Date published: 2025-10-17

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BPGM Activators

BPGM activators are chemical agents that promote the enzymatic activity of bisphosphoglycerate mutase (BPGM), a key regulatory enzyme in erythrocytes that catalyzes the conversion of 1,3-bisphosphoglycerate (1,3-BPG) to 2,3-bisphosphoglycerate (2,3-BPG). The generation of 2,3-BPG is a crucial step in the regulation of hemoglobin's oxygen-binding affinity, which in turn influences oxygen release to tissues. Activators of BPGM can enhance the enzyme's activity, leading to increased production of 2,3-BPG.

Direct activators of BPGM might bind to the enzyme and induce a conformational change that increases its catalytic efficiency, either by facilitating the binding of the substrate to the active site or by stabilizing the transition state of the reaction. These compounds often interact with regions of the enzyme that are distinct from the substrate binding site, allosterically modifying the enzyme's structure to enhance its natural activity. Indirect activators may work by upregulating the expression of the BPGM gene, thereby increasing the amount of enzyme produced within the cell. Alternatively, they might prolong the half-life of the BPGM protein by inhibiting its degradation pathways or by stabilizing its structure through post-translational modifications. Indirect activators could also influence other cellular factors that interact with BPGM, enhancing its activity without directly binding to the enzyme itself.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

D-Fructose 1,6-bisphosphate sodium salt

488-69-7sc-484714
50 g
$298.00
(0)

Fructose 1,6-bisphosphate is an intermediate in the glycolytic pathway. It can increase the quantity of 1,3-bisphosphoglycerate, the substrate for BPGM, thus potentially enhancing its activity.

D(+)Glucose, Anhydrous

50-99-7sc-211203
sc-211203B
sc-211203A
250 g
5 kg
1 kg
$37.00
$194.00
$64.00
5
(1)

Glucose initiates the glycolytic pathway, leading to the production of 1,3-bisphosphoglycerate. The increase in 1,3-bisphosphoglycerate provides more substrate for BPGM, potentially enhancing its activity.

Sodium Fluoride

7681-49-4sc-24988A
sc-24988
sc-24988B
5 g
100 g
500 g
$39.00
$45.00
$98.00
26
(4)

Sodium Fluoride inhibits enolase in the glycolytic pathway, potentially increasing the concentration of 2-phosphoglycerate, the substrate for BPGM, and thus enhancing its activity.

Pyruvic acid

127-17-3sc-208191
sc-208191A
25 g
100 g
$40.00
$94.00
(0)

Pyruvate is the end product of glycolysis. Increasing pyruvate can drive the glycolytic pathway, potentially increasing the amount of 1,3-bisphosphoglycerate, the substrate for BPGM, and enhancing its activity.

NAD+, Free Acid

53-84-9sc-208084B
sc-208084
sc-208084A
sc-208084C
sc-208084D
sc-208084E
sc-208084F
1 g
5 g
10 g
25 g
100 g
1 kg
5 kg
$56.00
$186.00
$296.00
$655.00
$2550.00
$3500.00
$10500.00
4
(2)

NAD+ is involved in the glycolytic pathway, and its presence can stimulate the production of 1,3-bisphosphoglycerate, the substrate for BPGM, potentially enhancing its activity.

Adenosine 5′-Triphosphate, disodium salt

987-65-5sc-202040
sc-202040A
1 g
5 g
$38.00
$74.00
9
(1)

ATP is used in the first step of the glycolytic pathway, which leads to the production of 1,3-bisphosphoglycerate. More ATP could potentially enhance the activity of BPGM by providing more substrate.

Citric Acid, Anhydrous

77-92-9sc-211113
sc-211113A
sc-211113B
sc-211113C
sc-211113D
500 g
1 kg
5 kg
10 kg
25 kg
$49.00
$108.00
$142.00
$243.00
$586.00
1
(2)

Citrate inhibits phosphofructokinase, a regulatory enzyme in glycolysis, potentially increasing the availability of 1,3-bisphosphoglycerate, BPGM's substrate, and thus enhancing its activity.

D-Galactose

59-23-4sc-202564
100 g
$224.00
4
(1)

Galactose is converted into glucose-1-phosphate, which can enter glycolysis, potentially increasing the availability of 1,3-bisphosphoglycerate, the substrate for BPGM, and thus enhancing its activity.

Lactic acid

50-21-5sc-215227
sc-215227A
100 ml
500 ml
$100.00
$175.00
1
(0)

Lactate can be converted back into pyruvate, driving the glycolytic pathway forward, potentially increasing the availability of 1,3-bisphosphoglycerate, the substrate for BPGM, and thus enhancing its activity.