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Literature summary for 3.4.24.28 extracted from

  • Luo, X.; Chen, L.; Huang, Q.; Zheng, J.; Zhou, W.; Peng, D.; Ruan, L.; Sun, M.
    Bacillus thuringiensis metalloproteinase Bmp1 functions as a nematicidal virulence factor (2013), Appl. Environ. Microbiol., 79, 460-468.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.24.28

Cloned(Commentary)

Cloned (Comment) Organism
gene bmp1, recombinant expression in Escherichia coli strain BL21(DE3) Bacillus thuringiensis

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 30-40% inhibition at 4-8 mM Bacillus thuringiensis
Co2+ 30% activation at 8 mM, 40% inhibition at 10 mM Bacillus thuringiensis
EDTA about 50% inhibition at 4-10 mM Bacillus thuringiensis
Mg2+ 72% inhibition at 4-8 mM Bacillus thuringiensis
Mn2+ 64% inhibition at 4-8 mM Bacillus thuringiensis
pepstatin A slight inhibition Bacillus thuringiensis
PMSF about 50% inhibition at 4-8 mM Bacillus thuringiensis
Zn2+ 57% inhibition at 8 mM Bacillus thuringiensis

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ 30% activation at 8 mM, 40% inhibition at 10 mM Bacillus thuringiensis
additional information no effect by Ca2+ Bacillus thuringiensis
Zn2+ required, exogenous Zn2+ activates at 1 mM Bacillus thuringiensis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Bacillus thuringiensis purified Bmp1 protein shows metalloproteinase activity and toxicity against Caenorhabditis elegans, Bmp1 protein destroys the intestinal tissues of Caenorhabditis elegans ?
-
 ?
additional information Bacillus thuringiensis YBT-1518 purified Bmp1 protein shows metalloproteinase activity and toxicity against Caenorhabditis elegans, Bmp1 protein destroys the intestinal tissues of Caenorhabditis elegans ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus thuringiensis L0AQH5 gene bmp1
-
Bacillus thuringiensis YBT-1518 L0AQH5 gene bmp1
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme from Escherichia coli strain BL21(DE3) Bacillus thuringiensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
casein + H2O
-
 Bacillus thuringiensis ?
-
 ?
casein + H2O
-
 Bacillus thuringiensis YBT-1518 ?
-
 ?
additional information purified Bmp1 protein shows metalloproteinase activity and toxicity against Caenorhabditis elegans, Bmp1 protein destroys the intestinal tissues of Caenorhabditis elegans Bacillus thuringiensis ?
-
 ?
additional information purified Bmp1 protein shows metalloproteinase activity and toxicity against Caenorhabditis elegans, Bmp1 protein destroys the intestinal tissues of Caenorhabditis elegans Bacillus thuringiensis YBT-1518 ?
-
 ?

Synonyms

Synonyms Comment Organism
BMP1
-
 Bacillus thuringiensis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
40
-
-
 Bacillus thuringiensis

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
20 60 activity range, recombinant enzyme Bacillus thuringiensis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
-
 Bacillus thuringiensis

pH Range

pH Minimum pH Maximum Comment Organism
5 10 activity range, recombinant enzyme Bacillus thuringiensis

General Information

General Information Comment Organism
evolution metalloproteinase Bmp1 encompasses a consecutive N-terminal signal peptide, an FTP superfamily domain, an M4 neutral protease GluZincin superfamily, two Big-3 superfamily motifs, and a Gram-positive anchor superfamily motif as a C-terminal domain Bacillus thuringiensis
physiological function Bmp1 metalloproteinase is a nematicidal virulence factor, purified Bmp1 protein shows metalloproteinase activity and toxicity against Caenorhabditis elegans, addition of Cry5Ba to Bmp1 protein enhances the toxicity by 7.9fold Bacillus thuringiensis