Distinct mechanisms of substrate selectivity in the DRE-TIM metallolyase superfamily: A role for the LeuA dimer regulatory domain
Author:
Funder
National Science Foundation
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference22 articles.
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5. Mechanistic and bioinformatic investigation of a conserved active site helix in alpha-isopropylmalate synthase from Mycobacterium tuberculosis, a member of the DRE-TIM metallolyase superfamily;Casey;Biochemistry,2014
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