Open AccessS ‐Adenosylmethionine decarboxylase from the thermophilic archaebacterium Sulfolobus solfataricus
Author(s) -
CACCIAPUOTI Giovanna,
PORCELLI Marina,
ROSA Mario,
GAMBACORTA Agata,
BERTOLDO Costanzo,
ZAPPIA Vincenzo
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16136.x
Subject(s) - sulfolobus solfataricus , thermophile , biochemistry , enzyme , sulfolobus , putrescine , chemistry , biology , archaea , gene
S ‐Adenosylmethionine decarboxylase from Sulfolobus solfataricus , a thermoacidophilic archaebacterium optimally growing at 87°C, has been purified to homogeneity. The specific activity of the homogeneous enzyme is 12 nmol CO 2 formed min −1 (mg protein) −1 and the overall yield 8%. The enzyme is thermophilic with an optimum at 75°C, is thermostable, and does not require divalent cations or putrescine for activity. It has a molecular mass of 32 kDa, and appears to be a monomeric protein. S ‐Adenosylmethionine decarboxylase from S. solfataricus contains covalently linked pyruvate as prosthetic group and is inactivated in a time‐dependent process by NaCNBH 3 , in the presence of both the substrate and the product. Incubation with decarboxylated S ‐adenosyl[Me‐ 3 H]methionine and NaCNBH 3 resulted in the labeling of the protein at the active site.