Date published: 2026-4-1

1-800-457-3801

SCBT Portrait Logo
Seach Input

IDH3B Activators

IDH3B Activators are chemical compounds that enhance the activity of IDH3B through various biochemical mechanisms. The primary substrate of IDH3B, Isocitrate, is fundamental for its activity; an increase in isocitrate concentration directly leads to enhanced IDH3B activity by providing more substrate for the catalysis. Similarly, NAD+ is vital as it acts as an electron acceptor in the reaction catalyzed by IDH3B, thus a higher availability of NAD+ can boost the enzyme's activity. The presence of Calcium ions is another level of regulation; they serve as allosteric activators, increasing the enzyme's affinity for isocitrate and thereby its functional activity. Moreover, ADP, as an allosteric activator, signals the cellular need for more ATP, thus promoting IDH3B's role in ATP production. Magnesium ions provide structural stability to IDH3B, ensuring optimal enzyme conformation for catalytic action, while DTT preserves the enzyme's reduced state, preventing oxidative inactivation and sustaining its activity.

On the other hand, compounds like Biotin and Thiamine pyrophosphate (TPP) do not directly activate IDH3B but are crucial for maintaining the enzyme's structural integrity, thus indirectly supporting its enzymatic function. Coenzyme A and Succinyl-CoA play roles in the broader context of the TCA cycle, with Coenzyme A involved in the production of substrates that IDH3B converts, and Succinyl-CoA providing a feedback mechanism that can enhance IDH3B activity to regulate the cycle's efficiency. Citric acid, as an upstream molecule in the TCA cycle, could influence IDH3B activity through substrate availability and TCA cycle flux maintenance. Lastly, Alpha-ketoglutarate, the product of the IDH3B-catalyzed reaction, in its levels can signal the need to adjust the enzyme's activity, fine-tuning the energy metabolism of the cell to its needs.

SEE ALSO...

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

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
$57.00
$191.00
$302.00
$450.00
$1800.00
$3570.00
$10710.00
4
(2)

NAD+ serves as a coenzyme for IDH3B, facilitating the oxidative decarboxylation of isocitrate to alpha-ketoglutarate.

Calcium

7440-70-2sc-252536
5 g
$209.00
(0)

Calcium ions can allosterically activate IDH3B, thus increasing its catalytic efficiency in the TCA cycle.

Adenosine-5′-Diphosphate, free acid

58-64-0sc-291846
sc-291846A
sc-291846B
sc-291846C
sc-291846D
sc-291846E
100 mg
500 mg
1 g
10 g
100 g
500 g
$79.00
$184.00
$348.00
$942.00
$4688.00
$9370.00
1
(0)

ADP acts as an allosteric activator of IDH3B, promoting its activity under conditions where energy production is needed.

D-(+)-Biotin

58-85-5sc-204706
sc-204706A
sc-204706B
1 g
5 g
25 g
$41.00
$107.00
$333.00
1
(4)

Biotin can support the structural integrity of IDH3B as a cofactor, indirectly enhancing its enzymatic activity.

Thiamine pyrophosphate

154-87-0sc-215966
sc-215966A
sc-215966B
sc-215966C
sc-215966D
1 g
5 g
25 g
100 g
1 kg
$33.00
$97.00
$290.00
$1149.00
$6024.00
1
(1)

TPP can stabilize the conformation of IDH3B for its activity in the TCA cycle.

Coenzyme A

85-61-0 anhydroussc-211123
sc-211123A
sc-211123B
sc-211123C
10 mg
25 mg
100 mg
250 mg
$83.00
$135.00
$418.00
$801.00
1
(1)

CoA can indirectly affect IDH3B activity by modulating substrate availability in the TCA cycle.

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
$50.00
$110.00
$145.00
$248.00
$598.00
1
(2)

Citric acid can modulate TCA cycle intermediates, indirectly enhancing IDH3B activity to maintain cycle flux.

α-Ketoglutaric Acid

328-50-7sc-208504
sc-208504A
sc-208504B
sc-208504C
sc-208504D
sc-208504E
sc-208504F
25 g
100 g
250 g
500 g
1 kg
5 kg
16 kg
$33.00
$43.00
$63.00
$110.00
$188.00
$738.00
$2091.00
2
(1)

Alpha-ketoglutarate levels can regulate TCA cycle enzyme activity, including IDH3B, to sustain metabolic homeostasis.