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Literature summary extracted from

  • Masayama, A.; Kato, S.; Terashima, T.; M?lgaard, A.; Hemmi, H.; Yoshimura, T.; Moriyama, R.
    Bacillus subtilis spore coat protein LipC is a phospholipase B (2010), Biosci. Biotechnol. Biochem., 74, 24-30.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.1.1.5 expressed in Escherichia coli BL21(DE3) cells Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
3.1.1.5 S11A the amount of free fatty acids in the mutant spores is about 35fold less than in the wild type spores Bacillus subtilis

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.5 Ca2+ 40% residual activity at 1 mM Bacillus subtilis
3.1.1.5 calcium dipicolinate 71% residual activity at 1 mM Bacillus subtilis
3.1.1.5 D-alanine 94% residual activity at 1 mM Bacillus subtilis
3.1.1.5 dipicolinate 82% residual activity at 1 mM Bacillus subtilis
3.1.1.5 dithiothreitol 78% residual activity at 5 mM Bacillus subtilis
3.1.1.5 EDTA 81% residual activity at 5 mM Bacillus subtilis
3.1.1.5 Hg2+ 61% residual activity at 1 mM Bacillus subtilis
3.1.1.5 L-alanine 93% residual activity at 1 mM Bacillus subtilis
3.1.1.5 Mn2+ 67% residual activity at 1 mM Bacillus subtilis
3.1.1.5 phenylmethylsulfonyl fluoride 72% residual activity at 1 mM Bacillus subtilis
3.1.1.5 Zn2+ 84% residual activity at 1 mM Bacillus subtilis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.1.5 Cu2+ 127% activity at 1 mM Bacillus subtilis
3.1.1.5 Fe2+ 124% activity at 1 mM Bacillus subtilis
3.1.1.5 additional information not influenced by Mg2+ Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.5 24669
-
 1 * 24669, deduced from amino acid sequence Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.5 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.5 His bind resin column chromatography Bacillus subtilis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.5 spore spore coat Bacillus subtilis
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.5 4-nitrophenyl butyrate + H2O
-
 Bacillus subtilis 4-nitrophenol + butyrate
-
 ?
3.1.1.5 4-nitrophenyl decanoate + H2O
-
 Bacillus subtilis 4-nitrophenol + decanoate
-
 ?
3.1.1.5 4-nitrophenyl hexanoate + H2O
-
 Bacillus subtilis 4-nitrophenol + hexanoate
-
 ?
3.1.1.5 4-nitrophenyl myristate + H2O best substrate Bacillus subtilis 4-nitrophenol + myristate
-
 ?
3.1.1.5 4-nitrophenyl palmitate + H2O
-
 Bacillus subtilis 4-nitrophenol + palmitate
-
 ?
3.1.1.5 4-nitrophenyl stearate + H2O worst substrate Bacillus subtilis 4-nitrophenol + stearate
-
 ?
3.1.1.5 additional information LipC cleaves both ester linkages of the sn-1 and sn-2 positions of phospholipids (phospholipase B activity) Bacillus subtilis ?
-
 ?
3.1.1.5 additional information no activity with tributyrin, tricaprilin or triolein Bacillus subtilis ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.1.5 monomer 1 * 24669, deduced from amino acid sequence Bacillus subtilis

Synonyms

EC Number Synonyms Comment Organism
3.1.1.5 LipC
-
 Bacillus subtilis
3.1.1.5 phospholipase B
-
 Bacillus subtilis

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.1.1.5 60 70 less than 20% activity remains after 30 min incubation at above 60°C Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.1.1.5 8.5
-
-
 Bacillus subtilis

General Information

EC Number General Information Comment Organism
3.1.1.5 physiological function LipC plays an important role in the degradation of the outer spore membrane during sporulation Bacillus subtilis