3.4.21.50: lysyl endopeptidase

This is an abbreviated version!
For detailed information about lysyl endopeptidase, go to the full flat file.

Reaction

Preferential cleavage: Lys-/-, including -Lys-/-Pro- =

Synonyms

Achrombacter protease I, Achromobacter lysyl endopeptidase, Achromobacter protease I, Achromobacter proteinase I, achromopeptidase, API, caseinase, endo-Lys-C protease, endopeptidase Lys-C, endoproteinase, endoproteinase Lys-C, endoproteinase lysine-C, KGP, LEP, Lys-C, Lys-C endoproteinase, Lys-specific serine endopeptidase, lysine endoproteinase, lysine specific gingipain, lysine specific protease, lysine specific proteinase, lysine-specific protease, Lysobacter lysyl endoproteinase, lysyl bond specific proteinase, Lysyl endopeptidase, protease I, protease IV, proteinase, Achromobacter lyticus alkaline I, proteinase, lysine specific, proteinase, Pseudomonas lyticus alkaline , I, Ps-1, Pseudomonas aeruginosa lysine -specific protease

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.50 lysyl endopeptidase

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Results	in table
4	Activating Compound
272	AA Sequence
13	Application
1	CAS Registry Number
7	Cloned(Commentary)
4	Crystallization (Commentary)
1796	Disease/ Diagnostics
9	General Information
2	General Stability
77	Inhibitors
74	KM Value [mM]
12	Localization
5	Metals/Ions
13	Molecular Weight [Da]
4	Natural Substrates/ Products (Substrates)
5	Organic Solvent Stability
102	Organism
7	PDB ID
26	pH Optimum
4	pH Range
7	pH Stability
1	pI Value
6	Posttranslational Modification
27	Protein Variants
8	Purification (Commentary)
1	Reaction
3	Reaction Type
51	Reference
1	Renatured (Commentary)
9	Source Tissue
7	Specific Activity [micromol/min/mg]
2	Storage Stability
163	Substrates and Products (Substrate)
14	Subunits
56	Synonyms
10	Temperature Optimum [°C]
1	Temperature Range [°C]
7	Temperature Stability [°C]
56	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.21.50 - lysyl endopeptidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Achromobacter lyticus

-

36610

mutants H210S and W169F, to 2.0 and 2.3 A resolution, respectively

Achromobacter lyticus

P15636

717034

neutron structure analysis of catalytic triad with Trp169 and His210. His57 is double protonated and forms hydrogen bonds to Ser194Ogamma and Asp113Odelta1, Odelta2. Resolution of data 2.0 A

Achromobacter lyticus

-

718032

purified recombinant enzyme, sitting drop vapor diffusion method, mixing of equal volumes of 0.001 ml of protein with reservoir solution containing 27% PEG 4000, 100 mM sodium acetate, pH 5.0, and 0.2 M ammonium sulfate, equilibration over 0.5 ml of reservoir solution, one week, X-ray diffraction structure determination and analysis at 1.6 A resolution, molecular replacement/heavy atom derivatization

Porphyromonas gingivalis

-

732885