Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species.

Lotte Bang Pedersen; C Nessi; P Setlow

Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species.

Cellebiologi og Fysiologi

9 Citationer (Scopus)

Abstract

Loss of 3, 7, or 10 of the amino-terminal 15 residues removed upon autoactivation of the zymogen of the germination protease (GPR), which initiates protein degradation during germination of spores of Bacillus species, did not result in significant changes in (i) the lack of enzymatic activity of the zymogen, (ii) the rate of zymogen autoactivation, or (iii) the unreactivity of the zymogen's single SH group. Removal of 13 amino-terminal residues resulted in a partially active enzyme whose SH group was as reactive as the fully active enzyme. These findings suggest that at least a part of the propeptide blocks access to the enzyme's active site. However, the free propeptide did not inhibit the enzyme.
Udgivelsesdato: 1997-Mar

Originalsprog	Engelsk
Tidsskrift	Journal of Bacteriology
Vol/bind	179
Udgave nummer	5
Sider (fra-til)	1824-7
Antal sider	3
ISSN	0021-9193
Status	Udgivet - 1997

Citationsformater

@article{67970f50e07911dcbee902004c4f4f50,

title = "Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species.",

abstract = "Loss of 3, 7, or 10 of the amino-terminal 15 residues removed upon autoactivation of the zymogen of the germination protease (GPR), which initiates protein degradation during germination of spores of Bacillus species, did not result in significant changes in (i) the lack of enzymatic activity of the zymogen, (ii) the rate of zymogen autoactivation, or (iii) the unreactivity of the zymogen's single SH group. Removal of 13 amino-terminal residues resulted in a partially active enzyme whose SH group was as reactive as the fully active enzyme. These findings suggest that at least a part of the propeptide blocks access to the enzyme's active site. However, the free propeptide did not inhibit the enzyme. Udgivelsesdato: 1997-Mar",

author = "Pedersen, {Lotte Bang} and C Nessi and P Setlow",

note = "Keywords: Amino Acid Sequence; Bacillus; Binding Sites; Endopeptidases; Enzyme Precursors; Molecular Sequence Data; Protein Processing, Post-Translational; Spores, Bacterial",

year = "1997",

language = "English",

volume = "179",

pages = "1824--7",

journal = "Journal of Bacteriology",

issn = "0021-9193",

publisher = "American Society for Microbiology",

number = "5",

}

TY - JOUR

T1 - Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species.

AU - Pedersen, Lotte Bang

AU - Nessi, C

AU - Setlow, P

N1 - Keywords: Amino Acid Sequence; Bacillus; Binding Sites; Endopeptidases; Enzyme Precursors; Molecular Sequence Data; Protein Processing, Post-Translational; Spores, Bacterial

PY - 1997

Y1 - 1997

N2 - Loss of 3, 7, or 10 of the amino-terminal 15 residues removed upon autoactivation of the zymogen of the germination protease (GPR), which initiates protein degradation during germination of spores of Bacillus species, did not result in significant changes in (i) the lack of enzymatic activity of the zymogen, (ii) the rate of zymogen autoactivation, or (iii) the unreactivity of the zymogen's single SH group. Removal of 13 amino-terminal residues resulted in a partially active enzyme whose SH group was as reactive as the fully active enzyme. These findings suggest that at least a part of the propeptide blocks access to the enzyme's active site. However, the free propeptide did not inhibit the enzyme. Udgivelsesdato: 1997-Mar

AB - Loss of 3, 7, or 10 of the amino-terminal 15 residues removed upon autoactivation of the zymogen of the germination protease (GPR), which initiates protein degradation during germination of spores of Bacillus species, did not result in significant changes in (i) the lack of enzymatic activity of the zymogen, (ii) the rate of zymogen autoactivation, or (iii) the unreactivity of the zymogen's single SH group. Removal of 13 amino-terminal residues resulted in a partially active enzyme whose SH group was as reactive as the fully active enzyme. These findings suggest that at least a part of the propeptide blocks access to the enzyme's active site. However, the free propeptide did not inhibit the enzyme. Udgivelsesdato: 1997-Mar

M3 - Journal article

C2 - 9045848

SN - 0021-9193

VL - 179

SP - 1824

EP - 1827

JO - Journal of Bacteriology

JF - Journal of Bacteriology

IS - 5

ER -