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Literature summary extracted from

  • Morita, H.; Tomita, S.; Maeda, H.; Okamoto, A.; Yamagata, Y.; Kusumoto, K.; Amano, H.; Ishida, H.; Takeuchi, M.
    Serine-type carboxypeptidase KexA of Aspergillus oryzae has broader substrate specificity than Saccharomyces cerevisiae Kex1 and is required for normal hyphal growth and conidiation (2012), Appl. Environ. Microbiol., 78, 8154-8157.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.16.6 a truncated form of KexA (amino acid residues 1 to 526 of KexA), which lack the potential transmembrane region and the succeeding C-terminal sequence (amino acid residues 527 to 625 of KexA) is expressed by using a protein expression system with the pIECS3 vector and Aspergillus nidulans Aspergillus oryzae

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.16.6 EDTA 14% inhibition Aspergillus oryzae
3.4.16.6 monoiodo acetic acid 90% inhibition Aspergillus oryzae
3.4.16.6 PMSF 68% inhibition Aspergillus oryzae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.4.16.6 58820
-
 truncated form, calculated from cDNA Aspergillus oryzae

Organism

EC Number Organism UniProt Comment Textmining
3.4.16.6 Aspergillus oryzae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.16.6 using anion-exchange chromatography and gel filtration Aspergillus oryzae

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.16.6 angiotensin 1 + H2O truncated KexA releases amino acid residues from the C terminus of angiotensin I Aspergillus oryzae ?
-
 ?
3.4.16.6 benzoyl-Gly-Arg + H2O enzyme shows very low activity Aspergillus oryzae benzoyl-Gly + L-arginine
-
 ?
3.4.16.6 benzyloxycarbonyl-Gly-Lys + H2O enzyme shows very low activity Aspergillus oryzae benzyloxycarbonyl-Gly + L-lysine
-
 ?
3.4.16.6 benzyloxycarbonyl-Phe-Leu + H2O enzyme shows very low activity Aspergillus oryzae benzyloxycarbonyl-Phe + L-leucine
-
 ?
3.4.16.6 benzyloxycarbonyl-Phe-Tyr-Leu + H2O
-
 Aspergillus oryzae benzyloxycarbonyl-Phe-Tyr + L-leucine
-
 ?
3.4.16.6 benzyloxycarbonyl-Tyr-Leu + H2O enzyme shows very low activity Aspergillus oryzae benzyloxycarbonyl-Tyr + L-leucine
-
 ?
3.4.16.6 bradykinin I + H2O truncated KexA releases amino acid residues from the C terminus of bradykinin I Aspergillus oryzae ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.4.16.6 KexA
-
 Aspergillus oryzae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.16.6 40
-
 maximum temperature at which the enzyme has residual activity of over 60% relative to maximum activity Aspergillus oryzae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.16.6 5.5
-
-
 Aspergillus oryzae

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.4.16.6 5 8
-
 Aspergillus oryzae

General Information

EC Number General Information Comment Organism
3.4.16.6 malfunction kexA deletion strain shows slightly lower growth speed. Deletion strain exhibits scarcely branched hyphae, whereas an kexA-overexpressing strain exhibits a hyperbranching phenotype Aspergillus oryzae