Active-site residues of procarboxypeptidase Y are accessible to chemical modification

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Standard

Active-site residues of procarboxypeptidase Y are accessible to chemical modification. / Sørensen, S O; Winther, Jakob R.

I: BBA General Subjects, Bind 1205, Nr. 2, 1994, s. 289-93.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Sørensen, SO & Winther, JR 1994, 'Active-site residues of procarboxypeptidase Y are accessible to chemical modification', BBA General Subjects, bind 1205, nr. 2, s. 289-93.

APA

Sørensen, S. O., & Winther, J. R. (1994). Active-site residues of procarboxypeptidase Y are accessible to chemical modification. BBA General Subjects, 1205(2), 289-93.

Vancouver

Sørensen SO, Winther JR. Active-site residues of procarboxypeptidase Y are accessible to chemical modification. BBA General Subjects. 1994;1205(2):289-93.

Author

Sørensen, S O ; Winther, Jakob R. / Active-site residues of procarboxypeptidase Y are accessible to chemical modification. I: BBA General Subjects. 1994 ; Bind 1205, Nr. 2. s. 289-93.

Bibtex

@article{60a5e1ebeff2439e80dafd4adc899e18,
title = "Active-site residues of procarboxypeptidase Y are accessible to chemical modification",
abstract = "The accessibility of the active-site cleft of procarboxypeptidase Y from Saccharomyces cerevisiae has been studied by chemical modifications of two specific amino-acid residues. Previous studies have shown that these residues, Cys-341 and Met-398 in the mature enzyme, are located in the S1 and S'1 substrate binding sites, respectively, of carboxypeptidase Y. We have found that these residues also in proCPY are accessible to modification with fairly bulky reagents and in the case of Met-398 the rate of modification is even faster than in carboxypeptidase Y. While the catalytic serine in the mature enzyme reacts with diisopropylfluorophosphate, this is not the case for procarboxypeptidase Y.",
keywords = "Acetophenones, Binding Sites, Carboxypeptidases, Cathepsin A, Enzyme Precursors, Enzyme Stability, Isoflurophate, Mercuric Chloride, Phenylmercury Compounds, Protein Conformation, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins",
author = "S{\o}rensen, {S O} and Winther, {Jakob R.}",
year = "1994",
language = "English",
volume = "1205",
pages = "289--93",
journal = "B B A - General Subjects",
issn = "0304-4165",
publisher = "Elsevier",
number = "2",

}

RIS

TY - JOUR

T1 - Active-site residues of procarboxypeptidase Y are accessible to chemical modification

AU - Sørensen, S O

AU - Winther, Jakob R.

PY - 1994

Y1 - 1994

N2 - The accessibility of the active-site cleft of procarboxypeptidase Y from Saccharomyces cerevisiae has been studied by chemical modifications of two specific amino-acid residues. Previous studies have shown that these residues, Cys-341 and Met-398 in the mature enzyme, are located in the S1 and S'1 substrate binding sites, respectively, of carboxypeptidase Y. We have found that these residues also in proCPY are accessible to modification with fairly bulky reagents and in the case of Met-398 the rate of modification is even faster than in carboxypeptidase Y. While the catalytic serine in the mature enzyme reacts with diisopropylfluorophosphate, this is not the case for procarboxypeptidase Y.

AB - The accessibility of the active-site cleft of procarboxypeptidase Y from Saccharomyces cerevisiae has been studied by chemical modifications of two specific amino-acid residues. Previous studies have shown that these residues, Cys-341 and Met-398 in the mature enzyme, are located in the S1 and S'1 substrate binding sites, respectively, of carboxypeptidase Y. We have found that these residues also in proCPY are accessible to modification with fairly bulky reagents and in the case of Met-398 the rate of modification is even faster than in carboxypeptidase Y. While the catalytic serine in the mature enzyme reacts with diisopropylfluorophosphate, this is not the case for procarboxypeptidase Y.

KW - Acetophenones

KW - Binding Sites

KW - Carboxypeptidases

KW - Cathepsin A

KW - Enzyme Precursors

KW - Enzyme Stability

KW - Isoflurophate

KW - Mercuric Chloride

KW - Phenylmercury Compounds

KW - Protein Conformation

KW - Saccharomyces cerevisiae

KW - Saccharomyces cerevisiae Proteins

M3 - Journal article

C2 - 8155711

VL - 1205

SP - 289

EP - 293

JO - B B A - General Subjects

JF - B B A - General Subjects

SN - 0304-4165

IS - 2

ER -

ID: 43974409