Services

Professional and Cost-Saving Solutions

Services
Online Inquiry

Our Products Cannot Be Used As Medicines Directly For Personal Use.

24 hour
Promise

Welcome! For price inquiries, please feel free to contact us through the form on the left side. We will get back to you as soon as possible.

Enzyme Activity Measurement of Lactate 2-Monooxygenase

Creative Enzymes is a member of the leading companies which provide high-quality service for enzyme activity. Our best assay instrument and extensive experience can support your research in a rapid and accurate way. We are professional in oxidoreductase measurement, including lactate 2-monooxygenase.

Lactate 2-monooxygenase (EC 1.13.12.4, used to be EC 1.1.3.2) belongs to the α-hydroxyacid oxidases flavoproteins group which catalyze the flavin mononucleotide (FMN)-dependent oxidation of their respective substrate. Lactate 2-monooxygenase catalyzes the oxidation of L-lactate using molecular oxygen to generate (S)-lactate, CO2, and H2O. Other common names in use are:

  • lactate oxidative decarboxylase;
  • lactate oxidase;
  • lactic oxygenase;
  • lactate oxygenase;
  • lactic oxidase;
  • L-lactate monooxygenase;
  • lactate monooxygenase;
  • L-lactate-2-monooxygenase

Enzymes in α-hydroxyacid oxidases flavoproteins group use molecular oxygen as the second substrate, the products of other enzymes such as lactate oxidase are pyruvate and H2O2, but whereas the products with lactate monooxygenase are acetate, CO2, and H2O. It is shown that the difference in properties is due largely to the relative stabilities of a common intermediate complex of reduced enzyme and pyruvate. It is observed with lactate monooxygenase that an intermediate with similar spectral characteristics, which identified as a reduced enzyme-pyruvate complex. With the monooxygenase, this complex was very stable, thereby eliminating free reduced enzyme as being involved in turnover. Instead, the reduced enzyme-pyruvate complex was found to react very rapidly with O2, resulting in a ternary complex of oxidized enzyme, pyruvate and H2O2, in which the oxidative decarboxylation of pyruvate occurred, thus obtained acetate, CO2 and H2O.

Lactate 2-monooxygenase existed in Gram-negative soil bacterium and some Mycobacterium. The activity of lactate 2-monooxygenase is found inhibited by anions, including chloride and phosphate. This enzyme participates in pyruvate metabolism. Creative Enzymes provides more targeted approach to efficiently test the enzymatic activity, through spectrophotometric assay.

Creative Enzymes makes every effort aiming at solving the tough questions in your enzyme research. We have the strong capability to formulate suitable assay methods for activity measurement according to your special demands. In the future, Creative Enzymes will continue to be your most reliable partner.

Enzyme Activity Measurement of Lactate 2-Monooxygenase
Figure: The reaction catalyzed by lactate 2-monooxygenase.

Our Products Cannot Be Used As Medicines Directly For Personal Use.