3.4.24.20: peptidyl-Lys metalloendopeptidase

This is an abbreviated version!
For detailed information about peptidyl-Lys metalloendopeptidase, go to the full flat file.

Reaction

Preferential cleavage in proteins: -Xaa-/-Lys- (in which Xaa may be Pro) =

Synonyms

Am-LysN, Armillaria mellea neutral proteinase, aspzincin metalloendopeptidase, aspzincin metalloprotease, EC 3.4.99.30, EC 3.4.99.32, GFMEP, Lys-N, LysN, MEP, peptidyl-Lys metalloendopeptidase, peptidyl-Lys metallopeptidase, Peptidyllysine metalloproteinase, POMEP, Proteinase, peptidyllysine metallo-

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.20 peptidyl-Lys metalloendopeptidase

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Results	in table
62	AA Sequence
4	Application
1	CAS Registry Number
1	Cloned(Commentary)
2	Crystallization (Commentary)
3	General Information
2	General Stability
60	Inhibitors
4	kcat/KM [mM/s]
1	Ki Value [mM]
15	KM Value [mM]
6	Localization
14	Metals/Ions
9	Molecular Weight [Da]
22	Organism
5	PDB ID
11	pH Optimum
4	pH Range
6	pH Stability
11	Protein Variants
7	Purification (Commentary)
1	Reaction
1	Reaction Type
18	Reference
5	Source Tissue
4	Specific Activity [micromol/min/mg]
2	Storage Stability
99	Substrates and Products (Substrate)
4	Subunits
20	Synonyms
6	Temperature Optimum [°C]
14	Temperature Stability [°C]
15	Turnover Number [1/s]

Engineering

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Engineering on EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

A101D

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, the mutant shows increased specificity towards arginine in subsites S2'-S4' compared to the wild-type protease

754029

D132N

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, mutation in the zinc binding motif, leading to a significant decrease in activity, showing 16% of wild-type protease activity

754029

D156A

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, 99% reduced activity compared to wild-type

754029

E120Q

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, mutation in the zinc binding motif, 97% reduced activity compared to wild-type

754029

G136L

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, 96% reduced activity compared to wild-type

754029

H123R

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, mutation in the zinc binding motif, leading to 99% decrease in activity compared to wild-type

754029

T105D

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, the mutant shows increased specificity towards arginine in subsites S2'-S4' compared to the wild-type protease

754029

T130A

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, 96% reduced activity compared to wild-type

754029

Y135F

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, 95% reduced activity compared to wild-type

754029

Y135W

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, 95% reduced activity compared to wild-type

754029

Y85L

Armillaria mellea

Q9Y7F7

site-directed mutagenesis, 97% reduced activity compared to wild-type

754029