Peptidyl-lys metalloendopeptidase (gene Tc-LysN) from Tramates coccinea

Enzyme Description

Species

Extremophile

EC Number

3.4.24.20 ↗

Sequence

Length: 405 amino acids

MRFPSIFTAVLFAASSALAAPVNTTTEDETAQIPAEAVIGYSDLEGDFDVAVLPFSASIAAKEEGVSLEKREAEAERALSLKVSGPEAVDGVQNFKVTTTLTNTGDESLKLLNDPRGALNTLPANTFDITTDSGEKPSFIGVKVKYVPRHAAQSTNEKSFTVLAPGESTSVTHDLSAAYNFTLPGAAKYTVEPANLFHYVDPETNEPVEIRADSEPHVAAVSGKLAVVRPTPTLTKRETYNGCSSSQKTGIQAAAPAAQTYVANALSYLQTHTASTARYTTWFGSYTSSRHSTVLSHYTNMNGNDYSSFTYDCTCTESDTYAYVYPDDFGYIYLCGAFWQAPTTGTDSKGGTLVHESSHFTRNAGTQDYVYGQSAAKSLAKSNPSEAIMNADNHEYFAENNPAQS

Uzair Ahmed et al. (2024) — A novel, robust peptidyl-lys metalloendopeptidase from Trametes coccinea recombinantly expressed in Komagataella phaffii

Applied Microbiology and Biotechnology · doi:10.1007/s00253-023-12986-3 ↗ · Activity - Classical

4 measurements ▼

Database ID

UniParc: UPI00292300CE ↗

Sequence Annotation

Explicit - Provided GenBank Accession Number (synthetic gene construct)

Protein Source

Recombinant, host yeast Komagataella phaffii

Experimental Data (4 measurements)

4 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 absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Acetonitrile	20%	100	214	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides , Peptides	—	—	Classical aqueous control (in %)
Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Acetonitrile	40%	100	202	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides , Peptides	—	—	Classical aqueous control (in %)
Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Methanol	20%	100	164	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides , Peptides	—	—	Classical aqueous control (in %)
Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Methanol	40%	100	151	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides , Peptides	—	—	Classical aqueous control (in %)

Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Acetonitrile	20%	100	214	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides, Peptides	—	—	Classical aqueous control (in %)
Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Acetonitrile	40%	100	202	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides, Peptides	—	—	Classical aqueous control (in %)
Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Methanol	20%	100	164	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides, Peptides	—	—	Classical aqueous control (in %)
Activity - Classical	Activity measured by absorbance spectrophotometry (colorimetric assay, Azo-peptides absorbance measurement, 450 nm) in the presence of organic solvent	Methanol	40%	100	151	%	50 mM sodium acetate buffer	5	60°C	? mM Azocasein	Azo-peptides, Peptides	—	—	Classical aqueous control (in %)

Visualization : Activity — Classical

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

Structure

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