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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

Activating Compound

Activating Compound on EC 3.4.11.10 - bacterial leucyl aminopeptidase

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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
activates, 30% activation at 17 mM
bicarbonate
-
activates
dithiothreitol
-
activates, 23% activation at 0.021 mM, inhibition above
additional information
-
full-length LAP is activated in a two-step process: proteolytic cleavage at the C terminus is followed by an intramolecular autocatalytic removal of a 12-amino acid propeptide at the N terminus
-