Elastase from Pseudomonas aeruginosa ME-4

Enzyme Description

Extremophile
No
EC Number

Sequence

Length: 301 amino acids
AEAGGPGGNQKIGKYTYGSDYGPLIVNDRCEMDDGNVITVDMNGSTDDSKTTPFRFACPTNTYKQVNGAYSPLNDAHFFGGVVFKLYRDWFGTSPLTHKLYMKVHYGRSVENAYWDGTAMLFGDGATMFYPLVSLDVAAHEVSHGFTEQNSGLIYRGQSGGMNEAFSDMAGEAAEFYMRGKNDFLIGYDIKKGSGALRYMDQPSRDGRSIDNASQYYNGIDVHHSSGVYNRAFYLLANSPGWDTRKAFEVFVDANRYYWTATSNYNSGACGVIRSAQNRNYSAADVTRAFSTVGVTCPSAL
Shinji Takenaka et al. (2012) β€” Organic solvent-tolerant elastase efficiently hydrolyzes insoluble, cross-linked, protein fiber of eggshell membranes
Biotechnology Letters  Β· doi:10.1007/s10529-012-0861-3 β†—  Β· Activity - Classical
7 measurements
Database ID
UniProt: L8AX98 β†—
Sequence Annotation
Explicit - Provided (197 first residues from UniProt cleaved from the mature protein)
Protein Source
Recombinant, host bacterium Escherichia coli BL21 (DE3)

Experimental Data (7 measurements)

7 measurements
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Acetone Β±100% 100.0 54.0 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Dimethyl Sulfoxide (DMSO) Β±100% 100.0 35.0 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Isopropanol Β±100% 100.0 75.0 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Ethanol Β±100% 100.0 79.0 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Benzene Β±100% 100.0 1.7 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Cyclohexane Β±100% 100.0 0.0 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)
Activity - Classical Activity measured by HPLC (amount of soluble peptides in post-centrifugation supernatant measurement) Toluene Β±100% 100.0 0.0 % 10 mM phosphate buffer 6.5 50Β°C 150 mg (solid) Eggshell membrane (solid) Soluble peptides β€” 140 rpm Classical aqueous control (in %)

Visualization : Activity β€” Classical

One bar per measurement. Colour = solvent, shade = solvent volume.

Structure

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