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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.

Word Map on EC 3.4.11.10

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

Renatured

Renatured on EC 3.4.11.10 - bacterial leucyl aminopeptidase

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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
activity gain of rLAP refolded after reversible denaturation by urea, at 37°C, monitoring of the secondary structure changes
recombinant LAP is refolded by adding guanidine-solubilized protein to the following solution: 0.5 M L-Arg, 50 mM Tris, pH 8.0, 1 mM CaCl2, and 0.05 mM ZnCl2
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