skip to main content
Visitante
Meu Espaço
Minha Conta
Sair
Identificação
This feature requires javascript
Tags
Revistas Eletrônicas (eJournals)
Livros Eletrônicos (eBooks)
Bases de Dados
Bibliotecas USP
Ajuda
Ajuda
Idioma:
Inglês
Espanhol
Português
This feature required javascript
This feature requires javascript
Primo Search
Busca Geral
Busca Geral
Acervo Físico
Acervo Físico
Produção Intelectual da USP
Produção USP
Search For:
Clear Search Box
Search in:
Busca Geral
Or select another collection:
Search in:
Busca Geral
Busca Avançada
Busca por Índices
This feature requires javascript
This feature requires javascript
Mapping of the Active Sites of Transglutaminases
Gross, Michael ; Folk, J.E.
The Journal of biological chemistry, 1973-02, Vol.248 (4), p.1301-1306
[Periódico revisado por pares]
Elsevier Inc
Texto completo disponível
Citações
Citado por
Exibir Online
Detalhes
Resenhas & Tags
Mais Opções
Nº de Citações
This feature requires javascript
Enviar para
Adicionar ao Meu Espaço
Remover do Meu Espaço
E-mail (máximo 30 registros por vez)
Imprimir
Link permanente
Referência
EasyBib
EndNote
RefWorks
del.icio.us
Exportar RIS
Exportar BibTeX
This feature requires javascript
Título:
Mapping of the Active Sites of Transglutaminases
Autor:
Gross, Michael
;
Folk, J.E.
É parte de:
The Journal of biological chemistry, 1973-02, Vol.248 (4), p.1301-1306
Descrição:
Calcium-activated guinea pig liver transglutaminase catalyzes the incorporation of amines at the carboxamide group of several aliphatic amides. Initial velocity findings with n-valeramide and methylamine as substrates are consistent with a modified double displacement mechanism for this reaction. This mechanism has already been demonstrated for amine incorporation at the γ-carboxamide group of peptide-bound glutamine (Folk, J. E. (1969) J. Biol. Chem. 244, 3707). Inhibition patterns for aliphatic amides suggest that binding of these compounds occurs at the site in the enzyme to which the carboxamide side chain of peptide-bound glutamine residues attaches. All of the straight-chain amides tested proved to be substrates with the exception of formamide. Branched-chain amides in which there is a methyl group in the α or β position of the methylene side chain are not substrates; those with methyl groups on the γ-carbon of the side chain are. These observations and their consideration lead to the suggestion that peptide-bound glutamine attaches to the enzyme with its β and γ methylene groups situated in a hydrophobic binding region and with its carboxamide group directed toward the active site —SH group of the enzyme. The dimensions of this site preclude the productive binding of peptide-bound asparagine. An active site pocket of fixed dimensions into which the carboxamide group and methylene side chain of substrate must be injected and from which product must be extruded is not consistent with the substrate specificity of the enzyme or with the ready dissociation of many products. This, taken together with present observations, favors an hypothesis of an essential substrate-induced conformational change in the active site of the enzyme that precedes or accompanies enzyme acylation.
Editor:
Elsevier Inc
Idioma:
Inglês
This feature requires javascript
This feature requires javascript
Voltar para lista de resultados
Anterior
Resultado
6
Avançar
This feature requires javascript
This feature requires javascript
Buscando em bases de dados remotas. Favor aguardar.
Buscando por
em
scope:(USP_PRODUCAO),scope:(USP_EBOOKS),scope:("PRIMO"),scope:(USP),scope:(USP_EREVISTAS),scope:(USP_FISICO),primo_central_multiple_fe
Mostrar o que foi encontrado até o momento
This feature requires javascript
This feature requires javascript