maksualase

Maksualase is a hypothetical enzyme commonly presented in introductory biochemistry texts to illustrate principles of enzyme catalysis. It is not known to correspond to any enzyme found in living systems and is defined for educational purposes to explore how catalytic proteins might operate. In many examples, maksualase acts on a fictional substrate called maksulose, undergoing a standard hydrolytic reaction that splits the substrate into two products.

Mechanism and properties discussed in teaching materials describe maksualase as a serine hydrolase–type enzyme with a catalytic triad often represented by serine, histidine, and aspartate residues. The proposed mechanism involves an acyl-enzyme intermediate formed during the initial acylation step, followed by a deacylation step that releases products. In instructional scenarios, kinetic parameters such as Michaelis–Menten behavior, Km values in the micromolar range, and a pH optimum near neutral are commonly used to illustrate how real enzymes are analyzed, even though maksualase itself is fictional.

Substrates, products, and inhibitors depicted for maksualase in teaching contexts are designed to demonstrate core concepts rather than reflect a real biological system. Examples often include a competitive inhibitor to show how binding affinity affects reaction rates, and simulated data sets used for fitting kinetic models and assessing experimental design.

Origin and status in literature: The maksualase construct originated in educational material as a safe, non-biological tool to teach enzyme kinetics and catalytic principles. It is intended to clarify methodology and problem-solving approaches without referencing any actual protein or organism.