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3.4.11.6: aminopeptidase B

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

Word Map on EC 3.4.11.6

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

Engineering

Engineering on EC 3.4.11.6 - aminopeptidase B

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F297A
the mutant shows no activity with kallidin or [Arg0]-Met-enkephalin
F297Y
the mutation causes a significant decrease in hydrolytic activity toward synthetic and peptide substrates (13fold and 15fold lower catalytic efficiencies with L-Arg-7-amido-4-methylcoumarin and L-Lys-7-amido-4-methylcoumarin, respectively. No activity with kallidin or [Arg0]-Met-enkephalin) as well as chloride anion sensitivity
Q169E
-
mutant shows no activity
Q169N
-
mutant shows a significant decrease in hydrolytic activity toward the fluorescent substrate Lys-4-methylcoumaryl-7-amide (MCA). Mutant shows an increase in IC50 values of inhibitors that interact with the catalytic pocket of aminopeptidase B. Km (Arg 4-methylcoumarin 7-amide) similar to wild-type, kcat (Arg 4-methylcoumarin 7-amide) decreased compared to wild-type. Km (Lys 4-methylcoumarin 7-amide) increased compared to wild-type, kcat (Lys 4-methylcoumarin 7-amide) decreased compared to wild-type
D315N
-
decreased activity compared to the wild type enzyme
D405N
-
decreased activity compared to the wild type enzyme
D406N
-
decreased activity compared to the wild type enzyme
E256Q
-
decreased activity compared to the wild type enzyme
E260Q
-
decreased activity compared to the wild type enzyme
E267Q
-
decreased activity compared to the wild type enzyme
E268Q
-
decreased activity compared to the wild type enzyme
E300Q
-
no activity
E326A
-
inactive
E326D
-
inactive
E326H
-
inactive
E326Q
-
inactive
E348A
-
inactive
E348D
-
inactive
E348E
-
inactive
E348H
-
inactive
E348Q
-
inactive
E387Q
-
increased activity compared to the wild type enzyme
E388Q
-
decreased activity compared to the wild type enzyme
E410Q
-
decreased activity compared to the wild type enzyme
E414Q
-
decreased activity compared to the wild type enzyme
H325A
-
inactive
H325F
-
inactive
H325Y
-
inactive
H329A
-
inactive
H329F
-
inactive
H329Y
-
inactive
Y229H
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
Y409F
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
Y441F
-
Km and kcat (L-Arg-2-naphthylamide) decreased compared to wild-type
additional information
-
immobilization of enzyme with 1% CaCl2 and 2.5% alginate, increase of in stability for immobilized enzyme