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3.4.11.1: leucyl aminopeptidase

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

Word Map on EC 3.4.11.1

Reaction

release of an N-terminal amino acid, Xaa-/-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolysed, but rates on arylamides are exceedingly low =

Synonyms

A-LAP, acidic M17 leucine aminopeptidase, AcLAP, adipocyte-derived leucine aminopeptidase, Aminopeptidase, aminopeptidase A, Aminopeptidase A/I, aminopeptidase I, aminopeptidase II, Aminopeptidase III, aminopeptidase LAP2, aminopeptidase N, AP 28, AP 56, APDkam589, APN, b/LAP, bovine lens/leucine aminopeptidase, BSAP, cathepsin III, CsLAP1, CsLAP2, cysteinyl-glycine hydrolysing activity, cysteinylglycine-hydrolysing activity, cytosol aminopeptidase, DR57, EC 3.4.1.1, Eg-LAP, endoplasmic reticulum aminopeptidase, ER-aminopeptidase-1, ERAP, ERAP1, ERAP2, FgLAP, FrvX, FTBL protein, FTBL proteins, HSA, L-leucine aminopeptidase, la, LAP, LAP yspII, LAP-A, LAP-N, LAP1, LAP2, lap3, LapA, LAPc, LeuAP, leucinamide aminopeptidase, leucinaminopeptidase, leucine amino peptidase, leucine aminopeptidase, leucine aminopeptidase 1, leucine aminopeptidase 2, leucine aminopeptidase 3, leucine aminopeptidase A, leucine aminopeptidase LAP-N, leucine aminopeptidase N, leucine aminopeptidase,, leucine aminopeptidase-A, Leucyl aminopeptidase, leucyl aminopeptidase (animal), leucyl aminopeptidase (plant), leucyl aminopeptidase yspII, leucyl peptidase, leucylaminopeptidase, leucylpeptidase, LmLAP-A, M17 family leucyl aminopeptidase metalloprotease, M17 LAP, M17 leucine amino peptidase, M17 leucine aminopeptidase, M17 leucyl aminopeptidase, M42 aminopeptidase, major leucyl aminopeptidase, More, PA2939, PaAP, PepA, PepA peptidase A, PepB, peptidase B, peptidase II, peptidase S, pepZ, PfLAP, PH1527, PhTET2, PILS-AP, PILSAP, Placental leucine aminopeptidase, PLAP, proline aminopeptidase, Prolyl aminopeptidase, proteins, specific or class, FTBL, PtLAP, puromycin insensitive leucyl-specific aminopeptidase, puromycin-insensitive leucine specific aminopeptidase, puromycin-insensitive leucyl-specific aminopeptidase, PVX_118180, rLAP, rMHJ_0461, S-Lap1, S-Lap2, S-Lap3, S-Lap4, S-Lap5, S-Lap6, S-Lap7, S-Lap8, SmLAP1, SmLAP2, Smp_03000, Smp_083870, sperm-leucylaminopeptidase, TbLAP-A, TbLAP1, TcLAP-A, TM0042, TpLAP, XoLAP

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.11 Aminopeptidases
                3.4.11.1 leucyl aminopeptidase

Storage Stability

Storage Stability on EC 3.4.11.1 - leucyl aminopeptidase

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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, apoenzyme or active enzyme, several years
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-70°C, 100 mM Tris-HCl buffer, pH 8.0, 6 weeks
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-80°C, 10% sucrose, 6 months, more than 90% of the enzyme activity remain
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-80°C, pure enzyme, 0.2 mM MnCl2, 2 weeks, stable
-80°C, purified enzyme after chloroform/octanol extraction purification step, in presence of 0.2 mM Mn2+, stable for at least 2 weeks
-80°C, purified enzyme, in 10 mM sodium phosphate, pH 7.8, 0.02 M magnesium acetate, 2 mM DTT, and 0.05 mM manganese chloride, stable for at least 2 months
0°C, or -20°C, pH 8.0, 1 year, 70% activity
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4°C, 0.1 M Tris-HCl buffer, 1 year
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4°C, partially purified enzyme after ion exchange chromatography purification step, stable for at least 6 months
4°C, partially purified enzyme, 6 months, stable, less stable after further purification
frozen, 6 months
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frozen, pH 7-9, presence of MgCl2, indefinitely
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Storage of crude enzyme solutions at -80, -20, 4 and 25°C for eight weeks reduces activity after the first three weeks of storage at all temperatures. At three weeks, residual activities are inversely proportional to their associated storage temperatures, with activity being reduced to 84, 77, 75 and 64% at temperatures of -80, -20, 4 and 25°C, respectively. Activity remained relatively stable from 4-8 weeks at temperatures of -80, -20 and 25°C. In contrast, samples stored at 4°C exhibit an additional about 10% decrease in activity during this time.
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