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

S O Sørensen; Jakob R. Winther

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

Biomolecular Sciences

5 Citationer (Scopus)

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.

Originalsprog	Engelsk
Tidsskrift	BBA General Subjects
Vol/bind	1205
Udgave nummer	2
Sider (fra-til)	289-93
Antal sider	5
ISSN	0304-4165
Status	Udgivet - 1994

Citationsformater

@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",

}

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

SN - 0304-4165

VL - 1205

SP - 289

EP - 293

JO - B B A - General Subjects

JF - B B A - General Subjects

IS - 2

ER -

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

Abstract

Fingeraftryk

Citationsformater