Putrescine or spermidine binding site of aminopropyltransferases and competitive inhibitors.
Biochem Pharmacol
; 41(2): 205-12, 1991 Jan 15.
Article
em En
| MEDLINE
| ID: mdl-1989632
ABSTRACT
A model of the active site of aminopropyltransferases was proposed based on the study of a number of monoamino and diamino compounds as potential inhibitors and substrates, respectively, of spermidine synthase purified from pig liver. The active site seems to have a relatively large hydrophobic cavity adjacent to a negatively charged site, to which a protonated amino group of putrescine binds, with another amino group of putrescine being situated in the hydrophobic cavity as a free form to be aminopropylated by decarboxylated S-adenosylmethionine. On the basis of the above-mentioned model, another modified one was proposed for spermine synthase, and several compounds mentioned model, another modified one was proposed for spermine synthase, and several compounds designed according to the modified model were found to potently inhibit spermine synthase, purified from rat brain, in competition with spermidine. The newly developed inhibitors were about two orders of magnitude more potent in vitro than a known inhibitor of spermine synthase, dimethyl(5'-adenosyl)sulfonium perchlorate.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Espermidina Sintase
/
Espermina Sintase
/
Putrescina
/
Espermidina
/
Cicloexilaminas
Limite:
Animals
Idioma:
En
Revista:
Biochem Pharmacol
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
Japão