Literature DB >> 2499329

Glucose-6-phosphate dehydrogenase. Characterization of a reactive lysine residue in the Pichia jadinii enzyme reveals a limited structural variation in a functionally significant segment.

J Jeffery1, I Wood, A Macleod, R Jeffery, H Jörnvall.   

Abstract

Glucose-6-phosphate dehydrogenase from the yeast Pichia jadinii has a reactive lysine residue in a segment of amino acid sequence Ile-Asp-His-Tyr-Leu-Gly-Lys*-Glu-Met-Val-Lys. This structure differs from that of other characterized glucose-6-phosphate dehydrogenases, but outside yeasts the segment is invariant in known mammalian, insect and bacterial forms. Thus, limited structural variation is now defined within yeasts for a part of the protein otherwise strictly conserved, and for which stringent structural requirements probably relate to enzymic mechanisms.

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Year:  1989        PMID: 2499329     DOI: 10.1016/s0006-291x(89)80143-3

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


  2 in total

1.  Eukaryotic glucose-6-phosphate dehydrogenases: structural screening of related proteins.

Authors:  T Bergman; H Jörnvall; I Wood; J Jeffery
Journal:  J Protein Chem       Date:  1991-02

2.  Cloning and sequence analysis of the glucose-6-phosphate dehydrogenase gene from the cyanobacterium Synechococcus PCC 7942.

Authors:  D J Scanlan; J Newman; M Sebaihia; N H Mann; N G Carr
Journal:  Plant Mol Biol       Date:  1992-08       Impact factor: 4.076

  2 in total

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