Difference between revisions of "XynA"

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{{SubtiWiki category|[[utilization of specific carbon sources]]}}
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=The gene=
 
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{{SubtiWiki category|[[utilization of specific carbon sources]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 20:17, 8 December 2010

  • Description: endo-1,4-beta-xylanase

Gene name xynA
Synonyms
Essential no
Product endo-1,4-beta-xylanase
Function xylan degradation
Metabolic function and regulation of this protein in SubtiPathways:
Sugar catabolism
MW, pI 23 kDa, 9.644
Gene length, protein length 639 bp, 213 aa
Immediate neighbours pps, yobD
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
XynA context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

utilization of specific carbon sources

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU18840

Phenotypes of a mutant

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans (according to Swiss-Prot)
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization: extracellular (signal peptide) PubMed

Database entries

  • KEGG entry: [3]

Additional information

Expression and regulation

  • Regulation:
    • constitutively expressed PubMed
  • Regulatory mechanism:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Massimiliano Marvasi, Pieter T Visscher, Lilliam Casillas Martinez
Exopolymeric substances (EPS) from Bacillus subtilis: polymers and genes encoding their synthesis.
FEMS Microbiol Lett: 2010, 313(1);1-9
[PubMed:20735481] [WorldCat.org] [DOI] (I p)

Original publications

Louise E Rasmussen, Jens F Sørensen, Anne S Meyer
Kinetics and substrate selectivity of a Triticum aestivum xylanase inhibitor (TAXI) resistant D11F/R122D variant of Bacillus subtilis XynA xylanase.
J Biotechnol: 2010, 146(4);207-14
[PubMed:20188130] [WorldCat.org] [DOI] (I p)

Annick Pollet, Stijn Lagaert, Elena Eneyskaya, Anna Kulminskaya, Jan A Delcour, Christophe M Courtin
Mutagenesis and subsite mapping underpin the importance for substrate specificity of the aglycon subsites of glycoside hydrolase family 11 xylanases.
Biochim Biophys Acta: 2010, 1804(4);977-85
[PubMed:20096384] [WorldCat.org] [DOI] (P p)

Louise E Rasmussen, Anne S Meyer
Size exclusion chromatography for the quantitative profiling of the enzyme-catalyzed hydrolysis of Xylo-oligosaccharides.
J Agric Food Chem: 2010, 58(2);762-9
[PubMed:19994888] [WorldCat.org] [DOI] (I p)

Tim Beliën, Iris J Joye, Jan A Delcour, Christophe M Courtin
Computational design-based molecular engineering of the glycosyl hydrolase family 11 B. subtilis XynA endoxylanase improves its acid stability.
Protein Eng Des Sel: 2009, 22(10);587-96
[PubMed:19531602] [WorldCat.org] [DOI] (I p)

Annick Pollet, Elien Vandermarliere, Jeroen Lammertyn, Sergei V Strelkov, Jan A Delcour, Christophe M Courtin
Crystallographic and activity-based evidence for thumb flexibility and its relevance in glycoside hydrolase family 11 xylanases.
Proteins: 2009, 77(2);395-403
[PubMed:19422059] [WorldCat.org] [DOI] (I p)

Birgit Voigt, Haike Antelmann, Dirk Albrecht, Armin Ehrenreich, Karl-Heinz Maurer, Stefan Evers, Gerhard Gottschalk, Jan Maarten van Dijl, Thomas Schweder, Michael Hecker
Cell physiology and protein secretion of Bacillus licheniformis compared to Bacillus subtilis.
J Mol Microbiol Biotechnol: 2009, 16(1-2);53-68
[PubMed:18957862] [WorldCat.org] [DOI] (I p)

C Lindner, J Stülke, M Hecker
Regulation of xylanolytic enzymes in Bacillus subtilis.
Microbiology (Reading): 1994, 140 ( Pt 4);753-7
[PubMed:8012596] [WorldCat.org] [DOI] (P p)