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Mutation analysis of the feedback inhibition site of phenylalanine-sensitive 3-deoxy-D-arabino-heptulosonate 7-phosphate synthase of Escherichia coli

✍ Scribed by Changyun Hu; Peihong Jiang; Jianfeng Xu; Yongqing Wu; Weida Huang

Publisher
John Wiley and Sons
Year
2003
Tongue
English
Weight
86 KB
Volume
43
Category
Article
ISSN
0233-111X

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✦ Synopsis

Abstract

In Escherichia coli, the phenylalanine‐sensitive 3‐deoxy‐D‐arabino‐heptulosonate‐7‐phosphate synthase (DAHPS) AroG catalyzes the first committed step in the biosynthesis of aromatic compounds. To investigate the feedback inhibition site of AroG, mutated enzymes prepared with sequence‐overlap extension PCR were expressed and purified. The enzymatic activity assay showed that the amino acid replacements at Phe144, Leu175, Leu179, Phe209, Trp215Ala and Val221 completely or partially relieved feedback inhibition of AroG addressed by the phenylalanine. Ile10Ala and Δ(1–15) desensitized feedback inhibition and caused a 70 ∼ 90% loss of the specific catalytic activities. These results strongly suggest an involvement of the interior region and the N‐terminus of the polypeptide chain of AroG in the formation of the feedback inhibition site of DAHPS.

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