Literature DB >> 15625870

Phosphoglycerate mutase has essential arginyl residues.

C L Borders1, B A Wilson.   

Abstract

Phosphoglycerate mutase is inactivated by butanedione in borate buffer. Inactivation by 0.13 mM reagent correlates with the modification of one arginyl residue per subunit, and is prevented by either 2, 3-diphosphoglycerate or 3-phosphoglycerate. With 0.50 mM butanedione, inactivation is accompanied by the modification of three arginyl residues per subunit, two of which are protected by the combined presence of cofactor and substrate.

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Year:  1976        PMID: 15625870     DOI: 10.1016/0006-291x(76)90218-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

1.  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

2.  Purification and properties of the manganese-dependent phosphoglycerate mutase of Bacillus subtilis.

Authors:  K Watabe; E Freese
Journal:  J Bacteriol       Date:  1979-02       Impact factor: 3.490

3.  The first case of a complete deficiency of diphosphoglycerate mutase in human erythrocytes.

Authors:  R Rosa; M O Prehu; Y Beuzard; J Rosa
Journal:  J Clin Invest       Date:  1978-11       Impact factor: 14.808

Review 4.  Arginyl residues and anion binding sites in proteins.

Authors:  J F Riordan
Journal:  Mol Cell Biochem       Date:  1979-07-31       Impact factor: 3.396

  4 in total

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