Chemical activators of CKMT1B play a pivotal role in modulating its enzymatic function. Creatine, a key player in muscle energy metabolism, directly enhances the activity of CKMT1B by supplying the phosphate group necessary for the conversion of adenosine diphosphate (ADP) to adenosine triphosphate (ATP), a critical process in energy transfer. Similarly, phosphocreatine serves as a phosphate donor in the reaction catalyzed by CKMT1B, further increasing its activity by providing the substrate for the phosphorylation of ADP. The presence of magnesium chloride is also essential as magnesium ions form a complex with ATP, which is a prerequisite for the phosphoryl transfer reaction facilitated by CKMT1B. Another substance, guanidinoacetate, becomes methylated in the presence of CKMT1B, forming creatine and, in doing so, indirectly augments the enzyme's function by increasing the availability of its substrate.
Additional compounds, such as uridine diphosphate, can broaden the substrate scope for CKMT1B, enhancing the enzyme's activity by offering alternative phosphate acceptors. Dithiothreitol (DTT) and beta-mercaptoethanol contribute to the activation of CKMT1B by preserving the reduced state of cysteine residues within the enzyme, protecting it from oxidative inactivation and maintaining its functional conformation. Iodoacetamide, under certain conditions, can also activate CKMT1B, presumably by blocking oxidative inactivation through alkylation of cysteine residues. Moreover, calcium chloride and zinc chloride can induce structural changes in CKMT1B that favor enzymatic activity, either by improving substrate alignment at the active site or by directly participating in the catalysis. Lastly, sodium fluoride can stabilize the structure of CKMT1B or modify its conformation to enhance the enzyme's catalytic efficiency, thus contributing to the overall activation of the enzyme. Each of these chemicals, through various mechanisms, ensures that CKMT1B operates at an optimal level, maintaining the enzyme's crucial role in cellular energy homeostasis.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Creatine, anhydrous | 57-00-1 | sc-214774 sc-214774A | 10 mg 50 g | $27.00 $77.00 | 2 | |
Creatine provides the phosphate group that CKMT1B transfers to ADP to regenerate ATP, directly increasing CKMT1B's enzymatic activity in the phosphocreatine pathway. | ||||||
Magnesium chloride | 7786-30-3 | sc-255260C sc-255260B sc-255260 sc-255260A | 10 g 25 g 100 g 500 g | $27.00 $34.00 $47.00 $123.00 | 2 | |
Magnesium acts as a cofactor that is required for the proper functioning of CKMT1B as it forms a complex with ATP, which is necessary for the phosphoryl transfer reaction catalyzed by CKMT1B. | ||||||
Adenosine-5′-Diphosphate, free acid | 58-64-0 | sc-291846 sc-291846A sc-291846B sc-291846C sc-291846D sc-291846E | 100 mg 500 mg 1 g 10 g 100 g 500 g | $77.00 $180.00 $312.00 $924.00 $4596.00 $9186.00 | 1 | |
As a substrate for CKMT1B, ADP is phosphorylated to ATP in the presence of phosphocreatine, directly increasing the enzymatic activity of CKMT1B. | ||||||
Uridine 5′-diphosphate sodium salt | 21931-53-3 | sc-222401 sc-222401A | 25 mg 100 mg | $37.00 $77.00 | ||
Uridine diphosphate can serve as an alternative phosphate acceptor for CKMT1B, its presence can enhance the activity of CKMT1B by providing more substrate variety for the transfer of phosphate groups. | ||||||
Guanidinoacetic Acid | 352-97-6 | sc-211571 sc-211571A sc-211571B | 25 mg 1 g 5 g | $166.00 $217.00 $273.00 | ||
Guanidinoacetate is a substrate for the creatine kinase reaction, and in the presence of CKMT1B, it can be methylated to form creatine, thereby indirectly increasing the activity of CKMT1B. | ||||||
α-Iodoacetamide | 144-48-9 | sc-203320 | 25 g | $250.00 | 1 | |
Iodoacetamide alkylates cysteine residues, and while often used as an inhibitor, specific conditions can lead to activation of certain enzymes. For CKMT1B, it could enhance activity if it prevents oxidative inactivation. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $65.00 $262.00 | 1 | |
Calcium ions can bind to and alter the conformation of CKMT1B, potentially increasing its enzymatic activity by inducing a more favorable alignment of the active site for substrate interaction. | ||||||
Sodium Fluoride | 7681-49-4 | sc-24988A sc-24988 sc-24988B | 5 g 100 g 500 g | $39.00 $45.00 $98.00 | 26 | |
Sodium fluoride can act as an allosteric activator for some enzymes. For CKMT1B, it can enhance activity by stabilizing the enzyme structure or altering its conformation to favor the enzymatic reaction. | ||||||
β-Mercaptoethanol | 60-24-2 | sc-202966A sc-202966 | 100 ml 250 ml | $88.00 $118.00 | 10 | |
Beta-mercaptoethanol, like DTT, maintains cysteine residues in a reduced state and can enhance the enzymatic activity of CKMT1B by preventing oxidative inactivation, maintaining the enzyme's functional conformation. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc can act as a cofactor for many enzymes and may increase the activity of CKMT1B by facilitating proper enzyme conformation or by participating directly in the catalytic activity of the enzyme. | ||||||