Regulation of Aspartate Family Amino Acid Biosynthesis in Brevibacterium flavum

1970 ◽  
Vol 34 (9) ◽  
pp. 1275-1282 ◽  
Author(s):  
Ryuichi MIYAJIMA ◽  
Isamu SHIIO
Keyword(s):  
Amino Acid ◽  
Amino Acid Biosynthesis ◽  
Acid Biosynthesis ◽  
Brevibacterium Flavum ◽  
Aspartate Family

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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