Difference between revisions of "MurAA"

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(Biological materials)
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* '''Expression vector:'''
 
* '''Expression vector:'''
 
** pRSETA-murAA, Expression of His(6)-MurAA, avalable in [[Ulf Gerth]]'s lab {{PubMed|14763982}}  
 
** pRSETA-murAA, Expression of His(6)-MurAA, avalable in [[Ulf Gerth]]'s lab {{PubMed|14763982}}  
 +
**pGP2597: (IPTG inducible expression, purification in ''E. coli'' with N-terminal Strep-tag, in [[pGP172]]), available in [[Jörg Stülke]]'s lab
 
          
 
          
 
* '''lacZ fusion:'''
 
* '''lacZ fusion:'''

Revision as of 09:26, 14 March 2014

  • Description: UDP-N-acetylglucosamine 1-carboxyvinyltransferase

Gene name murAA
Synonyms murA
Essential yes PubMed
Product UDP-N-acetylglucosamine 1-carboxyvinyltransferase
Function peptidoglycan precursor biosynthesis
Gene expression levels in SubtiExpress: murAA
Metabolic function and regulation of this protein in SubtiPathways:
murAA
MW, pI 46 kDa, 5.45
Gene length, protein length 1308 bp, 436 aa
Immediate neighbours spoIID, ywmB
Sequences Protein DNA DNA_with_flanks
Genetic context
MurAA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
MurAA expression.png



















Categories containing this gene/protein

cell wall synthesis, biosynthesis of cell wall components, essential genes

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU36760

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: Phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine (according to Swiss-Prot)
  • Protein family: MurA subfamily (according to Swiss-Prot)
  • Paralogous protein(s): MurAB

Extended information on the protein

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

Database entries

  • Structure: 3SG1 (from B. anthracis, 79% identity, 94% similarity)
  • KEGG entry: [3]

Additional information

Expression and regulation

  • Sigma factor:
  • Regulation:
  • Regulatory mechanism:
  • Additional information: subject to Clp-dependent proteolysis upon glucose starvation PubMed

Biological materials

  • Mutant:
  • Expression vector:
    • pRSETA-murAA, Expression of His(6)-MurAA, avalable in Ulf Gerth's lab PubMed
    • pGP2597: (IPTG inducible expression, purification in E. coli with N-terminal Strep-tag, in pGP172), available in Jörg Stülke's lab
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Ankur Gautam, Praveen Rishi, Rupinder Tewari
UDP-N-acetylglucosamine enolpyruvyl transferase as a potential target for antibacterial chemotherapy: recent developments.
Appl Microbiol Biotechnol: 2011, 92(2);211-25
[PubMed:21822642] [WorldCat.org] [DOI] (I p)

Original publications

Sean G Jackson, Fuzhong Zhang, Paul Chindemi, Murray S Junop, Paul J Berti
Evidence of kinetic control of ligand binding and staged product release in MurA (enolpyruvyl UDP-GlcNAc synthase)-catalyzed reactions .
Biochemistry: 2009, 48(49);11715-23
[PubMed:19899805] [WorldCat.org] [DOI] (I p)

Jean van Heijenoort
Lipid intermediates in the biosynthesis of bacterial peptidoglycan.
Microbiol Mol Biol Rev: 2007, 71(4);620-35
[PubMed:18063720] [WorldCat.org] [DOI] (P p)

Holger Kock, Ulf Gerth, Michael Hecker
MurAA, catalysing the first committed step in peptidoglycan biosynthesis, is a target of Clp-dependent proteolysis in Bacillus subtilis.
Mol Microbiol: 2004, 51(4);1087-102
[PubMed:14763982] [WorldCat.org] [DOI] (P p)

T Skarzynski, D H Kim, W J Lees, C T Walsh, K Duncan
Stereochemical course of enzymatic enolpyruvyl transfer and catalytic conformation of the active site revealed by the crystal structure of the fluorinated analogue of the reaction tetrahedral intermediate bound to the active site of the C115A mutant of MurA.
Biochemistry: 1998, 37(8);2572-7
[PubMed:9485407] [WorldCat.org] [DOI] (P p)

T Skarzynski, A Mistry, A Wonacott, S E Hutchinson, V A Kelly, K Duncan
Structure of UDP-N-acetylglucosamine enolpyruvyl transferase, an enzyme essential for the synthesis of bacterial peptidoglycan, complexed with substrate UDP-N-acetylglucosamine and the drug fosfomycin.
Structure: 1996, 4(12);1465-74
[PubMed:8994972] [WorldCat.org] [DOI] (P p)