3.4.21.108: HtrA2 peptidase

This is an abbreviated version!
For detailed information about HtrA2 peptidase, go to the full flat file.

Reaction

cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues =

Synonyms

DegP, dOmi/HtrA2, high temperature requirement A serine protease, high temperature requirement A2, high temperature requirement A2 protease, high temperature requirement A2 serine protease, high temperature requirement protein A2, high-temperature requirement factor A2, HtrA protease, HtrA/DegP, HtrA2, HtrA2 protease, HtrA2 serine protease, HtrA2(Omi), HtrA2/Omi, HtrA2/Omi serine protease, Nma11p, Omi, Omi protease, Omi/HtrA2, Omi/HtrA2 protease, Omi/HtrA2 serine protease, pro-apoptotic serine protease, S01.278, serine protease, serine protease HtrA2, serine protease HtrA2/Omi, serine protease Omi/HtrA2

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.21 Serine endopeptidases

                3.4.21.108 HtrA2 peptidase

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Results	in table
43	Activating Compound
714	AA Sequence
37	Application
1	CAS Registry Number
48	Cloned(Commentary)
6	Crystallization (Commentary)
418	Disease/ Diagnostics
7	Expression
30	General Information
2	General Stability
1	IC50 Value
45	Inhibitors
34	kcat/KM [mM/s]
34	KM Value [mM]
118	Localization
43	Molecular Weight [Da]
32	Natural Substrates/ Products (Substrates)
136	Organism
16	PDB ID
5	pH Optimum
2	pI Value
8	Posttranslational Modification
115	Protein Variants
28	Purification (Commentary)
1	Reaction
51	Reaction Type
128	Reference
121	Source Tissue
1	Specific Activity [micromol/min/mg]
5	Storage Stability
153	Substrates and Products (Substrate)
6	Subunits
203	Synonyms
6	Temperature Optimum [°C]
3	Temperature Range [°C]
3	Temperature Stability [°C]
23	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.21.108 - HtrA2 peptidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

-

Homo sapiens

O43464

732718

comparison of wild-type and mutan S276C. In wild-type, water molecule number 377 forms an interaction between side chains of S276 and I270* of the adjacent molecule. In mutant S276C, this water molecule is absent

Homo sapiens

O43464

753038

structure of the HtrA3 protease domain together with the PDZ domain. The protein forms a trimer

Homo sapiens

P83110

755093

structures of variant V226K/S306A and V325D. Upon binding of specific peptide ligand NH2-GWTMFWV-COOH, the PDZ domains open more dynamically in the wild type protease compared to the V226K mutant, whereas the movement is not observed in the V325D mutant. The movement relies on a PDZ vs. protease domain rotation which opens the protease domain-PDZ interface

Homo sapiens

O43464

755128

to 1.65 A resolution. The catalytic triad in the HtrA2 wild-type structure is disrupted, with the nearest accessible H198 side chain atom positioned 5.9 A away from the carboxylate oxygen of D228 and separated from the hydroxyl of S306 by 7.4 A, requiring substantial rearrangements to reestablish a catalytically competent conformation. Dynamic protein motions are important to HtrA protease activity

Homo sapiens

O43464

753188

hanging drop vapor diffusion method

Mammalia

-

653326