3.4.11.21: aspartyl aminopeptidase

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

Word Map on EC 3.4.11.21

3.4.11.21

3.4.11.7

angiotensin

aminopeptidases

renin-angiotensin

angiotensinase

gluap

amastatin

alanyl

glutamyl-aminopeptidase

3.4.24.11

maltase-glucoamylase

cysap

aspartyl-aminopeptidase

pepes

arylamide

drug development

lactase-phlorizin

medicine

synthesis

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

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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]

Metals Ions

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Metals Ions on EC 3.4.11.21 - aspartyl aminopeptidase

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Ba2+

Sus scrofa

activation

36021

Ca2+

Sus scrofa

4fold activation for Glu 2-naphthylamide at 0.1 mM and above

Co2+

Fe2+

activates over 2fold at 1 mM

755445

Mg2+

Toxoplasma gondii

S7UJV5

activates slightly at 1 mM

Mn2+

NaCl

a salt-tolerant aspartyl aminopeptidase, the relative activity of the enzyme remains 85% in 3 M NaCl solution for 15 days, Km and Vmax are slightly affected in 3 M NaCl solution. 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. Higher contents of ordered secondary structures, more salt bridges between hydrated surface acidic residues and specific basic residues, and stronger hydrophobicity of interior residues are the salt-tolerance mechanisms of aspartyl aminopeptidase

753626

Ni2+

Toxoplasma gondii

S7UJV5

activates about 2fold at 1 mM

755445

Zn2+

4 entries

additional information

10 entries