Isolation of a thermostable enzyme catalyzing disulfide bond formation from the archaebacterium Sulfolobus solfataricus.
A disulfide bond-forming enzyme was purified from the cytosol of the archaebacterium Sulfolobus solfataricus, strain MT-4. The enzyme, assayed by its ability to oxidize and reactivate reductively denatured ribonuclease A, had a small molecular size and displayed a high thermostability. The N-terminal amino acid sequence is reported.
Guagliardi
A
A
Dipartimento di Chimica Organica e Biologica, Università di Napoli, Italy.
Cerchia
L
L
De Rosa
M
M
Rossi
M
M
Bartolucci
S
S
D000595:Amino Acid Sequence; D002384:Catalysis; D002853:Chromatography, Liquid; D004220:Disulfides / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D004789:Enzyme Activation; D004795:Enzyme Stability; D006358:Hot Temperature; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010088:Oxidoreductases / Q000302:isolation & purification / Q000378:metabolism*; D050862:Oxidoreductases Acting on Sulfur Group Donors; D012260:Ribonucleases / Q000378:metabolism; D016944:Sulfolobus / Q000201:enzymology*
D004220:Disulfides; D010088:Oxidoreductases; D050862:Oxidoreductases Acting on Sulfur Group Donors; D012260:Ribonucleases