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Literature summary for 3.5.99.5 extracted from

  • Chen, Y.; Chen, Y.; Jiang, H.; Lu, D.; Hu, T.; Bi, G.; Ran, Y.; Yu, B.; Dong, H.; Su, D.
    A unique homo-hexameric structure of 2-aminomuconate deaminase in the bacterium Pseudomonas species AP-3 (2019), Front. Microbiol., 10, 2079.
    View publication on PubMed
Search for more literature for 3.5.99.5

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Pseudomonas sp. AP3

Crystallization (Commentary)

Crystallization (Comment) Organism
sitting-drop vapor diffusion method at 20°C, crystal structure is determined at 1.75 A Pseudomonas sp. AP3

Protein Variants

Protein Variants Comment Organism
R56A the mutant loses the ability to maintain the hexameric conformation, and reveales that the hydrogen bonds between residues Arg56 and Met96 have pivotal roles in the AmnE hexameric assembly Pseudomonas sp. AP3

Organism

Organism UniProt Comment Textmining
Pseudomonas sp. AP3 Q9KWS2
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Pseudomonas sp. AP3

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-aminomuconate + H2O
-
 Pseudomonas sp. AP3 (3E)-2-oxohex-3-enedioate + NH3
-
 ?

Subunits

Subunits Comment Organism
homohexamer the AmnE hexamer is in a stable state in solution, and that the residues Arg56 and Met96 located on the hexameric interface are two key residues required to maintain the hexameric conformation of AmnE Pseudomonas sp. AP3

Synonyms

Synonyms Comment Organism
AmnE
-
 Pseudomonas sp. AP3