Abstract
The title compound (1c), was designed and synthesized based on mechanistic data concerning enzyme-catalyzed alkyl transfer reactions, applied in this case to aminopropyl transferases. The inhibition by 1c of one such enzyme, spermidine synthase, was both potent (I50 = 4 × 10−7M) and specific. A closely related aminopropyltransferase, spermine synthase was only minimally affected by high concentrations of 1c. Similar, although not as marked, specifity between the two aminopropyltransferases was observed with the corresponding methyl sulfonium salt, 2c. Studies with structurally related compounds support the hypothesis that the strong inhibition of spermidine synthase by 1c derives from the incorporation in this compound of important features of the transition-state structure of this enzyme-catalyzed reaction.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1371-1377 |
| Number of pages | 7 |
| Journal | Topics in Catalysis |
| Volume | 96 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jan 1 1980 |
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All Science Journal Classification (ASJC) codes
- Catalysis
- Chemistry(all)
- Biochemistry
- Biophysics
- Molecular Biology
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Specific and potent inhibition of spermidine synthase by the transition-state analog, S-adenosyl-3-thio-1,8-diaminooctane. / Tang, Kuo Chang; Pegg, Anthony; Coward, James K.
In: Topics in Catalysis, Vol. 96, No. 3, 01.01.1980, p. 1371-1377.Research output: Contribution to journal › Article
TY - JOUR
T1 - Specific and potent inhibition of spermidine synthase by the transition-state analog, S-adenosyl-3-thio-1,8-diaminooctane
AU - Tang, Kuo Chang
AU - Pegg, Anthony
AU - Coward, James K.
PY - 1980/1/1
Y1 - 1980/1/1
N2 - The title compound (1c), was designed and synthesized based on mechanistic data concerning enzyme-catalyzed alkyl transfer reactions, applied in this case to aminopropyl transferases. The inhibition by 1c of one such enzyme, spermidine synthase, was both potent (I50 = 4 × 10−7M) and specific. A closely related aminopropyltransferase, spermine synthase was only minimally affected by high concentrations of 1c. Similar, although not as marked, specifity between the two aminopropyltransferases was observed with the corresponding methyl sulfonium salt, 2c. Studies with structurally related compounds support the hypothesis that the strong inhibition of spermidine synthase by 1c derives from the incorporation in this compound of important features of the transition-state structure of this enzyme-catalyzed reaction.
AB - The title compound (1c), was designed and synthesized based on mechanistic data concerning enzyme-catalyzed alkyl transfer reactions, applied in this case to aminopropyl transferases. The inhibition by 1c of one such enzyme, spermidine synthase, was both potent (I50 = 4 × 10−7M) and specific. A closely related aminopropyltransferase, spermine synthase was only minimally affected by high concentrations of 1c. Similar, although not as marked, specifity between the two aminopropyltransferases was observed with the corresponding methyl sulfonium salt, 2c. Studies with structurally related compounds support the hypothesis that the strong inhibition of spermidine synthase by 1c derives from the incorporation in this compound of important features of the transition-state structure of this enzyme-catalyzed reaction.
UR - http://www.scopus.com/inward/record.url?scp=0019327232&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0019327232&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(80)90102-3
DO - 10.1016/0006-291X(80)90102-3
M3 - Article
C2 - 7437076
AN - SCOPUS:0019327232
VL - 96
SP - 1371
EP - 1377
JO - Topics in Catalysis
JF - Topics in Catalysis
IS - 3
ER -