Arylsulphatase from Alteromonas carrageenovora

Article Abstract:

Arylsulphatase produced by the marine bacteria Alteromonas carrageenovora has 304 amino acids, 33100 Da molecular mass and 68 micro M Michaelis constant. The protein produced by the open reading frame of the atsA gene, that encodes the enzyme, is processed to form the mature enzyme. The activity of the enzyme is unaffected by sulphate ions and cysteine. The structure of the enzyme is similar to proteins produced by the pathogenic bacteria Mycobacterium leprae and Porphyromonas gingivalis. The enzyme hydrolyzes arylsulphate esters to provide sulphate.

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Alpha-agarases define a new family of glycoside hydrolases, distinct from beta-agarase families

Article Abstract:

The cloning and sequencing of the gene encoding [alpha]-agarase from Alteromonas agarilytica is discussed. Findings reveal the display of a complex modularity by [alpha]-agarase with the presence of five thrombospondin type 3 repeats and three carbohydrate-binding modules.

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Characterization and synergistic interactions of Fibrobacter succinogenes glycoside hydrolases

Article Abstract:

The synergistic interactions and characteristics among five cellulases from different glycoside hydrolase families of Fibrobacter succinogenes were examined. Results concluded that the mixtures holding greater amount of enzymes showed high level of synergism.

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