of enzyme-substrate complexes of kinases reveals structural features of these enzymes important to phosphoryl transfer. Recently determined crystal structures which mimic the transition state complex have added new insight into the debate as to whether kinases use associative or dissociative mechanisms of catalysis.

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Year:  1998        PMID: 9562560     DOI: 10.1016/s0969-2126(98)00043-4

Source DB:  PubMed          Journal:  Structure        ISSN: 0969-2126            Impact factor:   5.006


  43 in total

1.  Protein folding and function: the N-terminal fragment in adenylate kinase.

Authors:  S Kumar; Y Y Sham; C J Tsai; R Nussinov
Journal:  Biophys J       Date:  2001-05       Impact factor: 4.033

Review 2.  Biological phosphoryl-transfer reactions: understanding mechanism and catalysis.

Authors:  Jonathan K Lassila; Jesse G Zalatan; Daniel Herschlag
Journal:  Annu Rev Biochem       Date:  2011       Impact factor: 23.643

Review 3.  6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase: head-to-head with a bifunctional enzyme that controls glycolysis.

Authors:  Mark H Rider; Luc Bertrand; Didier Vertommen; Paul A Michels; Guy G Rousseau; Louis Hue
Journal:  Biochem J       Date:  2004-08-01       Impact factor: 3.857

4.  Ultrahigh and high resolution structures and mutational analysis of monomeric Streptococcus pyogenes SpeB reveal a functional role for the glycine-rich C-terminal loop.

Authors:  Gonzalo E González-Páez; Dennis W Wolan
Journal:  J Biol Chem       Date:  2012-05-29       Impact factor: 5.157

5.  Structural studies of ROK fructokinase YdhR from Bacillus subtilis: insights into substrate binding and fructose specificity.

Authors:  B Nocek; A J Stein; R Jedrzejczak; M E Cuff; H Li; L Volkart; A Joachimiak
Journal:  J Mol Biol       Date:  2010-12-23       Impact factor: 5.469

6.  The crystal structure of beryllofluoride Spo0F in complex with the phosphotransferase Spo0B represents a phosphotransfer pretransition state.

Authors:  Kottayil I Varughese; Igor Tsigelny; Haiyan Zhao
Journal:  J Bacteriol       Date:  2006-07       Impact factor: 3.490

7.  Molecular basis of 1,6-anhydro bond cleavage and phosphoryl transfer by Pseudomonas aeruginosa 1,6-anhydro-N-acetylmuramic acid kinase.

Authors:  John-Paul Bacik; Garrett E Whitworth; Keith A Stubbs; Anuj K Yadav; Dylan R Martin; Ben A Bailey-Elkin; David J Vocadlo; Brian L Mark
Journal:  J Biol Chem       Date:  2011-02-02       Impact factor: 5.157

Review 8.  Structural insights into the mechanism of phosphoenolpyruvate carboxykinase catalysis.

Authors:  Gerald M Carlson; Todd Holyoak
Journal:  J Biol Chem       Date:  2009-07-27       Impact factor: 5.157

9.  The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine: a thermodynamic analysis.

Authors:  Randy B Stockbridge; Richard Wolfenden
Journal:  J Biol Chem       Date:  2009-06-15       Impact factor: 5.157

10.  Crystal structure of a trimeric form of dephosphocoenzyme A kinase from Escherichia coli.

Authors:  Nicholas O'Toole; João A R G Barbosa; Yunge Li; Li-Wei Hung; Allan Matte; Miroslaw Cygler
Journal:  Protein Sci       Date:  2003-02       Impact factor: 6.725

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