ArticleJournal of protein chemistry1998
A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis.
Article in Journal of protein chemistry, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 47 citations in OpenAlex.
- Moonlighting inMicroorganisms · 2021Review
- Evidence for the Rapid and Divergent Evolution of Mycoplasmas: Structural and Phylogenetic Analysis of Enolases.Frontiers in molecular biosciences · 2021Article
- Effect of ions and inhibitors on the catalytic activity and structural stability ofJournal of biosciences · 2019Article
- Integration of enzymatic data in Bacillus subtilis genome-scale metabolic model improves phenotype predictions and enables in silico design of poly-γ-glutamic acid production strains.Microbial cell factories · 2019Article
- Featured Species-Specific Loops Are Found in the Crystal Structure ofFrontiers in cellular and infection microbiology · 2019Article
- Strain-transcending neutralization of malaria parasite by antibodies against Plasmodium falciparum enolase.Malaria journal · 2018Article
- Biochemical and Biophysical Characterization of the Enolase fromBioMed research international · 2018Article
- An octamer of enolase from Streptococcus suis.Protein & cell · 2012Article
- Metal selectivity determinants in a family of transition metal transporters.The Journal of biological chemistry · 2012Article
- Dissociation of the octameric enolase from S. pyogenes--one interface stabilizes another.PloS one · 2010Article
- Chemical unfolding of enolase from Saccharomyces cerevisiae exhibits a three-state model.The protein journal · 2010Article
- Purification, crystallization and preliminary crystallographic study of the putative enolase MJ0232 from the hyperthermophilic archaeon Methanococcus jannaschii.Acta crystallographica. Section F, Structural biology and crystallization communications · 2008Article
- Purification and properties of gammagamma-enolase from pig brain.Journal of protein chemistry · 1999Article
- A model of the quaternary structure of enolases, based on structural and evolutionary analysis of the octameric enolase from Bacillus subtilis.Journal of protein chemistry · 1998Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Purified enolase from Bacillus subtilis has a native mass of approximately 370 kDa. Since B. subtilis enolase was found to have a subunit mass of 46.58 kDa, the quaternary structure of B. subtilis is octameric. The pl for B. subtilis enolase is 6.1, the pH optimum (pHo) for activity is 8.1-8.2, and the Km for 2-PGA is approximately 0.67 mM. Using the dimeric Calpha structure of yeast dimeric enolase as a guide, these dimers were arranged as a tetramer of dimers to simulate the electron microscopy image processing obtained for the octameric enolase purified from Thermotoga maritima. This arrangement allowed identification of helix J of one dimer (residues 86-96) and the loop between helix L and strand 1 (HL-S1 loop) of another dimer as possible subunit interaction regions. Alignment of available enolase amino acid sequences revealed that in 16 there are two tandem glycines at the C-terminal end of helix L and the HL-S1 loop is truncated by 4-6 residues relative to the yeast polypeptide, two structural features absent in enolases known to be dimers. From these arrangements and alignments it is proposed that the GG tandem at the C-terminal end of helix L and truncation of the HL-S1 loop may play a critical role in octamer formation of enolases. Interestingly, the sequence features associated with dimeric quaternary structure are found in three phylogenetically disparate groups, suggesting that the ancestral enolase was an octamer and that the dimeric structure has arisen independently multiple times through evolutionary history.
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