BGPT: What are the kinetic parameters of enolase in bacillus going from PEP to 2PG in glycolysis

Explore by Goal

Quick Analysis Plan Copied

Premise correction: Enolase catalyzes 2-phosphoglycerate (2PG) → phosphoenolpyruvate (PEP), not PEP → 2PG . No supplied evidence reports Km, kcat, or Vmax for enolase from any Bacillus species; kinetic parameters for Bacillus enolase are therefore unknown from these records.

Long Analysis Plan

Directionality and Missing Data

The question reverses the reaction: enolase catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate, not PEP → 2PG . Additionally, none of the supplied evidence records measure kinetic parameters (Km, kcat, Vmax) for Bacillus enolase. The closest quantitative binding data come from rabbit, salmon, yeast, and E. coli enolases, where competitive inhibitors TSP and AEP bind with Kd ≈ 10⁻⁵ M and 10⁻⁶ M respectively , and S. mutans enolase activity was monitored via PEP formation at 240 nm . What is missing: direct Km and kcat measurements for Bacillus enolase in either direction. Confidence: high that parameters are absent here; low confidence in any extrapolation from yeast/E. coli data.

Feedback:

Updated: November 03, 2026

Top Data Sources Export MCP

1. γ-Enolase shifts from ubiquitous α-enolase to neuron-specific γ-enolase during SH-SY5Y enrichment into S- and N-type phenotypes, with cathepsin X regulating γ-enolase activity and neuronal differentiation via Trk/MAPK signaling; inhibition of cathepsin X promotes neurite outgrowth and alters γ-enolase dynamics. [2025]

7QualityResults Limitations Context Blindspots Methods Sample Conflict Data

↗ Paper Review ↗ Full Paper

2. This study identifies an immunodominant epitope in citrullinated α-enolase that is specific for rheumatoid arthritis (RA) and demonstrates its cross-reactivity with bacterial enolase, suggesting a potential link between bacterial infection and the autoimmune response in RA. [2008]

8QualityResults Limitations Context Blindspots Methods Sample Conflict

↗ Paper Review ↗ Full Paper

3. The study compares the effects of sodium fluoride and amine fluoride compounds on enolase and ATPase activities in fluoride-sensitive and fluoride-resistant Streptococcus mutans strains, finding that amine fluorides do not inhibit enolase more than NaF, ATPase is inhibited by amine fluorides/chlorides, and the fluoride-resistant strain shows some increased acid-resistance of enolase with no enolase gene differences detected. [2008]

7QualityResults Limitations Context Blindspots Methods Sample Conflict

↗ Paper Review ↗ Full Paper

4. High-resolution crystal structure of Saccharomyces cerevisiae apo-enolase at 2.25 Å reveals a non-parallel TIM-barrel dimer, an active-site sulfate binding region with conformational metal-ion ligands, and detailed structural features informing enolase catalysis and evolution. [1990]

9QualityResults Limitations Context Blindspots Methods Sample Conflict Data

↗ Paper Review ↗ Full Paper

5. The study builds a human brain proteome map to screen for autoantigens in Hashimoto's encephalopathy and identifies K-enolase as a novel autoantigen, with anti‑K‑enolase antibodies detected in some HE patients and correlating with corticosteroid responsiveness, suggesting diagnostic and mechanistic relevance. [2002]

8QualityResults Limitations Methods Sample Conflict Data

↗ Paper Review ↗ Full Paper

Key Insight

The question inverts enolase's catalytic direction — a common framing error since PEP is the product, not substrate; the reverse (PEP → 2PG) would require pyruvate kinase-family chemistry, not enolase.

Keep Exploring

What are the experimentally measured Km and kcat values for Bacillus subtilis enolase in the 2PG-to-PEP direction, and how do they compare across Gram-positive bacteria?

How do divalent metal ion requirements (Mg2+ vs Mn2+) alter enolase kinetic parameters in Bacillus species?

Why did evolution reverse the thermodynamic favorability of the enolase reaction to operate near equilibrium in glycolysis and gluconeogenesis?

Hypothesis Graveyard

Assuming enolase kinetics are universally conserved across bacteria: the 1971 inhibitor study shows binding-site equivalence across rabbit, salmon, yeast, and E. coli, but Bacillus was never tested, so cross-species extrapolation of Kd remains unverified.

Potential Experiments

Purify recombinant Bacillus subtilis eno (BSG_index) enolase, assay initial rates of 2PG → PEP at 240 nm across pH 6–8 and Mg²⁺ titrations, fit Michaelis-Menten to extract Km and kcat, directly filling the missing parameter space.

Science Art

Science Movie

Make a narrated HD Science movie for this answer ($32 per minute)

Discussion

BGPT Bias

I may overweight structural conservation arguments when kinetic data are absent, potentially overstating transferability of yeast/E. coli binding constants to Bacillus.

Stay current without chasing every paper.

Know what changed, what holds up, and what remains uncertain. Every Friday. No ads.

Biochemistry Evidence

Find exact reported results for molecular interactions, pathways, and reaction kinetics.Know what the science actually supports before you trust the answer.

Explore by Goal

Quick Analysis Plan Copied

Long Analysis Plan

Directionality and Missing Data

Top Data Sources Export MCP

2. This study identifies an immunodominant epitope in citrullinated α-enolase that is specific for rheumatoid arthritis (RA) and demonstrates its cross-reactivity with bacterial enolase, suggesting a potential link between bacterial infection and the autoimmune response in RA. [2008]

4. High-resolution crystal structure of Saccharomyces cerevisiae apo-enolase at 2.25 Å reveals a non-parallel TIM-barrel dimer, an active-site sulfate binding region with conformational metal-ion ligands, and detailed structural features informing enolase catalysis and evolution. [1990]

8. This study determines the complete primary amino acid sequence of rabbit muscle enolase, revealing a high degree of sequence identity with other eukaryotic and prokaryotic enolases, particularly showing 94% identity with mammalian muscle enolases. [1990]

12. This study investigates the effects of the G376E and G157D mutations on the stability and function of yeast enolase, providing insights into the structural implications of these mutations as a model for human muscle enolase deficiency. [2007]

Ask a Follow-Up

Key Insight

The question inverts enolase's catalytic direction — a common framing error since PEP is the product, not substrate; the reverse (PEP → 2PG) would require pyruvate kinase-family chemistry, not enolase.

Keep Exploring

What are the experimentally measured Km and kcat values for Bacillus subtilis enolase in the 2PG-to-PEP direction, and how do they compare across Gram-positive bacteria?

How do divalent metal ion requirements (Mg2+ vs Mn2+) alter enolase kinetic parameters in Bacillus species?

Why did evolution reverse the thermodynamic favorability of the enolase reaction to operate near equilibrium in glycolysis and gluconeogenesis?

Hypothesis Graveyard

Assuming enolase kinetics are universally conserved across bacteria: the 1971 inhibitor study shows binding-site equivalence across rabbit, salmon, yeast, and E. coli, but Bacillus was never tested, so cross-species extrapolation of Kd remains unverified.

Potential Experiments

Purify recombinant Bacillus subtilis eno (BSG_index) enolase, assay initial rates of 2PG → PEP at 240 nm across pH 6–8 and Mg²⁺ titrations, fit Michaelis-Menten to extract Km and kcat, directly filling the missing parameter space.

Science Art

Science Movie

Make a narrated HD Science movie for this answer ($32 per minute)

Discussion

BGPT Bias

I may overweight structural conservation arguments when kinetic data are absent, potentially overstating transferability of yeast/E. coli binding constants to Bacillus.

Stay current without chasing every paper.

My BGPT

Trending

Biochemistry Evidence

Find exact reported results for molecular interactions, pathways, and reaction kinetics.Know what the science actually supports before you trust the answer.

Explore by Goal

Quick Analysis Plan Copied

Long Analysis Plan

Directionality and Missing Data

Top Data Sources ExportMCP

2. This study identifies an immunodominant epitope in citrullinated α-enolase that is specific for rheumatoid arthritis (RA) and demonstrates its cross-reactivity with bacterial enolase, suggesting a potential link between bacterial infection and the autoimmune response in RA. [2008]

4. High-resolution crystal structure of Saccharomyces cerevisiae apo-enolase at 2.25 Å reveals a non-parallel TIM-barrel dimer, an active-site sulfate binding region with conformational metal-ion ligands, and detailed structural features informing enolase catalysis and evolution. [1990]

8. This study determines the complete primary amino acid sequence of rabbit muscle enolase, revealing a high degree of sequence identity with other eukaryotic and prokaryotic enolases, particularly showing 94% identity with mammalian muscle enolases. [1990]

12. This study investigates the effects of the G376E and G157D mutations on the stability and function of yeast enolase, providing insights into the structural implications of these mutations as a model for human muscle enolase deficiency. [2007]

Ask a Follow-Up

Key Insight

The question inverts enolase's catalytic direction — a common framing error since PEP is the product, not substrate; the reverse (PEP → 2PG) would require pyruvate kinase-family chemistry, not enolase.

Keep Exploring

What are the experimentally measured Km and kcat values for Bacillus subtilis enolase in the 2PG-to-PEP direction, and how do they compare across Gram-positive bacteria?

How do divalent metal ion requirements (Mg2+ vs Mn2+) alter enolase kinetic parameters in Bacillus species?

Why did evolution reverse the thermodynamic favorability of the enolase reaction to operate near equilibrium in glycolysis and gluconeogenesis?

Hypothesis Graveyard

Assuming enolase kinetics are universally conserved across bacteria: the 1971 inhibitor study shows binding-site equivalence across rabbit, salmon, yeast, and E. coli, but Bacillus was never tested, so cross-species extrapolation of Kd remains unverified.

Potential Experiments

Purify recombinant Bacillus subtilis eno (BSG_index) enolase, assay initial rates of 2PG → PEP at 240 nm across pH 6–8 and Mg²⁺ titrations, fit Michaelis-Menten to extract Km and kcat, directly filling the missing parameter space.

Science Art

Science Movie

Make a narrated HD Science movie for this answer ($32 per minute)

Discussion

BGPT Bias

I may overweight structural conservation arguments when kinetic data are absent, potentially overstating transferability of yeast/E. coli binding constants to Bacillus.

Stay current without chasing every paper.

My BGPT

Trending

Top Data Sources Export MCP