3.4.11.6: aminopeptidase B

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

Reaction

release of N-terminal Arg and Lys from oligopeptides when P1' is not Pro. Also acts on arylamides of Arg and Lys =

Synonyms

AAP, ACE2, Aminopeptidase, aminopeptidase B, aminopeptidase, arginine, aminopeptidase-B, Ap-B, APB, Arg-AP, Arg/Lys aminopeptidase, ArgAP, arginine aminopeptidase, arginine-aminopeptidase, arginyl aminopeptidase, arginyl peptidase, arylamidase, arylamidase II, BSAP, chloride-dependent-basic aminopeptidase, Cl--activated arginine aminopeptidase, Cl--activated arinine aminopeptidase, Co(II)-Ap-B, ColAP, cold-active aminopeptidase, Cu(II)-Ap-B, cytosol aminopeptidase, cytosol aminopeptidase IV, DAP BII, dipeptidyl aminopeptidase BII, double-zinc aminopeptidase, EC 3.4.13.6, KAP, L-arginine aminopeptidase, L-RAP, LAPase, leukocyte-derived arginine aminopeptidase, LRAP, lysine-specific aminopeptidase, minopeptidase, More, protease IV, pumAPE, RAP

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.11 Aminopeptidases

                3.4.11.6 aminopeptidase B

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Results	in table
26	Activating Compound
865	AA Sequence
1	Application
1	CAS Registry Number
19	Cloned(Commentary)
2	Crystallization (Commentary)
426	Disease/ Diagnostics
5	General Information
1	General Stability
48	IC50 Value
386	Inhibitors
18	kcat/KM [mM/s]
14	Ki Value [mM]
91	KM Value [mM]
53	Localization
80	Metals/Ions
46	Molecular Weight [Da]
15	Natural Substrates/ Products (Substrates)
3	Organic Solvent Stability
110	Organism
1	Oxidation Stability
5	PDB ID
33	pH Optimum
10	pH Range
5	pH Stability
9	pI Value
5	Posttranslational Modification
35	Protein Variants
40	Purification (Commentary)
6	Reaction
2	Reaction Type
109	Reference
190	Source Tissue
43	Specific Activity [micromol/min/mg]
8	Storage Stability
255	Substrates and Products (Substrate)
20	Subunits
100	Synonyms
20	Temperature Optimum [°C]
5	Temperature Range [°C]
26	Temperature Stability [°C]
57	Turnover Number [1/s]

Crystallization

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Crystallization on EC 3.4.11.6 - aminopeptidase B

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

enzyme in complex with inhibitors SAHA or M344, X-ray diffraction structure determination and analysis

Homo sapiens

P09960

754386

crystallized using the hanging-drop vapour diffusion method. X-ray diffraction data to 2.3 A resolution are collected using an orthorhombic crystal form belonging to space group P2(1)2(1)2(1), with unit-cell parameters a = 76.55, b = 130.86, c = 170.87 A

Pseudoxanthomonas mexicana

V5YM14

731085