Thermolysin from Bacillus thermoproteolyticus

Enzyme Description

Extremophile
Yes "thermophilic" organism
EC Number

Sequence

Length: 316 amino acids
ITGTSTVGVGRGVLGDQKNINTTYSTYYYLQDNTRGNGIFTYDAKYRTTLPGSLWADADNQFFASYDAPAVDAHYYAGVTYDYYKNVHNRLSYDGNNAAIRSSVHYSQGYNNAFWNGSQMVYGDGDGQTFIPLSGGIDVVAHELTHAVTDYTAGLIYQNESGAINEAISDIFGTLVEFYANKNPDWEIGEDVYTPGISGDSLRSMSDPAKYGDPDHYSKRYTGTQDNGGVHINSGIINKAAYLISQGGTHYGVSVVGIGRDKLGKIFYRALTQYLTPTSNFSQLRAAAVQSATDLYGSTSQEVASVKQAFDAVGVK
Kohei Oda et al. (1996) β€” A Novel Alcohol Resistant Metalloproteinase, Vimelysin, from Vibrio sp. T1800: Purification and Characterization
Bioscience, Biotechnology, and Biochemistry  Β· doi:10.1271/bbb.60.463 β†—  Β· Activity - Classical
22 measurements ▼
Database ID
UniProt: P00800 β†—
Sequence Annotation
Inferred - from protein name (first 232 residues from UniProt sequence absent from the mature protein)
Protein Source
Commercially purchased

Experimental Data (22 measurements)

22 measurements β€” page 2 of 2
Property Assay Solvent Solvent Volume Aqueous Reference Measured Value Units Extraction method Data type Solution pH Temperature Substrate(s) Product(s) Cofactor(s) Shaking Comments
Activity - Classical Activity measured by absorbance spectrophotometry (FAGLA absorbance measurement, 345 nm) in the presence of organic solvent Methanol 30 % (v/v) 100 6 % Digital Continuous 0.1 M MES 6.5 ? 1 mM FAGLA (FA-Gly-DL-Leu-NH2) Furylacryloyl-Gly , Leu-NH2 β€” β€” Classical aqueous control (in %)
Activity - Classical Activity measured by absorbance spectrophotometry (FAGLA absorbance measurement, 345 nm) in the presence of organic solvent Methanol 20 % (v/v) 100 12 % Digital Continuous 0.1 M MES 6.5 ? 1 mM FAGLA (FA-Gly-DL-Leu-NH2) Furylacryloyl-Gly , Leu-NH2 β€” β€” Classical aqueous control (in %)
1 2
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Visualization : Activity β€” Classical

One bar per measurement. Colour = solvent, shade = solvent volume. β€” β€” β€” Reference value. Hover for details.

Guillermo R. Castro et al. (1999) β€” Enzymatic activities of proteases dissolved in organic solvents
Enzyme and Microbial Technology  Β· doi:10.1016/S0141-0229(99)00099-X β†—  Β· Activity - Michaelis-Menten
3 measurements ▼
Mohammad Pazhang et al. (2006) β€” Effects of water-miscible solvents and polyhydroxy compounds on the structure and enzymatic activity of thermolysin
Journal of Biotechnology  Β· doi:10.1016/j.jbiotec.2006.05.017 β†—  Β· Activity - Classical Activity - Michaelis-Menten Stability - Half-life
68 measurements ▼
Hiroyasu Ogino et al. (2007) β€” Stabilities and Conformational Transitions of Various Proteases in the Presence of an Organic Solvent
Biotechnology Progress  Β· doi:10.1021/bp060252p β†—  Β· Stability - Half-life
1 measurement ▼
Bassem Jaouadi et al. (2013) β€” Biochemical and molecular characterization of Pseudomonas aeruginosa CTM50182 organic solvent-stable elastase
International Journal of Biological Macromolecules  Β· doi:10.1016/j.ijbiomac.2013.05.019 β†—  Β· Stability - Incubation
40 measurements ▼
Akli Ouelhadj et al. (2020) β€” Identification and homology modeling of a new biotechnologically compatible serine alkaline protease from moderately halotolerant Gracilibacillus boraciitolerans strain LO15
International Journal of Biological Macromolecules  Β· doi:10.1016/j.ijbiomac.2020.07.266 β†—  Β· Activity - Classical
10 measurements ▼

Structure

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