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Literature summary for 3.1.1.3 extracted from

  • Cherukuvada, S.L.; Seshasayee, A.S.; Raghunathan, K.; Anishetty, S.; Pennathur, G.
    Evidence of a double-lid movement in Pseudomonas aeruginosa lipase: insights from molecular dynamics simulations (2005), PLoS Comput. Biol., 1, e28.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.1.3

Protein Variants

Protein Variants Comment Organism
A217S the mutant movement of the lids is very similar to that in the wild-type lipase Pseudomonas aeruginosa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
29000
-
 x * 29000, crystal structure Pseudomonas aeruginosa

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa P26876
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information double-lid structure movements are involved in the enzyme function, Phe214 and Ala217 play important roles in lid movement, lid closure is driven by hydrophobic interactions, overview Pseudomonas aeruginosa ?
-
 ?

Subunits

Subunits Comment Organism
? x * 29000, crystal structure Pseudomonas aeruginosa
More the enzyme has a lid that stretched between residues 125 and 148, molecular dynamics simulations, using crystal structure with PDB ID 1EX9, for determination and anaylsis of the movement of the double-lid formed by this lid and a second lid, covering residues 210-222, hydrophobicity in lid movement, Phe214 and Ala217 play important roles in lid movement, lid closure is driven by hydrophobic interactions, Lid2 movement triggers movement of Lid1, overview Pseudomonas aeruginosa

Synonyms

Synonyms Comment Organism
lipase
-
 Pseudomonas aeruginosa