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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.11.6 expressed in Escherichia coli Rattus norvegicus

Protein Variants

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.11.6 arphamenine A the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM Rattus norvegicus
3.4.11.6 Arphamenine B the native enzyme is completely inhibited at 0.001 mM, the recombinant enzyme is completely inhibited at 0.001 mM Rattus norvegicus
3.4.11.6 bestatin the native enzyme is completely inhibited at 0.05 mM, the recombinant enzyme is completely inhibited at 0.1 mM Rattus norvegicus
3.4.11.6 EDTA the native enzyme is inhibited by 95% at 10 mM, the recombinant enzyme is inhibited by 71% at 10 mM Rattus norvegicus
3.4.11.6 additional information not affected by phenylmethylsulfonylfluoride Rattus norvegicus
3.4.11.6 N-ethylmaleimide the native enzyme is inhibited by 45% at 1 mM, the recombinant enzyme is inhibited by 71% at 1 mM Rattus norvegicus
3.4.11.6 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.4.11.6 0.108
-
 L-Arg-2-naphthylamide
-
 Rattus norvegicus
3.4.11.6 0.135
-
 L-Lys-2-naphthylamide
-
 Rattus norvegicus

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.11.6 72000
-
 SDS-PAGE Rattus norvegicus

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.6 Rattus norvegicus
-
-
-

Purification (Commentary)

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

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.11.6 testis
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

EC Number Synonyms Comment Organism
3.4.11.6 Ap-B
-
 Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
3.4.11.6 3
-
 L-Lys-2-naphthylamide
-
 Rattus norvegicus
3.4.11.6 20
-
 L-Arg-2-naphthylamide
-
 Rattus norvegicus