Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.11.6 extracted from

  • Pham, V.L.; Cadel, M.S.; Gouzy-Darmon, C.; Hanquez, C.; Beinfeld, M.C.; Nicolas, P.; Etchebest, C.; Foulon, T.
    Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling (2007), BMC Biochem., 8, 21.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.11.6

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E326A inactive Rattus norvegicus
E326D inactive Rattus norvegicus
E326H inactive Rattus norvegicus
E326Q inactive Rattus norvegicus
E348A inactive Rattus norvegicus
E348D inactive Rattus norvegicus
E348E inactive Rattus norvegicus
E348H inactive Rattus norvegicus
E348Q inactive Rattus norvegicus
H325A inactive Rattus norvegicus
H325F inactive Rattus norvegicus
H325Y inactive Rattus norvegicus
H329A inactive Rattus norvegicus
H329F inactive Rattus norvegicus
H329Y inactive Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
arphamenine A the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM Rattus norvegicus
Arphamenine B the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM Rattus norvegicus
bestatin the native enzyme is completely inhibited at 0.05 mM, the recombinant enzyme is completely inhibited at 0.1 mM Rattus norvegicus
EDTA the native enzyme is inhibited by 95% at 10 mM, the recombinant enzyme is inhibited by 71% at 10 mM Rattus norvegicus
additional information not affected by phenylmethylsulfonylfluoride Rattus norvegicus
N-ethylmaleimide the native enzyme is inhibited by 45% at 1 mM, the recombinant enzyme is inhibited by 71% at 1 mM Rattus norvegicus
o-phenanthroline the native enzyme is inhibited by 76% at 0.5 mM, the recombinant enzyme is inhibited by 80% at 0.5 mM Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.108
-
 L-Arg-2-naphthylamide
-
 Rattus norvegicus
0.135
-
 L-Lys-2-naphthylamide
-
 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Na+ 3fold increase of activity at 0.2 mM Rattus norvegicus
Zn2+ metalloenzyme containing Zn2+ Rattus norvegicus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
72000
-
 SDS-PAGE Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography and DEAE Trisacryl Plus M column chromatography Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glucagon + H2O
-
 Rattus norvegicus miniglucagon + ?
-
 ?
L-Arg-2-naphthylamide + H2O
-
 Rattus norvegicus L-Arg + 2-naphthylamine
-
 ?
L-Lys-2-naphthylamide + H2O
-
 Rattus norvegicus L-Lys + 2-naphthylamine
-
 ?
leukotriene A4 + H2O has a residual catalytic ability to hydrolyze leukotriene A4 Rattus norvegicus leukotriene B4 + ?
-
 ?

Subunits

Subunits Comment Organism
monomer 1 * 72000, SDS-PAGE Rattus norvegicus

Synonyms

Synonyms Comment Organism
Ap-B
-
 Rattus norvegicus

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3
-
 L-Lys-2-naphthylamide
-
 Rattus norvegicus
20
-
 L-Arg-2-naphthylamide
-
 Rattus norvegicus