Details

Autor(en) / Beteiligte

• Genda, Tomoko
• Nakamatsu, Tsuyoshi
• Ozak, Hachiro

Titel

Purification and characterization of malate dehydrogenase from Corynebacterium glutamicum

Ist Teil von

• Journal of bioscience and bioengineering, 2003, Vol.95 (6), p.562-566

Ort / Verlag

Japan: Elsevier B.V

Erscheinungsjahr

2003

Quelle

Alma/SFX Local Collection

Beschreibungen/Notizen

• The malate dehydrogenase (MDH) (EC 1.1.1.37) from Corynebacterium glutamicum ( Brevibacterium flavum) ATCC14067 was purified to homogeneity. Its amino-terminal sequence (residues 1 to 8) matched the sequence (residues 2 to 9) of the MDH from C. glutamicum (GenBank accession no. CAC83073). The molecular mass of the native enzyme was 130 kDa. The protein was a homotetramer, with a 33-kDa subunit molecular mass. The enzyme was almost equally active both for NADU andNADPH as coenzyme on the bases of the k cat values at pH 6.5 which is the optimum pH for the both coenzymes. Plotting of the logarithms of the 1/Km, ke, and k cat K m values with respect to oxalacetate against pH lead to speculation that imidazolium is possibly a functional group in the active center of the enzyme. Citrate activated the enzyme in the oxidation of malate to oxalacetate and inhibited it in the reverse reaction.