Literature DB >> 215219

Properties of adenylate kinase after modification of Arg-97 by phenylglyoxal.

J Berghäuser, R H Schirmer.   

Abstract

Adenylate kinase (ATP:AMP phosphotransferase, EC 2.7.4.3) isolated from porcine skeletal and heart muscle and from rabbit muscle are inactivated when a single arginine residue is modified. In adenylate kinase from pig the modified residue was identified as Arg-97 by peptide-mapping. In native adenylate kinase Arg-97 is located at the bottom of the active site cleft. The protein fluorescence of modified adenylate kinase is reduced. Whereas the addition of AMP, ADP and MgATP quench the fluorescence of native adenylate kinase, the fluorescence of phenylglyoxal-modified adenylate kinase is only affected by ADP and MgATP. This finding is discussed in connection with the structural isomerization observed in native adenylate kinase by X-ray diffraction analysis.

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Year:  1978        PMID: 215219     DOI: 10.1016/0005-2795(78)90527-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  1 in total

1.  An essential arginine residue for initiation of protein-primed DNA replication.

Authors:  J C Hsieh; S K Yoo; J Ito
Journal:  Proc Natl Acad Sci U S A       Date:  1990-11       Impact factor: 11.205

  1 in total

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