Final answer:
The advantage of protein kinases acting in multiple-enzyme sequences includes the highly coordinated cascade of events that lead to precise control of cellular functions. Phosphorylation by protein kinases can activate proteins, which allows for efficient and specific signaling responses. Multiple allosteric sites also allow for intricate regulation of enzyme activity.
Step-by-step explanation:
The advantage of protein kinases acting in multiple-enzyme sequences is multi-fold. These kinases catalyze protein phosphorylation, a pivotal post-translational modification that plays a critical role in regulating biological activities within a cell. By acting in sequences, protein kinases contribute to a highly coordinated cascade of events, leading to a finely-tuned control over cellular functions.
Protein kinases, which phosphorylate proteins, activate these proteins, thus altering cell activity. This allows for the efficient and specific response to cellular signals or environmental stress, such as aluminum (Al) stress in plants. For instance, phosphorylation by kinases is involved in Al-responsive malate efflux from root tips, which is essential for alleviating Al-induced root inhibition.
Furthermore, kinase sequences can have different allosteric sites allowing for intricate control over enzyme activity. Enzyme X might be regulated by phosphorylation at distinct residues, with each modification having a different outcome on the enzyme's function and thus on cellular processes. Activation and deactivation of enzymes by different kinases, responding to various cellular states, exemplify the high level of control achieved through multiple-enzyme sequences.