5-Enolpyruvylshikimate-3-phosphate Synthase of Bacillus subtilis is an Allosteric Enzyme. Analysis of Arg24Asp, Pro105Ser and His385Lys mutations suggests a hidden phosphoenol pyruvate-binding site-Reference-Cited by-同舟云学术

5-Enolpyruvylshikimate-3-phosphate Synthase of Bacillus subtilis is an Allosteric Enzyme. Analysis of Arg24Asp, Pro105Ser and His385Lys mutations suggests a hidden phosphoenol pyruvate-binding site

Published:1995-04 Issue:1 Volume:229 Page:99-106
ISSN:0014-2956
Container-title:European Journal of Biochemistry
language:en
Short-container-title:Eur J Biochem

Author:

Majumder Kumud,Selvapandiyan Angamuthu,Fattah Farkad A.,Arora Naresh,Ahmad Suhail,Bhatnagar Raj K.

Publisher

Wiley

Subject

Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1995.tb20443.x/fullpdf

Reference32 articles.

1. The Enzymatic Formation and Isolation of 3-Enolpyruvylshikimate 5-Phosphate

2. Mode of action of N-phosphonomethylglycine. Inhibition of aromatic amino acid biosynthsis

3. Substrate synergism and the steady-state kinetic reaction mechanism for EPSP synthase from Escherichia coli

4. 5-Enolpyruvylshikimate-3-phosphate synthase of Klebsiella pneumoniae. 1. Purification and properties

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