PMID:15378531
| Citation |
Xu, J, Hu, C, Shen, S, Wang, W, Jiang, P and Huang, W (2004) Requirement of the N-terminus for dimer formation of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate synthase AroG of Escherichia coli. J. Basic Microbiol. 44:400-6 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1002/jobm.200410396 |
| Keywords |
3-Deoxy-7-Phosphoheptulonate Synthase; Aldehyde-Lyases/genetics; Aldehyde-Lyases/isolation & purification; Aldehyde-Lyases/metabolism; Amino Acid Substitution; Binding Sites; Dimerization; Escherichia coli/enzymology; Feedback, Physiological; Models, Molecular; Phenylalanine/metabolism; Sequence Deletion/genetics; Sequence Deletion/physiology |
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