Mechanism of feedback inhibition by leucine. Binding of leucine to wild-type and feedback resistant α-isopropylmalate syntheses and its structural consequences-Reference-Cited by-同舟云学术

Mechanism of feedback inhibition by leucine. Binding of leucine to wild-type and feedback resistant α-isopropylmalate syntheses and its structural consequences

Published:1973-07 Issue:16 Volume:12 Page:2980-2986
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Teng-Leary Elizabeth,Kohlhaw Gunter B.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00740a006

Reference17 articles.

1. α-Isopropylmalate synthase from Salmonella typhimurium—Amino acid composition, NH2-terminal analysis, and fingerprint analysis

2. Lack of End-Product Inhibition and Repression of Leucine Synthesis in a Strain of Salmonella typhimurium

3. A MULTISITE-MUTATION MAP OF THE LEUCINE OPERON OF SALMONELLA TYPHIMURIUM

4. Binding of Diffusible Molecules by Macromolecules: Rapid Measurement by Rate of Dialysis

5. Enzymatic Synthesis of Deoxyribonucleic Acid

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2. Structural and functional characterization of α-isopropylmalate synthase and citramalate synthase, members of the LeuA dimer superfamily;Archives of Biochemistry and Biophysics;2012-03

3. The C-terminal regulatory domain is required for catalysis by Neisseria meningitidis α-isopropylmalate synthase;Biochemical and Biophysical Research Communications;2010-02

4. Kinetic and Chemical Mechanism of α-Isopropylmalate Synthase from Mycobacterium tuberculosis;Biochemistry;2006-06-30

5. Slow-onset Feedback Inhibition: Inhibition of Mycobacterium tuberculosis α-Isopropylmalate Synthase by l-Leucine;Journal of the American Chemical Society;2005-06-25