Difference between revisions of "Lip"

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<pubmed> 15812018,12523966,18721749,12218047,16342303, 12951259 11583117 11491291</pubmed>
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[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 14:42, 20 November 2011

  • Description: extracellular lipase

Gene name lip
Synonyms lipA
Essential no
Product extracellular lipase
Function lipid degradation
MW, pI 22 kDa, 10.059
Gene length, protein length 636 bp, 212 aa
Immediate neighbours ansZ, yczC
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Lip context.gif
This image was kindly provided by SubtiList




Categories containing this gene/protein

utilization of lipids

This gene is a member of the following regulons

AbrB regulon

The gene

Basic information

  • Locus tag: BSU02700

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family:
  • Paralogous protein(s): LipB

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • the amount of the mRNA is substantially decreased upon depletion of RNase Y PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J  
RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. 
Mol Microbiol. 2011 81(6): 1459-1473. 
PubMed:21815947

Ykelien L Boersma, Tjaard Pijning, Margriet S Bosma, Almer M van der Sloot, Luís F Godinho, Melloney J Dröge, Remko T Winter, Gertie van Pouderoyen, Bauke W Dijkstra, Wim J Quax
Loop grafting of Bacillus subtilis lipase A: inversion of enantioselectivity.
Chem Biol: 2008, 15(8);782-9
[PubMed:18721749] [WorldCat.org] [DOI] (P p)

Melloney J Dröge, Ykelien L Boersma, Gertie van Pouderoyen, Titia E Vrenken, Carsten J Rüggeberg, Manfred T Reetz, Bauke W Dijkstra, Wim J Quax
Directed evolution of Bacillus subtilis lipase A by use of enantiomeric phosphonate inhibitors: crystal structures and phage display selection.
Chembiochem: 2006, 7(1);149-57
[PubMed:16342303] [WorldCat.org] [DOI] (P p)

Helga Westers, Peter G Braun, Lidia Westers, Haike Antelmann, Michael Hecker, Jan D H Jongbloed, Hirofumi Yoshikawa, Teruo Tanaka, Jan Maarten van Dijl, Wim J Quax
Genes involved in SkfA killing factor production protect a Bacillus subtilis lipase against proteolysis.
Appl Environ Microbiol: 2005, 71(4);1899-908
[PubMed:15812018] [WorldCat.org] [DOI] (P p)

Thorsten Eggert, Ulf Brockmeier, Melloney J Dröge, Wim J Quax, Karl-Erich Jaeger
Extracellular lipases from Bacillus subtilis: regulation of gene expression and enzyme activity by amino acid supply and external pH.
FEMS Microbiol Lett: 2003, 225(2);319-24
[PubMed:12951259] [WorldCat.org] [DOI] (P p)

Melloney J Dröge, Carsten J Rüggeberg, Almer M van der Sloot, Judith Schimmel, Dolf Swaving Dijkstra, Raymond M D Verhaert, Manfred T Reetz, Wim J Quax
Binding of phage displayed Bacillus subtilis lipase A to a phosphonate suicide inhibitor.
J Biotechnol: 2003, 101(1);19-28
[PubMed:12523966] [WorldCat.org] [DOI] (P p)

Jan D H Jongbloed, Haike Antelmann, Michael Hecker, Reindert Nijland, Sierd Bron, Ulla Airaksinen, Frens Pries, Wim J Quax, Jan Maarten van Dijl, Peter G Braun
Selective contribution of the twin-arginine translocation pathway to protein secretion in Bacillus subtilis.
J Biol Chem: 2002, 277(46);44068-78
[PubMed:12218047] [WorldCat.org] [DOI] (P p)

T Eggert, G van Pouderoyen, B W Dijkstra, K E Jaeger
Lipolytic enzymes LipA and LipB from Bacillus subtilis differ in regulation of gene expression, biochemical properties, and three-dimensional structure.
FEBS Lett: 2001, 502(3);89-92
[PubMed:11583117] [WorldCat.org] [DOI] (P p)

G van Pouderoyen, T Eggert, K E Jaeger, B W Dijkstra
The crystal structure of Bacillus subtilis lipase: a minimal alpha/beta hydrolase fold enzyme.
J Mol Biol: 2001, 309(1);215-26
[PubMed:11491291] [WorldCat.org] [DOI] (P p)

jetzzt 3

jetzt 4

Zhong Ni, Peng Zhou, Xin Jin, Xian-Fu Lin
Integrating In Silico and In vitro approaches to dissect the stereoselectivity of Bacillus subtilis lipase A toward ketoprofen vinyl ester.
Chem Biol Drug Des: 2011, 78(2);301-8
[PubMed:21477088] [WorldCat.org] [DOI] (I p)

Bo Chen, Zhen Cai, Wei Wu, Yunlong Huang, Juergen Pleiss, Zhanglin Lin
Morphing activity between structurally similar enzymes: from heme-free bromoperoxidase to lipase.
Biochemistry: 2009, 48(48);11496-504
[PubMed:19883129] [WorldCat.org] [DOI] (I p)

Allison V Banse, Arnaud Chastanet, Lilah Rahn-Lee, Errett C Hobbs, Richard Losick
Parallel pathways of repression and antirepression governing the transition to stationary phase in Bacillus subtilis.
Proc Natl Acad Sci U S A: 2008, 105(40);15547-52
[PubMed:18840696] [WorldCat.org] [DOI] (I p)

Eerappa Rajakumara, Priyamvada Acharya, Shoeb Ahmad, Rajan Sankaranaryanan, Nalam M Rao
Structural basis for the remarkable stability of Bacillus subtilis lipase (Lip A) at low pH.
Biochim Biophys Acta: 2008, 1784(2);302-11
[PubMed:18053819] [WorldCat.org] [DOI] (P p)