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The putative l ‐lactate dehydrogenase from Methanococcus jannaschii is an NADPH‐dependent l ‐malate dehydrogenase
Author(s) -
Madern Dominique
Publication year - 2000
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2000.02113.x
Subject(s) - methanococcus , biology , lactate dehydrogenase , open reading frame , malate dehydrogenase , biochemistry , dehydrogenase , enzyme , peptide sequence , branched chain alpha keto acid dehydrogenase complex , archaea , gene
The enyme encoded by Methanococcus jannaschii open reading frame (ORF) 0490 was purified and characterized. It was shown to be an NADPH‐dependent [lactate dehydrogenase (LDH)‐like] l ‐malate dehydrogenase (MalDH) and not an l ‐lactate dehydrogenase, as had been suggested previously on the basis of amino acid sequence similarity. The results show the importance of biochemical data in the assignment of ORF function in genomic sequences and have implications for the phylogenetic distribution of members of the MalDH/LDH enzyme superfamilies within the prokaryotic kingdom.