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- Title
Interaction between DAHP synthase and chorismate mutase endows new regulation on DAHP synthase activity in Corynebacterium glutamicum.
- Authors
Li, Pan-Pan; Li, De-Feng; Liu, Di; Liu, Yi-Ming; Liu, Chang; Liu, Shuang-Jiang
- Abstract
Previous research on Corynebacterium glutamicum revealed that 3-deoxy- d-arabino-heptulosonate 7-phosphate synthase (DS, formerly DS2098) interacts with chorismate mutase (CM, formerly CM0819). In this study, we investigated the interaction by means of structure-guided mutation and enzymatic assays. Our results show that the interaction imparted a new mechanism for regulation of DAHP activity: In the absence of CM, DS activity was not regulated by prephenate, whereas in the presence of CM, prephenate markedly inhibited DS activity. Prephenate competed with the substrate phosphoenolpyruvate, and the inhibition constant ( K) was determined to be 0.945 mM. Modeling based on the structure of the complex formed between DAHP synthase and chorismate mutase of Mycobacterium tuberculosis predicted the interaction surfaces of the putative DS-CM complex. The amino acid residues and structural domains that contributed to the interaction surfaces were experimentally identified to be the SPAGARYE sequence of DS and the SGGTR loop and C-terminus (RGKLG) of CM.
- Subjects
CHORISMATE mutase; CORYNEBACTERIUM glutamicum; GENETIC mutation; AMINO acids; ENZYME inhibitors; MYCOBACTERIUM tuberculosis
- Publication
Applied Microbiology & Biotechnology, 2013, Vol 97, Issue 24, p10373
- ISSN
0175-7598
- Publication type
Article
- DOI
10.1007/s00253-013-4806-0