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Peng, Y. Auxiliary Enzyme. Encyclopedia. Available online: https://encyclopedia.pub/entry/61435 (accessed on 12 November 2026).
Peng Y. Auxiliary Enzyme. Encyclopedia. Available at: https://encyclopedia.pub/entry/61435. Accessed November 12, 2026.
Peng, Yu. "Auxiliary Enzyme" Encyclopedia, https://encyclopedia.pub/entry/61435 (accessed November 12, 2026).
Peng, Y. (2026, October 25). Auxiliary Enzyme. In Encyclopedia. https://encyclopedia.pub/entry/61435
Peng, Yu. "Auxiliary Enzyme." Encyclopedia. Web. 25 October, 2026.

Auxiliary Enzyme

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An auxiliary enzyme is an enzyme added to a coupled assay to convert a product or intermediate of the primary reaction into a measurable signal. The primary enzyme generates the chemical species being followed, while one or more supporting reactions connect its formation to a detectable change [1]. Enzyme-based measurements relate the measured signal to the amount or turnover of a particular metabolite through the stoichiometry of the coupled reactions [2]. In an ADP-linked assay, pyruvate kinase converts ADP and phosphoenolpyruvate into ATP and pyruvate, and lactate dehydrogenase couples pyruvate reduction to NADH oxidation. Other coupled systems use sequential carbohydrate-converting enzymes to connect the target reaction with a spectrophotometric readout [3][4]. Sufficient auxiliary activity allows the signal to track the primary reaction without becoming constrained by the supporting conversion steps.

coupled enzyme assay coupling enzyme reaction kinetics signal generation
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References

  1. Jean-Philippe Goddard; Jean-Louis Reymond; Recent advances in enzyme assays. Trends Biotechnol. 2004, 22, 363-370. [CrossRef]
  2. Wenyun Lu; Xiaoyang Su; Matthias S. Klein; Ian A. Lewis; Oliver Fiehn; Joshua D. Rabinowitz; Metabolite Measurement: Pitfalls to Avoid and Practices to Follow. Annu. Rev. Biochem. 2017, 86, 277-304. [CrossRef]
  3. Jayodita C Sanghvi; Sergi Regot; Silvia Carrasco; Jonathan R Karr; Miriam V Gutschow; Benjamin Bolival; Markus W Covert; Accelerated discovery via a whole-cell model. Nat. Methods 2013, 10, 1192-1195. [CrossRef]
  4. Bradley A. Webb; Farhad Forouhar; Fu-En Szu; Jayaraman Seetharaman; Liang Tong; Diane L. Barber; Structures of human phosphofructokinase-1 and atomic basis of cancer-associated mutations. Nature 2015, 523, 111-114. [CrossRef]
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Subjects: Biochemistry & Molecular Biology
Contributor MDPI registered users' name will be linked to their SciProfiles pages. To register with us, please refer to https://encyclopedia.pub/register : Yu Peng
View Times: 6
Entry Collection: Biosynthesis and Synthetic Biology
Revisions: 2 times (View History)
Update Date: 25 Oct 2026
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