EVIDENCE FOR A BROADLY-SPECIFIC, AMINO-ACID REQUIRING DEHYDROGENASE AT THE PYRUVATE BRANCHPOINT IN SEA-ANEMONES

The tissues of a number of species of sea anemones contain an enzyme(s) capable of oxidizing NADH in the presence of pyruvate and either L‐arginine or L‐alanine. The activities using either amino acid coelute on Sephadex G‐100 and DEAE‐Sephadex −50 columns. In addition, the peak DEAE‐Sephadex fractions utilize other amino acids including glycine, lysine and threonine. The above catalytic activities may be due to a single, broadly‐specific enzyme. Copyright © 1979 Wiley‐Liss, Inc., A Wiley Company