3.4.24.36: leishmanolysin

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For detailed information about leishmanolysin, go to the full flat file.

Reaction

Preference for hydrophobic residues at P1 and P1' and basic residues at P2' and P3'. A model nonapeptide is cleaved at -Ala-Tyr-/-Leu-Lys-Lys- =

Synonyms

66 kDa surface metallopeptidase, Cell surface protease, glycoprotein 63, Glycoprotein gp63, gp63, GP63 metalloprotease, GP63 protein, GP63 surface metalloprotease, GP63 virulence protein, Leishmania metalloproteinase, Leishmania surface metalloprotease, leishmanolysin-like molecule, Major surface glycoprotein, major surface protease, major surface-metalloprotease, metalloprotease GP63, MSP, Promastigote surface endopeptidase, Promastigote surface protease, protective surface protease, Surface acid proteinase, surface leishmanolysin-like molecule, surface protease GP63, surface protein GP63, surface proteinase GP63, virulence factor major surface protease

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.36 leishmanolysin

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Results	in table
1	Activating Compound
559	AA Sequence
12	Application
1	CAS Registry Number
5	Cloned(Commentary)
4	Crystallization (Commentary)
17	General Information
1	General Stability
14	Inhibitors
9	kcat/KM [mM/s]
10	KM Value [mM]
55	Localization
13	Metals/Ions
10	Molecular Weight [Da]
32	Natural Substrates/ Products (Substrates)
104	Organism
1	PDB ID
12	pH Optimum
4	pH Range
1	pH Stability
5	pI Value
8	Posttranslational Modification
14	Protein Variants
7	Purification (Commentary)
1	Reaction
1	Reaction Type
54	Reference
49	Source Tissue
1	Storage Stability
90	Substrates and Products (Substrate)
9	Subunits
182	Synonyms
10	Temperature Optimum [°C]
9	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.24.36 - leishmanolysin

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

homology modeling based on the structure of Leishmania major gp63. The protein consists of the N-terminal, central and C-terminal domain

Leishmania donovani

P23223

696516

Leishmania major, crystallographic parameters

Leishmania major

-

31228

molecular dynamics simulation of enzyme in water. Upon solvation, enzyme undergoes a sharp structural relaxation with respect to the crystal structure. Fingerprint fluctuations of enzyme are characterized by the motion of a large part of the N-terminal domain, which is also involved in substrate recognition and proenzyme activation. Residues involved in interdomain binding are highly conserved

Leishmania major

-

670848

monoclinic crystals, space group C2 with a : 107.2 A, b : 90.6 A, c : 70.6 A, and tetragonal crystals, space group P4(1)2(1)2(1), a : b : 63.6 A, c : 251.4 A

Leishmania major

P08148

653919