Saccharomyces carlsbergensis enzyme activity

Candida utilis has high levels of NAD-GDH when grown on either glutamate or some other amino acids. Addition of either ammonia or glutamine to yeast so adapted can result in rapid and extensive inactivation of NAD-GDH at a faster rate than can be accounted for by the immediate cessation of enzyme synthesis (331). The NADP-GDH is not subject to rapid changes in activity under these conditions. In Saccharomyces carlsbergensis synthesis of NAD-GDH is also repressed by NH4+ and derepressed by glutamate the reverse is true for NADP-GDH (90,238). 

The properties of a-D-galactosidase (mol. wt. 3.0 x 10 ) from Saccharomyces carlsbergensis have been shown to be similar to those of other extracellular enzymes in yeast. The carbohydrate content (57 %) consists of D-mannose (ca. 92%), D-glucose (7%), and 2-amino-2-deoxy-D-glucose (1%) 35% of its amino acid residues can be accounted for by L-threonine, L-serine, and l-aspartic acid. Although the enzyme remains active after treatment with sodium dodecyl sulphate, it is denatured by urea and guanidinium chloride. With urea or 60 °C heat denaturation, the enzyme dissociates into two types of subunits and was therefore considered to be the first reported external enzyme from yeast with an oligomeric structure. 

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