Difference between revisions of "Eno"
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+ | [[Category:Protein-coding genes]] |
Revision as of 12:43, 21 July 2009
- Description: enolase, glycolytic/ gluconeogenic enzyme
Gene name | eno |
Synonyms | |
Essential | yes |
Product | enolase |
Function | enzyme in glycolysis/ gluconeogenesis |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 46,4 kDa, 4.49 |
Gene length, protein length | 1290 bp, 430 amino acids |
Immediate neighbours | pgm, yvgK |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU33900
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: 2-phospho-D-glycerate = phosphoenolpyruvate + H2O (according to Swiss-Prot) 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
- Protein family: enolase family (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information: Reversible Michaelis-Menten PubMed
- Domains:
- substrate binding domain (366–369)
- Cofactor(s): Mg2+
- Effectors of protein activity:
- Inhibited by EDTA PubMed
Database entries
- Structure: 3ES8 (from Oceanobacillus iheyensis, complex with Mg(2+) and malate)
- UniProt: P37869
- KEGG entry: [3]
- E.C. number: 4.2.1.11
Additional information
There are indications that this enzyme is an octamer PubMed
Expression and regulation
- Sigma factor: SigA
- Regulation: expression activated by glucose (3.3 fold) PubMed
- Additional information:
Biological materials
- Mutant: GP698 (cat), available in Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion: pHT315-yfp-eno, available in Mijakovic lab
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Stülke lab
Labs working on this gene/protein
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References