One approach to the general problem of the structure and function of enzymes involves proteolytic hydrolysis with examination of the structure, composition, and catalytic activity of the hydrolysis products. Fragments retaining partial enzyme activity have been obtained from trypsin and pepsin by autolysis (2, 3) and from trypsinogen by peptic digestion (4). Over half of the amino acid residues of papain may be removed by aminopeptidase without activity loss (5). Ribonuclease loses activity when a peptide of 20 residues is removed from the NH&erminal end, but regains activity when recombined with the peptide (6). Removal of COOH-terminal residues by carboxypeptidase has little effect on the activity of chymotrypsin (7), lysozyme (S), or ribonuclease (9, 10). In contrast, studies in this laboratory, preliminary to the investigations reported herein, (II), showed that treatment of muscle aldolase by crude trypsin or carboxypeptidase readily caused marked activity loss. The purpose of this paper is to present observations on the striking decrease in aldolase catalytic activity and concomitant change in specificity accompanying release of terminal tyrosine residues by carboxypeptidase digestion.
The catalytic activity of carboxypeptidase-degraded aldolase.
E. Drechsler,P. Boyer,A. Kowalsky
Published 1959 in Journal of Biological Chemistry
ABSTRACT
PUBLICATION RECORD
- Publication year
1959
- Venue
Journal of Biological Chemistry
- Publication date
1959-10-01
- Fields of study
Biology, Medicine, Chemistry
- Identifiers
- External record
- Source metadata
Semantic Scholar, PubMed
CITATION MAP
EXTRACTION MAP
CLAIMS
- Carboxypeptidase digestion of muscle aldolase causes a marked loss of catalytic activity.박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review
CONCEPTS
- aldolase
The glycolytic enzyme examined here for changes in activity and specificity after proteolytic degradation.
Aliases: aldolase enzyme
박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review - carboxypeptidase digestion
Proteolytic treatment with carboxypeptidase used to remove amino acids from the protein's carboxyl terminus.
Aliases: carboxypeptidase-degradation
박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review - catalytic activity
The enzymatic activity of aldolase measured as its ability to catalyze its reaction.
Aliases: enzyme activity
박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review - muscle aldolase
The aldolase preparation isolated from muscle and used as the substrate for carboxypeptidase treatment.
Aliases: muscle enzyme aldolase
박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review - substrate specificity
The pattern of substrates or reaction behavior recognized by aldolase in catalysis.
Aliases: specificity
박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review - terminal tyrosine residues
Tyrosine amino acids located at the carboxyl terminus of the aldolase molecule and released by digestion.
Aliases: COOH-terminal tyrosine residues, C-terminal tyrosine residues
박진우 (dztg5apj7m) extractionAK (4715169a40) reviewKiller Whale (322360f1c1) reviewB (s683577b42) review뀨 (7c402c1b98) reviewq (76h6bfydm6) review
REFERENCES
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