3.4.11.21: aspartyl aminopeptidase

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

Reaction

release of an N-terminal aspartate or glutamate from a peptide, with a preference for aspartate =

Synonyms

AAP, acid aminopeptidase, acid peptidase, alpha-aspartyl dipeptidase, Aminopeptidase, aminopeptidase A, angiotensinase, APA, Ape4, Ape4 aspartyl aminopeptidase, Ape4 metalloprotease, Asp-AP, AspAP, aspartate aminopeptidase, aspartic aminopeptidase, aspartyl aminopeptidase, aspartyl(glutamyl)-specific aminopeptidase, aspartyl-AP, CNAG_01169, DAP, DNPEP, EC 3.4.11.7, glutamyl (aspartyl)-specific aminopeptidase A, glutamyl aminopeptidase, L-aspartate aminopeptidase, Lb-PepA, Lc-PepA, M18 aspartyl aminopeptidase, M18AAP, More, PepA, peptidase E, PfM18AAP, PvM18AAP, soluble acid aminopeptidase, TgAAP, TGGT1_297970, Yhr113w

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.11 Aminopeptidases

                3.4.11.21 aspartyl aminopeptidase

Advanced search results

Do not include text mining results

Include results (more...)

Include results (more...)

Results	in table
2	Activating Compound
1576	AA Sequence
8	Application
1	CAS Registry Number
15	Cloned(Commentary)
1	Crystallization (Commentary)
88	Disease/ Diagnostics
8	Expression
28	General Information
1	General Stability
59	IC50 Value
164	Inhibitors
2	kcat/KM [mM/s]
10	Ki Value [mM]
21	KM Value [mM]
33	Localization
28	Metals/Ions
25	Molecular Weight [Da]
9	Natural Substrates/ Products (Substrates)
52	Organism
31	PDB ID
18	pH Optimum
6	pH Range
2	pH Stability
1	pI Value
1	Posttranslational Modification
16	Protein Variants
18	Purification (Commentary)
4	Reaction
3	Reaction Type
49	Reference
1	Renatured (Commentary)
59	Source Tissue
11	Specific Activity [micromol/min/mg]
113	Substrates and Products (Substrate)
25	Subunits
119	Synonyms
8	Temperature Optimum [°C]
3	Temperature Range [°C]
15	Temperature Stability [°C]
4	Turnover Number [1/s]

General Stability

print visible entries

print all entries

General Stability on EC 3.4.11.21 - aspartyl aminopeptidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.

top print hide Go to General Stability Search

Please wait a moment until the data is sorted. This message will disappear when the data is sorted.

GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

enzyme structure homology modelling, molecular dynamics simulation, secondary structure, acidic residues and hydrophobicity of interior residues demonstrate that aspartyl aminopeptidase has a greater stability than non-salttolerant protease in high salinity

Aspergillus oryzae

Q2UPZ7

753626