Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity

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Standard

Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. / Winther, Jakob R.; Sørensen, P.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 88, Nr. 20, 1991, s. 9330-4.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Winther, JR & Sørensen, P 1991, 'Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity', Proceedings of the National Academy of Sciences of the United States of America, bind 88, nr. 20, s. 9330-4.

APA

Winther, J. R., & Sørensen, P. (1991). Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proceedings of the National Academy of Sciences of the United States of America, 88(20), 9330-4.

Vancouver

Winther JR, Sørensen P. Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. Proceedings of the National Academy of Sciences of the United States of America. 1991;88(20):9330-4.

Author

Winther, Jakob R. ; Sørensen, P. / Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity. I: Proceedings of the National Academy of Sciences of the United States of America. 1991 ; Bind 88, Nr. 20. s. 9330-4.

Bibtex

@article{1e42b22ed3314a22a9ac23de517969f5,
title = "Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity",
abstract = "The zymogen of the vacuolar carboxypeptidase Y from Saccharomyces cerevisiae was purified and characterized with respect to activation as well as refolding in vitro. The purified procarboxypeptidase Y has no detectable activity but can be efficiently activated by proteinase K from Tritirachium album. We used this method of activation as a tool for the investigation of refolding procarboxypeptidase Y in vitro. The proenzyme, denatured in 6 M guanidinium chloride, is renatured efficiently after dilution of the denaturant, whereas the mature enzyme regains little activity in the same procedure. Changes in intrinsic fluorescence reveal the mature enzyme to be considerably more stable than the proenzyme toward denaturation with guanidinium chloride. This suggests that the propeptide induces a metastable structure important for overcoming energy barriers that might otherwise obstruct a productive folding pathway. The relatively large number of charged amino acid residues and a high theoretical potential for alpha-helix formation in the carboxypeptidase Y propeptide suggest a structural similarity to a number of other propeptides and heat shock proteins.",
keywords = "Carboxypeptidases, Cathepsin A, Endopeptidases, Enzyme Precursors, Guanidine, Guanidines, Heat-Shock Proteins, Kinetics, Mitosporic Fungi, Osmolar Concentration, Protein Denaturation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Spectrometry, Fluorescence, Substrate Specificity",
author = "Winther, {Jakob R.} and P S{\o}rensen",
year = "1991",
language = "English",
volume = "88",
pages = "9330--4",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "20",

}

RIS

TY - JOUR

T1 - Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzymatic activity

AU - Winther, Jakob R.

AU - Sørensen, P

PY - 1991

Y1 - 1991

N2 - The zymogen of the vacuolar carboxypeptidase Y from Saccharomyces cerevisiae was purified and characterized with respect to activation as well as refolding in vitro. The purified procarboxypeptidase Y has no detectable activity but can be efficiently activated by proteinase K from Tritirachium album. We used this method of activation as a tool for the investigation of refolding procarboxypeptidase Y in vitro. The proenzyme, denatured in 6 M guanidinium chloride, is renatured efficiently after dilution of the denaturant, whereas the mature enzyme regains little activity in the same procedure. Changes in intrinsic fluorescence reveal the mature enzyme to be considerably more stable than the proenzyme toward denaturation with guanidinium chloride. This suggests that the propeptide induces a metastable structure important for overcoming energy barriers that might otherwise obstruct a productive folding pathway. The relatively large number of charged amino acid residues and a high theoretical potential for alpha-helix formation in the carboxypeptidase Y propeptide suggest a structural similarity to a number of other propeptides and heat shock proteins.

AB - The zymogen of the vacuolar carboxypeptidase Y from Saccharomyces cerevisiae was purified and characterized with respect to activation as well as refolding in vitro. The purified procarboxypeptidase Y has no detectable activity but can be efficiently activated by proteinase K from Tritirachium album. We used this method of activation as a tool for the investigation of refolding procarboxypeptidase Y in vitro. The proenzyme, denatured in 6 M guanidinium chloride, is renatured efficiently after dilution of the denaturant, whereas the mature enzyme regains little activity in the same procedure. Changes in intrinsic fluorescence reveal the mature enzyme to be considerably more stable than the proenzyme toward denaturation with guanidinium chloride. This suggests that the propeptide induces a metastable structure important for overcoming energy barriers that might otherwise obstruct a productive folding pathway. The relatively large number of charged amino acid residues and a high theoretical potential for alpha-helix formation in the carboxypeptidase Y propeptide suggest a structural similarity to a number of other propeptides and heat shock proteins.

KW - Carboxypeptidases

KW - Cathepsin A

KW - Endopeptidases

KW - Enzyme Precursors

KW - Guanidine

KW - Guanidines

KW - Heat-Shock Proteins

KW - Kinetics

KW - Mitosporic Fungi

KW - Osmolar Concentration

KW - Protein Denaturation

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

KW - Spectrometry, Fluorescence

KW - Substrate Specificity

M3 - Journal article

C2 - 1924396

VL - 88

SP - 9330

EP - 9334

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 20

ER -

ID: 43974556