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Rapid degradation of D- and L-succinimide-containing peptides by a post-proline endopeptidase from human erythrocytes

Journal Article · · Biochemistry; (United States)
DOI:https://doi.org/10.1021/bi00398a040· OSTI ID:5446051
;
The authors have been interested in the metabolic fate of proteins containing aspartyl succinimide (Asu) residues. These residues can be derived from the spontaneous rearrangement of Asp and Asn residues and from the spontaneous demethylation of enzymatically methylated L-isoAsp and D-Asp residues. Incubation of the synthetic hexapeptide N-Ac-Val-Tyr-Pro-Asu-Gly-Ala with the cytosolic fraction of human erythrocytes resulted in rapid cleavage of the prolyl-aspartyl succinimide bond producing the tripeptide N-Ac-Val-Try-Pro. The rate of this reaction is equal for both L- and D-Asu-containing peptides and is 10-fold greater that the rate of cleavage of a corresponding peptide containing a normal Pro-Asp linkage. When the aspartyl succinimide ring was replaced with an isoaspartyl residue, the cleavage rate was about 5 times that of the normal Pro-Asp peptide. The tripeptide-producing activity copurified on DEAE-cellulose chromatography with an activity that cleaves N-carbobenzoxy-Gly-Pro-4-methylcoumarin-7-amide, a post-proline endopeptidase substrate. These two activities were both inhibited by an antiserum to rat brain post-proline endopeptidase, and it appears that they are catalyzed by the same enzyme. This enzyme has a molecular weight of approximately 80,000 and is covalently labeled and inhibited by (/sup 3/H) diisopropyl fluorophosphate. The facile cleavage of the succinimide- and isoaspartyl-containing peptides by this post-proline endopeptidase suggests that it may play a role in the metabolism of peptides containing altered aspartyl residues.
Research Organization:
Univ. of California, Los Angeles
OSTI ID:
5446051
Journal Information:
Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:24; ISSN BICHA
Country of Publication:
United States
Language:
English

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Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINOPEPTIDASES
BIOCHEMISTRY
BIODEGRADATION
BIOLOGICAL MATERIALS
BIOLOGICAL PATHWAYS
BLOOD
BLOOD CELLS
BODY FLUIDS
CARBON 14 COMPOUNDS
CARBOXYLIC ACIDS
CHEMICAL REACTIONS
CHEMISTRY
CHROMATOGRAPHY
DECOMPOSITION
DICARBOXYLIC ACIDS
ENZYMES
ERYTHROCYTES
HYDROLASES
ION EXCHANGE CHROMATOGRAPHY
LABELLED COMPOUNDS
MATERIALS
ORGANIC ACIDS
ORGANIC COMPOUNDS
PEPTIDE HYDROLASES
PEPTIDES
PROTEINS
SEPARATION PROCESSES
SUCCINIC ACID
TRITIUM COMPOUNDS