Literature DB >> 1290942

Induced-fit movements in adenylate kinases.

G E Schulz1.   

Abstract

Adenylate kinases have an M(r) around 23,000 which classifies them among the smallest phosphoryl group transferring enzymes. In order to prevent phosphoryl transfer to water, i.e. hydrolysis, these enzymes undergo induced-fit motions on substrate binding and assemble/disassemble their catalytic centres during each reaction cycle. Details of these processes have been derived from several X-ray structure analyses. The disturbance of these analyses by crystal-packing effects is discussed.

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Year:  1992        PMID: 1290942     DOI: 10.1039/fd9929300085

Source DB:  PubMed          Journal:  Faraday Discuss        ISSN: 1359-6640            Impact factor:   4.008


  9 in total

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6.  Nicotinamide riboside kinase structures reveal new pathways to NAD+.

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7.  ATP and AMP mutually influence their interaction with the ATP-binding cassette (ABC) adenylate kinase cystic fibrosis transmembrane conductance regulator (CFTR) at separate binding sites.

Authors:  Christoph O Randak; Qian Dong; Amanda R Ver Heul; Adrian H Elcock; Michael J Welsh
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8.  Energetics and structural characterization of the large-scale functional motion of adenylate kinase.

Authors:  Elena Formoso; Vittorio Limongelli; Michele Parrinello
Journal:  Sci Rep       Date:  2015-02-12       Impact factor: 4.379

9.  Mutating the Conserved Q-loop Glutamine 1291 Selectively Disrupts Adenylate Kinase-dependent Channel Gating of the ATP-binding Cassette (ABC) Adenylate Kinase Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) and Reduces Channel Function in Primary Human Airway Epithelia.

Authors:  Qian Dong; Sarah E Ernst; Lynda S Ostedgaard; Viral S Shah; Amanda R Ver Heul; Michael J Welsh; Christoph O Randak
Journal:  J Biol Chem       Date:  2015-04-17       Impact factor: 5.157

  9 in total

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