31phospho-NMR demonstration of phosphocysteine as a catalytic intermediate on the Escherichia coli phosphotransferase system EIIMtl.
J Biol Chem
; 266(11): 6690-2, 1991 Apr 15.
Article
em En
| MEDLINE
| ID: mdl-2016284
ABSTRACT
The mannitol-specific phosphotransferase system transport protein, Enzyme IIMtl, contains two catalytically important phosphorylated amino acid residues, both present on the cytoplasmic part of the enzyme. Recently, this portion has been subcloned, purified, and shown to be an enzymatically active domain. The N-terminal half has also been subcloned and shown to be the mannitol-binding domain. When combined the two domains catalyze mannitol phosphorylation at the expense of phospho-HPr (van Weeghel, R. P., Meyer, G. H., Pas, H. H., Keck, W. H., and Robillard, G. T., Biochemistry in press). The phospho-NMR spectrum of the purified phosphorylated cytoplasmic domain, taken at pH 8.0, shows two signals, one at -6.9 ppm compared with inorganic phosphate resulting from phosphohistidine and one at +11.9 ppm originating from phosphocysteine. Addition of mannitol plus membranes containing the N-terminal mannitol-binding domain results in the formation of mannitol 1-phosphate and the disappearance of the two signals at -6.9 and +11.9 ppm.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Contexto em Saúde:
3_ND
Problema de saúde:
3_neglected_diseases
/
3_zoonosis
Assunto principal:
Sistema Fosfotransferase de Açúcar do Fosfoenolpiruvato
/
Cisteína
/
Escherichia coli
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
1991
Tipo de documento:
Article
País de afiliação:
Holanda