3.4.24.B16: protease lasA

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

Reaction

proteolytic degradation of proteins =

Synonyms

bacteriolytic enzyme, LasA, LasA endopeptidase, LasA protease, M23.002, Pseudomonas elastase, staphylolysin, staphylolytic enzyme

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.24 Metalloendopeptidases

                3.4.24.B16 protease lasA

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Results	in table
1	Activating Compound
1	AA Sequence
9	Application
1	CAS Registry Number
1	Cloned(Commentary)
1	Crystallization (Commentary)
3	Expression
3	General Information
19	Inhibitors
3	KM Value [mM]
10	Localization
3	Metals/Ions
14	Molecular Weight [Da]
16	Natural Substrates/ Products (Substrates)
26	Organism
2	pH Optimum
1	pI Value
6	Posttranslational Modification
8	Protein Variants
9	Purification (Commentary)
6	Reaction
8	Reaction Type
23	Reference
1	Specific Activity [micromol/min/mg]
1	Storage Stability
33	Substrates and Products (Substrate)
7	Subunits
44	Synonyms
1	Temperature Optimum [°C]
3	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.24.B16 - protease lasA

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

crystal structures of active LasA as a complex with tartrate and in the uncomplexed form, to 1.28 A resolution. The overall fold resembles that of the other M23 family members, the LasA active site is less constricted and utilizes a different set of metal ligands. The active site of uncomplexed LasA contains a five-coordinate zinc ion with trigonal bipyramidal geometry and two metal-bound water molecules. Manual docking study of the pentapeptide Gly-Gly-Phe-Gly-Gly in the active site so that the carbonyl oxygen of the scissile peptide occupies the approximate position of Tyr151-bound tartrate oxygen O1 and the P2 and P1 glycines follow the path of the tartrate carbon skeleton

Pseudomonas aeruginosa

P14789

712754