[51] Peptidyl-asp metalloendopeptidase

Hagmann, Marie-Luise; Geuß, U.; Fischer, Stephan; Kresse, Georg-Burkhard

doi:10.1016/0076-6879(95)48053-6

Cited by 14 publications

(3 citation statements)

References 8 publications

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“…Therefore, it was further digested with endoproteinase Asp‐N. This enzyme is expected to cleave at the N ‐terminal side of aspartic acid residues41 and occasionally also at the N ‐terminal side of glutamic acid residues 42, 43. Using this enzyme, cleavage was expected N ‐terminal to the Asp residue at position 16.…”

Section: Resultsmentioning

confidence: 99%

Structure determination of two conotoxins fromConus textile by a combination of matrix-assisted laser desorption/ionization time-of-flight and electrospray ionization mass spectrometry and biochemical methods

et al. 2000

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Two highly modified conotoxins from the mollusc Conus textile, ϵ‐TxIX and Gla(1)‐TxVI, were characterized by matrix‐assisted laser desorption/ionization and electrospray mass spectrometry and also by electrospray ionization tandem and triple mass spectrometry in combination with enzymatic cleavage and chemical modification reactions. The mass spectrometric studies allowed the confirmation of the sequence determined by Edman degradation and assignment of unidentified amino acid residues, among which bromotryptophan residues and an O‐glycosylated threonine residue were observed. Methyl esterification was found necessary for the site‐specific assignment of the Gla residues in the peptides. Copyright © 2000 John Wiley & Sons, Ltd.

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Section: Resultsmentioning

confidence: 99%

Structure determination of two conotoxins fromConus textile by a combination of matrix-assisted laser desorption/ionization time-of-flight and electrospray ionization mass spectrometry and biochemical methods

et al. 2000

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“…However, the length of the peptide fragment generated by LysN that includes S129 (Table ) is longer than the pore’s length and therefore not within the detectable and discernible length range for polypeptide discrimination with the AeL nanopore. , We overcame that limitation by changing the protease to cleave the relevant fragment into one that is sufficiently short. Specifically, we used another enzyme, AspN peptidyl-Asp metalloendopeptidase from the Gram-negative bacteria Pseudomonas fragi, − which cleaves at the amino terminus side of aspartic acid residues. This process should produce the polypeptide fragments listed in Table .…”

Section: Resultsmentioning

confidence: 99%

Discrimination between Alpha-Synuclein Protein Variants with a Single Nanometer-Scale Pore

Bakshloo

Yahiaoui

Bourderioux

et al. 2023

ACS Chem. Neurosci.

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Alpha-synuclein is one of several key factors in the regulation of nerve activity. It is striking that single-or multiplepoint mutations in the 140-amino-acid-long protein can change its structure, which leads to the protein's aggregation and fibril formation (which is associated with several neurodegenerative diseases, e.g., Parkinson's disease). We recently demonstrated that a single nanometer-scale pore can identify proteins based on its ability to discriminate between protease-generated polypeptide fragments. We show here that a variation of this method can readily discriminate between the wild-type alpha synuclein, a known deleterious point mutation of the glutamic acid at position 46 replaced with a lysine (E46K), and post-translational modifications (i.e., tyrosine Y39 nitration and serine 129 phosphorylation).

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“…This enzyme is expected to cleave at the N-terminal side of aspartic acid residues 41 and occasionally also at the N-terminal side of glutamic acid residues. 42,43 Using this enzyme, cleavage was expected N-terminal to the Asp residue at position 16. The digestion mixture was analyzed by ESIMS on a Q-TOF mass spectrometer.…”

Section: Mass Spectrometric Characterization Of Conotoxin Gla(1)-txvimentioning

confidence: 99%

Structure determination of two conotoxins from Conus textile by a combination of matrix‐assisted laser desorption/ionization time‐of‐flight and electrospray ionization mass spectrometry and biochemical methods

Kalume¹,

Stenflo²,

Czerwiec³

et al. 2000

J. Mass Spectrom.

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Two highly modified conotoxins from the mollusc Conus textile, "-TxIX and Gla(1)-TxVI, were characterized by matrix-assisted laser desorption/ionization and electrospray mass spectrometry and also by electrospray ionization tandem and triple mass spectrometry in combination with enzymatic cleavage and chemical modification reactions. The mass spectrometric studies allowed the confirmation of the sequence determined by Edman degradation and assignment of unidentified amino acid residues, among which bromotryptophan residues and an O-glycosylated threonine residue were observed. Methyl esterification was found necessary for the site-specific assignment of the Gla residues in the peptides.

show abstract

[51] Peptidyl-asp metalloendopeptidase

Cited by 14 publications

References 8 publications

Structure determination of two conotoxins fromConus textile by a combination of matrix-assisted laser desorption/ionization time-of-flight and electrospray ionization mass spectrometry and biochemical methods

Structure determination of two conotoxins fromConus textile by a combination of matrix-assisted laser desorption/ionization time-of-flight and electrospray ionization mass spectrometry and biochemical methods

Discrimination between Alpha-Synuclein Protein Variants with a Single Nanometer-Scale Pore

Structure determination of two conotoxins from Conus textile by a combination of matrix‐assisted laser desorption/ionization time‐of‐flight and electrospray ionization mass spectrometry and biochemical methods

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