Literature DB >> 10998181

The putative L-lactate dehydrogenase from Methanococcus jannaschii is an NADPH-dependent L-malate dehydrogenase.

D Madern1.   

Abstract

The enzyme 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.

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Year:  2000        PMID: 10998181     DOI: 10.1046/j.1365-2958.2000.02113.x

Source DB:  PubMed          Journal:  Mol Microbiol        ISSN: 0950-382X            Impact factor:   3.501


  4 in total

1.  Methanoarchaeal sulfolactate dehydrogenase: prototype of a new family of NADH-dependent enzymes.

Authors:  Adriana Irimia; Dominique Madern; Giuseppe Zaccaï; Frédéric M D Vellieux
Journal:  EMBO J       Date:  2004-03-11       Impact factor: 11.598

2.  Pcal_1699, an extremely thermostable malate dehydrogenase from hyperthermophilic archaeon Pyrobaculum calidifontis.

Authors:  Ghazaleh Gharib; Naeem Rashid; Qamar Bashir; Qura-Tul Ann Afza Gardner; Muhammad Akhtar; Tadayuki Imanaka
Journal:  Extremophiles       Date:  2015-10-28       Impact factor: 2.395

3.  Desulfovibrio sp. genes involved in the respiration of sulfate during metabolism of hydrogen and lactate.

Authors:  Jennifer L Steger; Carr Vincent; Jimmy D Ballard; Lee R Krumholz
Journal:  Appl Environ Microbiol       Date:  2002-04       Impact factor: 4.792

4.  Fundamental and biotechnological applications of neutron scattering measurements for macromolecular dynamics.

Authors:  Moeava Tehei; Roy Daniel; Giuseppe Zaccai
Journal:  Eur Biophys J       Date:  2006-07-26       Impact factor: 1.733

  4 in total

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