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.

Word Map on EC 3.4.24.20

3.4.24.20

frondosa

collision

grifola

collision-induced

pleurotus

ostreatus

b-ions

molecular biology

silac

lysine-specific

synthesis

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]

General Information

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General Information on EC 3.4.24.20 - peptidyl-Lys metalloendopeptidase

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malfunction

Armillaria mellea

Q9Y7F7

mutants with extended S1' binding pocket show specificity towards arginine in subsites S2'-S4' compared to the wild-type protease resulting from the additional negative charge which attract and interact with positively charged residues better than the wild-type. The strict lysine specificity at P1' is preserved in the recombinant rAm-LysN. Relative specificity of site-directed mutants in the substrate binding sites of rAm-LysN compared to the wild-type enzyme with the reference peptide SAQKMVS, overview

754029

physiological function

Armillaria mellea

Q9Y7F7

peptidyl-Lys metallopeptidase (LysN) from Armillaria mellea is an aspzincin metalloprotease, which cleaves in front of lysines

754029

additional information

2 entries