STRUCTURAL DETERMINANTS OF THE STABILITY OF THERMOLYSIN-LIKE PROTEINASES

VGH EIJSINK; OR VELTMAN; W AUKEMA; G VRIEND; G VENEMA

STRUCTURAL DETERMINANTS OF THE STABILITY OF THERMOLYSIN-LIKE PROTEINASES

VGH EIJSINK, OR VELTMAN, W AUKEMA, G VRIEND, G VENEMA

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Abstract

Thermolysin is a member of a family of homologous proteinases which differ in their resistance to thermally induced unfolding and subsequent autolytic degradation. Site-directed mutagenesis studies of the thermolysin-like proteinase (TLP) from Bacillus stearothermophilus (TLP-ste) show that its reduced resistance to thermally induced autolysis, as compared to thermolysin, is due to only some of the 44 naturally occurring amino-acid differences between them. in fact TLP-ste becomes more resistant than thermolysin by mutation of just a few of these amino-acids. The crucial differences are all localized to a solvent-exposed region in the N-terminal domain of TLP-ste.

Original language	English
Pages (from-to)	374-379
Number of pages	6
Journal	Nature Structural & Molecular Biology
Volume	2
Issue number	5
Publication status	Published - May-1995

Keywords

STEAROTHERMOPHILUS NEUTRAL PROTEASE
BACILLUS-STEAROTHERMOPHILUS
TRANSITION-STATE
THERMOSTABILITY
SUBTILIS
GENE
RESOLUTION
SUBDOMAINS
EXPRESSION
MUTATIONS

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title = "STRUCTURAL DETERMINANTS OF THE STABILITY OF THERMOLYSIN-LIKE PROTEINASES",

abstract = "Thermolysin is a member of a family of homologous proteinases which differ in their resistance to thermally induced unfolding and subsequent autolytic degradation. Site-directed mutagenesis studies of the thermolysin-like proteinase (TLP) from Bacillus stearothermophilus (TLP-ste) show that its reduced resistance to thermally induced autolysis, as compared to thermolysin, is due to only some of the 44 naturally occurring amino-acid differences between them. in fact TLP-ste becomes more resistant than thermolysin by mutation of just a few of these amino-acids. The crucial differences are all localized to a solvent-exposed region in the N-terminal domain of TLP-ste.",

keywords = "STEAROTHERMOPHILUS NEUTRAL PROTEASE, BACILLUS-STEAROTHERMOPHILUS, TRANSITION-STATE, THERMOSTABILITY, SUBTILIS, GENE, RESOLUTION, SUBDOMAINS, EXPRESSION, MUTATIONS",

author = "VGH EIJSINK and OR VELTMAN and W AUKEMA and G VRIEND and G VENEMA",

year = "1995",

month = may,

language = "English",

volume = "2",

pages = "374--379",

journal = "Nature Structural & Molecular Biology",

issn = "1545-9993",

publisher = "Nature Publishing Group",

number = "5",

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TY - JOUR

T1 - STRUCTURAL DETERMINANTS OF THE STABILITY OF THERMOLYSIN-LIKE PROTEINASES

AU - EIJSINK, VGH

AU - VELTMAN, OR

AU - AUKEMA, W

AU - VRIEND, G

AU - VENEMA, G

PY - 1995/5

Y1 - 1995/5

N2 - Thermolysin is a member of a family of homologous proteinases which differ in their resistance to thermally induced unfolding and subsequent autolytic degradation. Site-directed mutagenesis studies of the thermolysin-like proteinase (TLP) from Bacillus stearothermophilus (TLP-ste) show that its reduced resistance to thermally induced autolysis, as compared to thermolysin, is due to only some of the 44 naturally occurring amino-acid differences between them. in fact TLP-ste becomes more resistant than thermolysin by mutation of just a few of these amino-acids. The crucial differences are all localized to a solvent-exposed region in the N-terminal domain of TLP-ste.

AB - Thermolysin is a member of a family of homologous proteinases which differ in their resistance to thermally induced unfolding and subsequent autolytic degradation. Site-directed mutagenesis studies of the thermolysin-like proteinase (TLP) from Bacillus stearothermophilus (TLP-ste) show that its reduced resistance to thermally induced autolysis, as compared to thermolysin, is due to only some of the 44 naturally occurring amino-acid differences between them. in fact TLP-ste becomes more resistant than thermolysin by mutation of just a few of these amino-acids. The crucial differences are all localized to a solvent-exposed region in the N-terminal domain of TLP-ste.

KW - STEAROTHERMOPHILUS NEUTRAL PROTEASE

KW - BACILLUS-STEAROTHERMOPHILUS

KW - TRANSITION-STATE

KW - THERMOSTABILITY

KW - SUBTILIS

KW - GENE

KW - RESOLUTION

KW - SUBDOMAINS

KW - EXPRESSION

KW - MUTATIONS

M3 - Article

SN - 1545-9993

VL - 2

SP - 374

EP - 379

JO - Nature Structural & Molecular Biology

JF - Nature Structural & Molecular Biology

IS - 5

ER -

STRUCTURAL DETERMINANTS OF THE STABILITY OF THERMOLYSIN-LIKE PROTEINASES

Abstract

Keywords

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