1986
DOI: 10.1111/j.1432-1033.1986.tb10442.x
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Purification and characterization of propylamine transferase from Sulfolobus solfataricus, an extreme thermophilic archaebacterium

Abstract: The enzyme propylamine transferase, catalyzing the transfer of the propylamine moiety from S-adenosyl(5')-3-methylthiopropylamine to several amine acceptors, has been purified 643-fold in 20% yield from Sulfolobus solfaturicus, an extreme thermophilic archaebacterium optimally growing at 87 "C. The purified enzyme (specific activity 2.05 units/mg protein), is homogeneous by criteria of gel electrophoresis, gel filtration, isoelectric focusing and ultracentrifugation analysis. The molecular mass of the native e… Show more

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Cited by 31 publications
(31 citation statements)
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References 38 publications
(14 reference statements)
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“…The fifth equation can be obtained assuming that the enzyme possesses its maximum stability at a temperature near its maximum activity. It has been reported (Cacciapuoti et al, 1986) that propylamine transferase shows its activity maximum at about 87'C. Thus, we assume that form B, which is populated above 50 ' C , has its stability maximum at this temperature.…”
Section: Asu(k"); B+u(kuh)mentioning
confidence: 99%
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“…The fifth equation can be obtained assuming that the enzyme possesses its maximum stability at a temperature near its maximum activity. It has been reported (Cacciapuoti et al, 1986) that propylamine transferase shows its activity maximum at about 87'C. Thus, we assume that form B, which is populated above 50 ' C , has its stability maximum at this temperature.…”
Section: Asu(k"); B+u(kuh)mentioning
confidence: 99%
“…This is in agreement with and confirms the picture of the enzyme shown in the preceding paper (Facchiano et al, 1992). The structural reorganization at high temperature not only allows a better catalytic efficiency (Cacciapuoti et al, 1986), but also increases the enzyme stability. From Fig.…”
Section: Analysis Of Equilibriamentioning
confidence: 99%
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