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

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species. / Pedersen, Lotte Bang; Nessi, C; Setlow, P.

In: Journal of Bacteriology, Vol. 179, No. 5, 1997, p. 1824-7.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Pedersen, LB, Nessi, C & Setlow, P 1997, 'Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species.', Journal of Bacteriology, vol. 179, no. 5, pp. 1824-7.

APA

Pedersen, L. B., Nessi, C., & Setlow, P. (1997). Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species. Journal of Bacteriology, 179(5), 1824-7.

Vancouver

Pedersen LB, Nessi C, Setlow P. Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species. Journal of Bacteriology. 1997;179(5):1824-7.

Author

Pedersen, Lotte Bang ; Nessi, C ; Setlow, P. / Most of the propeptide is dispensable for stability and autoprocessing of the zymogen of the germination protease of spores of Bacillus species. In: Journal of Bacteriology. 1997 ; Vol. 179, No. 5. pp. 1824-7.

Bibtex

@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",

}

RIS

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

VL - 179

SP - 1824

EP - 1827

JO - Journal of Bacteriology

JF - Journal of Bacteriology

SN - 0021-9193

IS - 5

ER -

ID: 2830745