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Title: The Catalytic Machinery of a Key Enzyme in Amino Acid Biosynthesis

Journal Article · · J. Amino Acids
DOI:https://doi.org/10.4061/2011/352538· OSTI ID:1032381

The aspartate pathway of amino acid biosynthesis is essential for all microbial life but is absent in mammals. Characterizing the enzyme-catalyzed reactions in this pathway can identify new protein targets for the development of antibiotics with unique modes of action. The enzyme aspartate {beta}-semialdehyde dehydrogenase (ASADH) catalyzes an early branch point reaction in the aspartate pathway. Kinetic, mutagenic, and structural studies of ASADH from various microbial species have been used to elucidate mechanistic details and to identify essential amino acids involved in substrate binding, catalysis, and enzyme regulation. Important structural and functional differences have been found between ASADHs isolated from these bacterial and fungal organisms, opening the possibility for developing species-specific antimicrobial agents that target this family of enzymes.

Research Organization:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Organization:
National Institutes of Health (NIH)
OSTI ID:
1032381
Journal Information:
J. Amino Acids, Vol. 2011, Issue (352538) ; 2011
Country of Publication:
United States
Language:
ENGLISH

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