Alteromonas haloplanktis

Bisucaberin (48) from Alteromonas haloplanktis (181) is a cyclic dimer of succinyl-((V-hydroxycadaverin) (348) cf. the cyclic trimer proferrioxamine E (Table 6). 

A very large number of enzymes show an absolute requirement for a monovalent cation for catalytic activity, and for most of these K+ is most effective.90,91 Usually Na+ is inactive but a small number of enzymes [apart from (Na+, K+)-ATPase] have a specific requirement for Na+, such as oxaloacetate decarboxylase.92 The oxidation of NAD-linked substrates by the aerobic marine bacterium Alteromonas haloplanktis requires the presence of Na+.93 Monovalent ions other than Na+ can usually replace K+ but with lowered activity. The Rb+ cation usually substitutes quite effectively, but there has been much interest in replacing K+ with Tl+, in order to exploit the NMR properties of the latter cation. T + sometimes causes inhibition, as it binds more strongly than K+ and sometimes to additional sites, reflecting its soft chemical character. On occasions Tl+ may activate an enzyme more effectively than the native K+. Some examples of enzymes activated by monovalent cations are given in Table 5. 

Biodispersion Alteromonas sp. Alteromonas haloplanktis Alteromonas madeodii Heteropolysaccharide containing repeating tetrasaccharide units [L-Rha —> 2-acetamido —> 2-deoxy-D-Glu —> 3-0-[(R)-l-carboxyethyl]-D-Glu] [o-Gal —> 3-0-acetyl-2-acetamido-2-deoxy-DGIu —> 2-acetamido-2-deoxy-L-guluronic acid —> 3,6-dideoxy-3-(4-hydroxybutyramido)-D-Gal]... 

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