Importance of secondary enzyme-substrate interactions in human cathepsin G and chymotrypsin II catalysis

Boudier, Christian; Jung, Marie‐Louise; Stambolieva, N.; Bieth, Joseph G.

doi:10.1016/0003-9861(81)90247-2

Cited by 28 publications

(14 citation statements)

References 27 publications

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“…Residues near to the protease cleavage sites were reported to largely change the hydrolysis kinetics of a protease, which was termed a ‘secondary enzyme–substrate interaction’ . This phenomenon was reported for a variety of proteases, including pepsin, trypsin, chymotrypsin and elastase . Analogously, in this study, crosslinked and non‐crosslinked glycation structures near to a potential cleavage site may also change the action preference and hydrolysis kinetics of pepsin, trypsin, chymotrypsin and elastase, resulting in discrepancies in the digested peptides.…”

Section: Resultssupporting

confidence: 58%

“…35 This phenomenon was reported for a variety of proteases, including pepsin, trypsin, chymotrypsin and elastase. 36,37 Analogously, in this study, crosslinked and non-crosslinked glycation structures near to a potential cleavage site may also change the action preference and hydrolysis kinetics of pepsin, trypsin, chymotrypsin and elastase, resulting in discrepancies in the digested peptides. These changes should largely change the nutritional value of the relevant proteins.…”

Section: Peptide Analysis Of Digests By Lc-esi-ms/msmentioning

confidence: 73%

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Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

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BACKGROUND Milk proteins are widely used in food production and are often glycated by reducing sugar. Although many studies have reported the digestibility of glycated milk protein, most have focused on measuring degree of hydrolysis (DH), showing sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS‐PAGE) image of digests. Detailed information on the changes in peptide composition of digests has seldom been revealed. Therefore, in addition to measuring the DH and showing the SGS‐PAGE images of digests, we also analyzed the peptidomics in digests using liquid chromatography–electrospray ionization–tandem mass spectrometry (LC‐ESI‐MS/MS) and Mascot database in this work to further reveal the influence of glycation on protein nutrition. RESULTS Compared with β‐lactoglobulin and bovine serum albumin (BSA), DH of β‐casein was suppressed to a lesser extent by glycation in both gastric and intestinal stages. Aggregates of glycated BSA were less sensitive to the action of digestive enzymes throughout gastrointestinal digestion according to SDS‐PAGE images. Changes in the peptide composition of digests induced by glycation were distinctly displayed, showing both absence of peptides and occurrence of new peptides, based on the results obtained from LC‐ESI‐MS/MS. CONCLUSIONS Glycation can greatly change the peptide composition in digests of milk protein. The nutritional impact of the change in the peptide composition requires further investigation, and the impact of MRPs in unabsorbed digests on the gut flora should be an interesting field for further studies. © 2018 Society of Chemical Industry

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Section: Resultssupporting

confidence: 58%

Section: Peptide Analysis Of Digests By Lc-esi-ms/msmentioning

confidence: 73%

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Zhao

et al. 2019

J Sci Food Agric

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“…Previously,it was reported that Suc-Tyr-Leu-Phe-pNA(3)was a good substrate for achymotrypsin and its stereoisomer,Suc-Tyr-D-Leu-D-Phe-pNA(7),inhibited the enzyme .In the latter case,the pNA moiety of the peptide significantly participated in binding of the peptide with a-chymotrypsin,resulting in the manifestation of the inhibitory activity.8)Thus, kinetic parameters for the amidolysis of Suc-Tyr-Leu-Phe-pNA(3)and newly synthesized Suc-Ala-Leu-Phe-pNA(5)by cathepsin G were determined and the results are summarized in Table I in comparison with those of a-chymotrypsin.As can be seen in the table,k cat/Km values with cathepsin G are much smaller than those with a-chymotrypsin.This tendency is compatible with data reported previously: 7,9) The hydrolysis of Suc-Phe-pNA(1)and Suc-Leu-Phe-pNA(2)by both enzymes was negligible.For hydrolysis of the Phe-pNA bond,a three amino acids sequence was required. The extension of the tripeptide substrates (3,5)at the N-terminus,Suc-Ala-Tyr-Leu-Phe-pNA (4)and Suc-Ala-Ala-Leu-Phe-pNA(6),resulted in markedly decreased hydrolysis rates of the Phe-pNA bond by both enzymes.Tripeptide substrates are the most favorable for both enzymes when the Leu-Phe-pNA moiety was employed because the kcat/Km values of SucVal-Pro-Phe-pNA and Suc-X-Val-Pro-Phe-pNA(X:Met,Leu,Phe,Ala,Lys and Glu) were similar.10)…”

supporting

confidence: 94%

Amino acids and peptides. XXII. Synthesis of substrates and inhibitors of human leukocyte cathepsin G.

Okada

Tsuda

Teno

et al. 1988

CHEMICAL & PHARMACEUTICAL BULLETIN

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“…The role of substrate conformation was also exemplified by the study of Graf and Hollosi (88) on the conversion by tsypsin of P-lipotropin to P-endorphin which was found to be more specific because of a secondary structure promoting medium. Finally, it has been shown that interactions with part of the substrate remote from the cleavage point are important in promoting proteolysis; this observation, which was first made by Schechter and Berger (89), seems to be true for many and various proteases as presented by Boudier et al (90) conformation (95). The studies of Fletcher et al (36) on proinsulin and proglucagon converting activities in secretory granules seem to confirm the importance of protein sequences around the maturation site.…”

Section: Prepro-calc! Tonlnmentioning

confidence: 77%

Proteases and posttranslational processing of prohormones: a review

Lazure¹,

Seidah²,

Pélaprat³

et al. 1983

Can. J. Biochem. Cell Biol.

138

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Pioneering work on insulin and on lipotropin, published in 1967, led to the formulation of the hypothesis that biologically active peptides such as peptide hormones are derived from larger precursor molecules by enzymatic cleavage at basic amino acid pairs. Since then, an ever-increasing number of hormones and active peptides including neuropeptides have been found to be contained within the sequence of a larger precursor protein and are released by limited proteolytic cleavage. The hypothesis concerning the posttranslational maturation of precursor molecules into smaller active entities is now firmly established in many tissues (e.g., pituitary gland, pancreas) and for all kinds of organisms (e.g. mammals, fish), though the nature of the enzyme(s) responsible for this maturation process still remains unknown. This article presents current knowledge of the intracellular processing of precursor molecules, especially the conversion of prohormone to hormone. The discussion deals principally with the evidences concerning the localization of the maturation process mainly in the secretory granules, the role of basic amino acid pairs at the cleavage site, and the possible involvement of serine and (or) thiol endopeptidases in that process.

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Importance of secondary enzyme-substrate interactions in human cathepsin G and chymotrypsin II catalysis

Cited by 28 publications

References 27 publications

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Digestibility of glycated milk proteins and the peptidomics of their in vitro digests

Amino acids and peptides. XXII. Synthesis of substrates and inhibitors of human leukocyte cathepsin G.

Proteases and posttranslational processing of prohormones: a review

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