Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Chen, C.K.; Lee, G.C.; Ko, T.P.; Guo, R.T.; Huang, L.M.; Liu, H.J.; Ho, Y.F.; Shaw, J.F.; Wang, A.H.
    Structure of the alkalohyperthermophilic Archaeoglobus fulgidus lipase contains a unique C-terminal domain essential for long-chain substrate binding (2009), J. Mol. Biol., 390, 672-685.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.1.1.3 hanging drop method, crystallographic analysis of wild-type and S136A mutant enzyme, 1.8 A resolution data Archaeoglobus fulgidus

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.3 additional information deletion of the C-terminal domain reduces the optimal temperature from 90 to 80°C. The lack of the C-terminal domain also causes the protein to be less thermostable. However, the deletion also changes the optimal pH and pH stability of the recombinant enzyme. It reduces the optimal pH from 10.0 to 9.0 and causes the protein to be less pH stable. Without the C-terminal domain, the enzyme loses its function to hydrolyze long-chain ester substrates Archaeoglobus fulgidus

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.3 Archaeoglobus fulgidus O28511
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.3 4-nitrophenyl octanoate + H2O
-
 Archaeoglobus fulgidus 4-nitrophenol + octanoate
-
 ?
3.1.1.3 4-nitrophenyl palmitate + H2O
-
 Archaeoglobus fulgidus 4-nitrophenol + palmitate
-
 ?
3.1.1.3 tricaprylin + 3 H2O the apparent rate of hydrolysis correlates with the degree of micellar formation. Consistent with observations from other lipases, the lid conformation may change from the closed to the open form in the presence of lipid interface. Together with the evidence of the lid structure in in this enzyme, it is classified as a lipase rather than as a carboxylesterase Archaeoglobus fulgidus 3 octanoate + glycerol
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.1.1.3 60
-
 assay at Archaeoglobus fulgidus
3.1.1.3 90
-
-
 Archaeoglobus fulgidus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.1.1.3 30 90 30°C: about 50% of maximal activity, 90°C: optimum, recombinant enzyme Archaeoglobus fulgidus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.3 80
-
 30 min, about 5% loss of activity Archaeoglobus fulgidus
3.1.1.3 90
-
 30 min, about 95% loss of activity Archaeoglobus fulgidus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.3 8.5
-
 assay at Archaeoglobus fulgidus
3.1.1.3 10
-
 at 60°C Archaeoglobus fulgidus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.1.1.3 5 11 pH 5.0: about 55% of maximal activity, pH 11.0: about 85% of maximal activity Archaeoglobus fulgidus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.1.1.3 5
-
 60°C, activity after incubation for 2 h at pH 5.0 is about 20% lower compared to activity at pH 10.0 Archaeoglobus fulgidus
3.1.1.3 10
-
 60°C, 2 h, pH of highest stability Archaeoglobus fulgidus
3.1.1.3 11
-
 60°C, activity after incubation for 2 h at pH 5.0 is about 30% lower compared to activity at pH 10.0 Archaeoglobus fulgidus