Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.1.5 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
Search for more literature for 3.1.1.5

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
spore spore coat Bacillus subtilis
-

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
LipC
-
 Bacillus subtilis
phospholipase B
-
 Bacillus subtilis

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
-
 Bacillus subtilis

General Information

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