Structure of Aspartate-β-semialdehyde Dehydrogenase from Escherichia coli, a Key Enzyme in the Aspartate Family of Amino Acid Biosynthesis

1999 ◽  
Vol 289 (4) ◽  
pp. 991-1002 ◽  
Author(s):  
Andrea Hadfield ◽  
Gitay Kryger ◽  
Jun Ouyang ◽  
Gregory A. Petsko ◽  
Dagmar Ringe ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Semialdehyde Dehydrogenase ◽  
Key Enzyme ◽  
Aspartate Family

scholarly journals The Catalytic Machinery of a Key Enzyme in Amino Acid Biosynthesis

2011 ◽  
Vol 2011 ◽  
pp. 1-11 ◽  
Author(s):  
Ronald E. Viola ◽  
Christopher R. Faehnle ◽  
Julio Blanco ◽  
Roger A. Moore ◽  
Xuying Liu ◽  
...  
Keyword(s):  
Amino Acid ◽  
Antimicrobial Agents ◽  
Enzyme Regulation ◽  
Essential Amino Acids ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Semialdehyde Dehydrogenase ◽  
Key Enzyme ◽  
Aspartate Pathway ◽  
Enzyme Catalyzed Reactions

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 β-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.

Mechanistic insights into the allosteric regulation of Pseudomonas aeruginosa aspartate kinase

2018 ◽  
Vol 475 (6) ◽  
pp. 1107-1119 ◽  
Author(s):  
Chang-Cheng Li ◽  
Mei-Jia Yang ◽  
Li Liu ◽  
Tao Li ◽  
Cui-Ting Peng ◽  
...  
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Aspartate Kinase ◽  
Inhibitory Mechanism ◽  
Acid Biosynthesis ◽  
Distinctive Features ◽  
Open Conformation ◽  
Biochemical Analyses ◽  
Aspartate Family

In plants and microorganisms, aspartate kinase (AK) catalyzes an initial commitment step of the aspartate family amino acid biosynthesis. Owing to various structural organizations, AKs from different species show tremendous diversity and complex allosteric controls. We report the crystal structure of AK from Pseudomonas aeruginosa (PaAK), a typical α2β2 hetero-tetrameric enzyme, in complex with inhibitory effectors. Distinctive features of PaAK are revealed by structural and biochemical analyses. Essentially, the open conformation of Lys-/Thr-bound PaAK structure clarifies the inhibitory mechanism of α2β2-type AK. Moreover, the various inhibitory effectors of PaAK have been identified and a general amino acid effector motif of AK family is described.

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