3.4.11.10: bacterial leucyl aminopeptidase

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

Reaction

release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids =

Synonyms

AAP, Aeromonas proteolytica aminopeptidase, Aminopeptidase, aminopeptidase A, aminopeptidase A (bacteria), aminopeptidase Ap1, aminopeptidase II, AP-II, API, APII, AVP, bacterial leucine aminopeptidase, bacterial M17 aminopeptidase, BSAP, Bsu aminopeptidase, BsuAP, CGase, cysteinylglycinase, double-zinc aminopeptidase, extracellular aminopeptidase, FgLAP, HpM17AP, LAP, LAPII, leucine aminopeptidase, leucine aminopeptidase II, leucine APN, Leucyl aminopeptidase, M17 aminopeptidase, M17 metallo-aminopeptidase, More, MtLAP, PepA, Peptidase A, pepZ, PhpA, ribosomal-bound aminopeptidase, rLAP55, Rv2213, SSAP, TAP, TH-2, thermophilic aminopeptidase, thermostable leucine aminopeptidase, Vibrio aminopeptidase, VpAP, ywaD

ECTree

     3 Hydrolases

         3.4 Acting on peptide bonds (peptidases)

             3.4.11 Aminopeptidases

                3.4.11.10 bacterial leucyl aminopeptidase

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Results	in table
4	Activating Compound
28139	AA Sequence
8	Application
1	CAS Registry Number
32	Cloned(Commentary)
18	Crystallization (Commentary)
10	General Information
4	General Stability
17	IC50 Value
203	Inhibitors
8	kcat/KM [mM/s]
73	Ki Value [mM]
135	KM Value [mM]
25	Localization
103	Metals/Ions
51	Molecular Weight [Da]
38	Natural Substrates/ Products (Substrates)
98	Organism
1	Oxidation Stability
46	PDB ID
38	pH Optimum
7	pH Range
7	pH Stability
5	Posttranslational Modification
49	Protein Variants
43	Purification (Commentary)
17	Reaction
5	Reaction Type
95	Reference
2	Renatured (Commentary)
2	Source Tissue
84	Specific Activity [micromol/min/mg]
4	Storage Stability
255	Substrates and Products (Substrate)
38	Subunits
155	Synonyms
32	Temperature Optimum [°C]
2	Temperature Range [°C]
21	Temperature Stability [°C]
128	Turnover Number [1/s]

General Stability

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General Stability on EC 3.4.11.10 - bacterial leucyl aminopeptidase

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

generally extremely stable

Vibrio proteolyticus

-

81173

not denatured in aliphatic alcohols up to 20% concentration

Vibrio proteolyticus

-

81189

only partially inactivated in 8 M urea

Vibrio proteolyticus

-

81176

urea-caused unfolding transitions of rLAP as a function of urea concentration are monitored by circular dichroism (CD) and fluorescence (FL) spectroscopy exhibiting single transitions by both techniques. Free energy change for unfolding measured by CD and FL spectroscopy are 2.8 and 3.7 kcal/mol, respectively

Vibrio proteolyticus

Q01693

753862