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.

Word Map on EC 3.4.19.5

3.4.19.5

asrgl1s

asparaginases

plant-type

autoproteolytic

circularly

acylases

autoprocessing

glycosylasparaginases

dihydroorotases

medicine

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]

Subunits

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Subunits on EC 3.4.19.5 - beta-aspartyl-peptidase

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heterodimer

Lupinus luteus

Q9ZSD6

alphabeta, 1 * 23000, alpha-subunit + 1 * 14000, beta-subunit, SDS-PAGE, 1 * 22893, His-tagged alpha-subunit + 1 * 13605, beta-subunit, mass spectrometry

octamer

tetramer

the enzyme is dimer of heterodimers (alphabeta)2

669365

additional information

Escherichia coli

P39377

the quarternary structure of the enzyme is octameric and can be described as a tetramer od dimers. Each subunit folds into two distinct domains

647274