3.4.19.5: beta-aspartyl-peptidase

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

Reaction

Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide =

Synonyms

ASNase3, asparaginase, asparaginase-like protein 1, asparagine beta-amidohydrolase, ASRGL1, beta-aspartyl dipeptidase, beta-aspartyl peptidase, CpsIadA, dipeptidase, beta-aspartyl, EC 3.4.13.10, EcAIII, hASRGL1, IAD, isoaspartyl aminopeptidase, isoaspartyl aminopeptidase/asparaginase, isoaspartyl dipeptidase, isoaspartyl peptidase, isoaspartyl peptidase/L-asparaginase, LlA, Ntn-hydrolase, potassium-independent asparaginase

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.19 Omega peptidases

                3.4.19.5 beta-aspartyl-peptidase

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Results	in table
1	Activating Compound
2640	AA Sequence
1	Application
1	CAS Registry Number
8	Cloned(Commentary)
8	Crystallization (Commentary)
26	Disease/ Diagnostics
3	General Information
4	General Stability
3	Inhibitors
9	kcat/KM [mM/s]
31	KM Value [mM]
1	Localization
4	Metals/Ions
11	Molecular Weight [Da]
3	Natural Substrates/ Products (Substrates)
16	Organism
1	Pathway
66	PDB ID
5	pH Optimum
1	pH Range
1	Posttranslational Modification
21	Protein Variants
7	Purification (Commentary)
1	Reaction
1	Reaction Type
16	Reference
7	Source Tissue
1	Specific Activity [micromol/min/mg]
1	Storage Stability
55	Substrates and Products (Substrate)
5	Subunits
28	Synonyms
3	Temperature Optimum [°C]
1	Temperature Range [°C]
7	Temperature Stability [°C]
29	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.19.5 - beta-aspartyl-peptidase

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

uncleaved (inactive) as well as the cleaved (active), aspartate-bound structures. Cleavage does not greatly alter the overall structure of the enzyme with the exception of the conformational change in the conserved HGG loop that coincides with cleavage

Cavia porcellus

-

731313

structures of the isoaspartyl dipeptidase from Colwellia psychrerythraea, both ligand-free and that complexed with beta-isoaspartyl lysine, at 1.85 A and 2.33 A resolution, respectively. In both structures, the enzyme forms an octamer with two Zn2+ ions in the active site

Colwellia psychrerythraea

Q484B6

755151

-

Escherichia coli

P37595

698748

hanging drop method of vapor diffusion, the best crystals are observed growing at 25°C from 10% poly(ethylene glycol)8000, 100 mM homopipes, pH 5, in the presence of MgCl2

Escherichia coli

-

647275

hanging drop vapor diffusion method, 1.9 A resolution

Escherichia coli

P37595

669365

hanging drop vapor diffusion method. X-ray crystal structure of the D285N mutant complexed with beta-Asp-His

Escherichia coli

P39377

667676

hanging-drop vapour-diffusion method, crystal structure of EcAIII at 1.65 A resolution

Escherichia coli

-

667054

sitting drop vapor diffusion method, crystal structure in the absence and presence of the phosphinic inhibitor Asp-PSI[PO2CH2]-LeuOH

Escherichia coli

P39377

647274