Literature DB >> 2043108

Different segment similarities in long-chain dehydrogenases.

B Persson1, J Jeffery, H Jörnvall.   

Abstract

Long-chain dehydrogenases were scrutinized for common patterns. Overall molecular similarities are not discerned, in contrast to the situation for several short-chain and medium-chain dehydrogenases, but coenzyme-binding segments are discernible. Species variants of glucose-6-phosphate dehydrogenase reveal about 20% strictly conserved residues, grouped into three segments and supporting assignments of sites for coenzyme-binding and catalysis. Glycine is overrepresented among the residues conserved, typical of distantly related proteins. Two of the enzymes within the pentose phosphate pathway reveal a distant similarity of interest for further evaluation, between a C-terminal 178-residue segment of glucose-6-phosphate dehydrogenase and the N-terminal part of 6-phosphogluconate dehydrogenase.

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Year:  1991        PMID: 2043108     DOI: 10.1016/0006-291x(91)91970-n

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


  2 in total

1.  A catalytic consensus motif for D-mannitol 2-dehydrogenase, a member of a polyol-specific long-chain dehydrogenase family, revealed by kinetic characterization of site-directed mutants of the enzyme from Pseudomonas fluorescens.

Authors:  Mario Klimacek; Bernd Nidetzky
Journal:  Biochem J       Date:  2002-10-01       Impact factor: 3.857

Review 2.  Medium- and short-chain dehydrogenase/reductase gene and protein families : the SDR superfamily: functional and structural diversity within a family of metabolic and regulatory enzymes.

Authors:  K L Kavanagh; H Jörnvall; B Persson; U Oppermann
Journal:  Cell Mol Life Sci       Date:  2008-12       Impact factor: 9.261

  2 in total

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