Requirement of the N-terminus for dimer formation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate synthase AroG of Escherichia coli.
J Basic Microbiol
; 44(5): 400-6, 2004.
Article
en En
| MEDLINE
| ID: mdl-15378531
ABSTRACT
The first regulatory step in the synthesis of aromatic amino acids is catalyzed by 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase (DAHPS). In Escherichia coli, the allosteric DAHPS exists as three isozymes, AroG, AroF and AroH, each independently feedback-inhibited by corresponding end product amino acids, phenylalanine, tyrosine and typtophan. Structural biological evidences have suggested that the N-terminus of AroG is involved in the formation of a putative inhibitor-binding site and feedback inhibition signal transmission. Our previous work showed that a single amino acid residue replacement Ile10Ala or deletion of 15 N-terminal amino acids could lead to a dramatic loss of AroG enzymatic activity (Hu et al. 2003). Here we demonstrate that the deletion of N-terminus prevents the enzyme from forming a dimeric structure, indicating that the N-terminus of AroG plays a critical role in the formation of the essential tight dimeric structure.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Aldehído-Liasas
/
Escherichia coli
Tipo de estudio:
Diagnostic_studies
Idioma:
En
Revista:
J Basic Microbiol
Asunto de la revista:
MICROBIOLOGIA
Año:
2004
Tipo del documento:
Article
País de afiliación:
China