Literature DB >> 190679

Arginyl residues: anion recognition sites in enzymes.

J F Riordan, K D McElvany, C L Borders.   

Abstract

Chemical modification with 2,3-butanedione in borate buffer indicates that nine of ten glycolytic enzymes studied contain arginyl residues at their active sites. Fructose-1,6-diphosphatase also has arginines at its binding site for the allosteric inhibitor, adenosine monophosphate. These and other data suggest that, as a general rule, enzymes acting on anionic substrates or cofactors will probably contain arginyl residues as components of their ligand binding sites. This could account in part for the relatively infrequent occurrence of arginine in proteins.

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Year:  1977        PMID: 190679     DOI: 10.1126/science.190679

Source DB:  PubMed          Journal:  Science        ISSN: 0036-8075            Impact factor:   47.728


  66 in total

1.  Probing the location and function of the conserved histidine residue of phosphoglucose isomerase by using an active site directed inhibitor N-bromoacetylethanolamine phosphate.

Authors:  M Meng; T L Chane; Y J Sun; C D Hsiao
Journal:  Protein Sci       Date:  1999-11       Impact factor: 6.725

2.  Mutation analysis of the Pip interaction domain reveals critical residues for protein-protein interactions.

Authors:  M A Ortiz; J Light; R A Maki; N Assa-Munt
Journal:  Proc Natl Acad Sci U S A       Date:  1999-03-16       Impact factor: 11.205

3.  Interactions with the substrate phenolic group are essential for hydroxylation by the oxygenase component of p-hydroxyphenylacetate 3-hydroxylase.

Authors:  Chanakan Tongsook; Jeerus Sucharitakul; Kittisak Thotsaporn; Pimchai Chaiyen
Journal:  J Biol Chem       Date:  2011-11-03       Impact factor: 5.157

4.  Evidence for the importance of arginine residues in pig kidney alkaline phosphatase.

Authors:  M N Woodroofe; P J Butterworth
Journal:  Biochem J       Date:  1979-07-01       Impact factor: 3.857

5.  Structure-function studies on the interaction of PsaC with the Photosystem 1 heterodimer : The site directed change R561E in PsaB destabilizes the subunit interaction in Synechocystis sp. PCC 6803.

Authors:  S M Rodday; R Schulz; L McLntosh; J Biggins
Journal:  Photosynth Res       Date:  1994-12       Impact factor: 3.573

6.  Interactions of integrin GPIIb/IIIa-derived peptides with fibrinogen investigated by NMR spectroscopy.

Authors:  L J Yao; K H Mayo
Journal:  Biochem J       Date:  1996-04-01       Impact factor: 3.857

7.  Characterization of site-directed mutants of residues R58, R59, D116, W340 and R372 in the active site of E. coli cystathionine beta-lyase.

Authors:  Pratik H Lodha; Allison F Jaworski; Susan M Aitken
Journal:  Protein Sci       Date:  2010-03       Impact factor: 6.725

8.  Identification of amino acid residues essential for enzyme activity of sheep liver 5,10-methylenetetrahydrofolate reductase.

Authors:  K Varalakshmi; H S Savithri; N A Rao
Journal:  Biochem J       Date:  1986-05-15       Impact factor: 3.857

9.  Arginine residues are critical for the heparin-cofactor activity of antithrombin III.

Authors:  A M Jorgensen; C L Borders; W W Fish
Journal:  Biochem J       Date:  1985-10-01       Impact factor: 3.857

10.  Modification of C1- transport in skeletal muscle of Rana temporaria with the arginine-binding reagent phenylglyoxal.

Authors:  J M Skydsgaard
Journal:  J Physiol       Date:  1998-07-15       Impact factor: 5.182

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