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

BRENDA support

Literature summary for 3.4.22.34 extracted from

  • Saska, I.; Gillon, A.D.; Hatsugai, N.; Dietzgen, R.G.; Hara-Nishimura, I.; Anderson, M.A.; Craik, D.J.
    An asparaginyl endopeptidase mediates in vivo protein backbone cyclization (2007), J. Biol. Chem., 282, 29721-29728.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
acetyl-Glu-Ser-Glu-Asn-aldehyde hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner Nicotiana benthamiana
acetyl-Glu-Ser-Glu-Asn-aldehyde hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner Oldenlandia affinis
acetyl-Glu-Ser-Glu-Asn-aldehyde hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner Viola tricolor
Acetyl-Tyr-Val-Ala-Asp-aldehyde hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner, reduced amounts of cyclic cyclotide produced in transiently transformed tobacco leaves determined Nicotiana benthamiana
Acetyl-Tyr-Val-Ala-Asp-aldehyde hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner Oldenlandia affinis
Acetyl-Tyr-Val-Ala-Asp-aldehyde hydrolysis of the the Asn-containing substrate inhibited in a concentration-dependent manner Viola tricolor
pepstatin A no effect on ability to cleave the Asn-containing substrate Nicotiana benthamiana
pepstatin A no effect on ability to cleave the Asn-containing substrate Oldenlandia affinis
pepstatin A no effect on ability to cleave the Asn-containing substrate Viola tricolor
phenylmethylsulfonyl fluoride no effect on ability to cleave the Asn-containing substrate Nicotiana benthamiana
phenylmethylsulfonyl fluoride no effect on ability to cleave the Asn-containing substrate Oldenlandia affinis
phenylmethylsulfonyl fluoride no effect on ability to cleave the Asn-containing substrate Viola tricolor
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane i.e. E-64, no effect on ability to cleave the Asn-containing substrate Nicotiana benthamiana
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane i.e. E-64, no effect on ability to cleave the Asn-containing substrate Oldenlandia affinis
trans-epoxysuccinyl-L-leucylamido(4-guanidino)butane i.e. E-64, no effect on abilityto cleave the Asn-containing substrate Viola tricolor

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Nicotiana benthamiana role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event ?
-
?
additional information Viola tricolor role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event ?
-
?
additional information Oldenlandia affinis role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event ?
-
?

Organism

Organism UniProt Comment Textmining
Nicotiana benthamiana
-
no endogenous cyclotides, transiently transformed with the cyclotide kalata B1
-
Oldenlandia affinis
-
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-
Viola tricolor
-
endogenous cyclotides as potential substrates for backbone cyclization by legumain analyzed
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf leaf extracts, assay for asparaginyl bond hydrolysis in Viola tricolor
-
leaf leaf extracts, assay for asparaginyl bond hydrolysis in Oldenlandia affinis
-
leaf leaf extracts, assay for asparaginyl bond hydrolysis in, analysis of backbone cyclization of endogenous cyclotides in Nicotiana benthamiana
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
involvement of legumain in backbone cyclization of plant-produced cyclotides analyzed, assay for asparaginyl bond hydrolysis in leaf extracts described Viola tricolor
additional information
-
involvement of legumain in backbone cyclization of plant-produced cyclotides analyzed, assay for asparaginyl bond hydrolysis in leaf extracts described Oldenlandia affinis
additional information
-
involvement of legumain in backbone cyclization of plant-produced cyclotides determined, transient expression of precursor of the cyclotide kalata B1 in tobacco leads to production of the circular cyclotide, in vivo asparaginyl bond hydrolysis shown to be necessary for cyclization, reduced amounts of cyclic cyclotide shown by suppression of legumain either by decreasing gene expression or by a specific inhibitor, detection and quantification of cyclotide proteins by MALDI-TOF Nicotiana benthamiana

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O role of legumain in backbone cyclization of proteins analyzed, catalysis of protein backbone cyclization by coupling asparaginyl bond hydrolysis at the C terminus of the cyclotide domain with peptide bond ligation Viola tricolor benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O role of legumain in backbone cyclization of proteins analyzed, catalysis of protein backbone cyclization by coupling asparaginyl bond hydrolysis at the C terminus of the cyclotide domain with peptide bond ligation Oldenlandia affinis benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
?
benzyloxycarbonyl-Ala-Ala-Asn-4-methylcoumarin-7-amide + H2O role of legumain in backbone cyclization of proteins determined, catalysis of protein backbone cyclization by coupling asparaginyl bond hydrolysis at the C terminus of the cyclotide domain with peptide bond ligation Nicotiana benthamiana benzyloxycarbonyl-Ala-Ala-Asn + 7-amino-4-methylcoumarin
-
?
additional information role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event Nicotiana benthamiana ?
-
?
additional information role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event Viola tricolor ?
-
?
additional information role in backbone cyclization of proteins determined, catalyis of peptide bond cleavage and of ligation of plant-specific cyclotides in a single processing event Oldenlandia affinis ?
-
?

Synonyms

Synonyms Comment Organism
AEP
-
Nicotiana benthamiana
AEP
-
Viola tricolor
AEP
-
Oldenlandia affinis
asparagine endopeptidase
-
Nicotiana benthamiana
asparagine endopeptidase
-
Viola tricolor
asparagine endopeptidase
-
Oldenlandia affinis