ABSTRACT: Ectoaminopeptidase activities of pelagic marine microbial communities were investigated on several research cruises in the western Antarctic Peninsula region from 1992 to 1994, using the fluorigenic substrate analogue L-leucyl-b-naphthylamine. K_m values at in situ temperature were comparable to those observed by other investigators for a variety of aquatic environments. Competitive inhibition by dipeptides of a variety of amino acids showed that the aminopeptidases present were broadly specific; no strong tendency toward greater affinity for hydrophobic or hydrophilic amino acids was observed. Seawater cultures (1.0 µm filtrate) were inoculated with a variety of monomeric organic compounds and incubated for 24 to 72 h prior to activity determination; histidine and phenylalanine were found to consistently inhibit aminopeptidase expression. It is hypothesized that auxotrophy for histidine and phenylalanine may be widespread in these assemblages, giving rise to high levels of constitutive, nonspecific aminopeptidase activity which results in significant respiration of the more common amino acids. Whatever the exact mechanism, aminopeptidase activity is strongly affected by the specific compounds present and not simply by the carbon-to-nitrogen ratio.

KEY WORDS: Aminopeptidase · Enzyme specificity · Enzyme regulation · Antarctica

Published in AME Vol. 15, No. 3 (1998) on August 31
ISSN: 0948-3055. Copyright © Inter-Research, Oldendorf/Luhe, 1998