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Literature summary extracted from

  • Irimia, A.; Vellieux, F.M.; Madern, D.; Zaccai, G.; Karshikoff, A.; Tibbelin, G.; Ladenstein, R.; Lien, T.; Birkeland, N.K.
    The 2.9 A resolution crystal structure of malate dehydrogenase from Archaeoglobus fulgidus: mechanisms of oligomerisation and thermal stabilisation (2004), J. Mol. Biol., 335, 343-356.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.37 sitting drop method, crystal structure in complex with NAD+ solved at 2.9 A resolution. Crystal structure shows a compact homodimer with one coenzyme bound per subunit Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.37 Archaeoglobus fulgidus
-
-
-

Subunits

EC Number Subunits Comment Organism
1.1.1.37 dimer crystal structure shows a compact homodimer with one coenzyme bound per subunit. The crystal structure reveals that the association of the dimers to form tetramers is prevented by several deletions, taking place at the level of two loops that are known to be essential for the tetramerization process within the LDH and malDH enzymes Archaeoglobus fulgidus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.37 NAD+
-
Archaeoglobus fulgidus