Enzyme Activity Measurement for Oxidoreductases Acting on Nitrogen and Sulfur Using Spectrophotometric Assays

Creative Enzymes offers highly specialized enzyme activity measurement services for oxidoreductases that act on nitrogen and sulfur atoms. Leveraging cutting-edge spectrophotometric techniques and the expertise of our experienced enzymologists, we deliver precise, reproducible, and tailored assay solutions. Our advanced methods have been specifically optimized to overcome the inherent challenges of nitrogen- and sulfur-containing substrates, providing unmatched accuracy and reliability in enzyme activity determination.

Scientific Background

Oxidoreductases acting on nitrogen and sulfur groups are critical biocatalysts in a wide range of metabolic and industrial processes. These enzymes, classified as EC 1.4, EC 1.5, EC 1.6, EC 1.7, and EC 1.8, encompass hundreds of members that play vital roles in redox biology, environmental cycles, and pharmaceutical pathways.

Unlike other oxidoreductases, nitrogen- and sulfur-acting enzymes catalyze reactions involving substrates with strong UV/visible absorbance. This property complicates conventional spectrophotometric assays, particularly those based on NAD(P)H cofactors, as interference can obscure detection. Creative Enzymes has developed proprietary assay protocols that carefully control reaction conditions and substrate interference, ensuring the accurate quantification of enzyme activity.

These enzymes are increasingly significant for drug discovery, environmental biotechnology, agricultural innovation, and personal care product development, making robust assay services essential for both academic research and industrial applications.

Comprehensive Service Offerings

Service Workflow

Service Details

• Measurement of enzyme activity across all subclasses of EC 1.4–1.8.
• Options for kinetic characterization, substrate specificity testing, and inhibitor screening.
• High-throughput capacity for large-scale screening projects.
• Custom-tailored assays to meet unique project requirements.

Enzyme Classes Covered

	EC 1.4 Acting on the CH-NH2 group of donors EC 1.4.1 With NAD or NADP as acceptor EC 1.4.2 With a cytochrome as acceptor EC 1.4.3 With oxygen as acceptor EC 1.4.4 With a disulfide as acceptor EC 1.4.5 With an iron-sulfur flavoprotein as acceptor EC 1.4.7 With an iron-sulfur protein as acceptor EC 1.4.9 With TTQ acceptors EC 1.4.98 With tryptophan tryptophylquinone acceptors EC 1.4.99 With other acceptors
	EC 1.5 Acting on the CH-NH group of donors EC 1.5.1 With NAD or NADP as acceptor EC 1.5.3 With oxygen as acceptor EC 1.5.4 With a disulfide as acceptor EC 1.5.5 With a quinone or similar compound as acceptor EC 1.5.7 With an iron-sulfur protein as acceptor EC 1.5.8 With a flavin as acceptor EC 1.5.99 With other acceptors
	EC 1.6 Acting on NADH or NADPH EC 1.6.1 With NAD or NADP as acceptor EC 1.6.2 With a heme protein as acceptor EC 1.6.3 With oxygen as acceptor EC 1.6.4 With a disulfide as acceptor EC 1.6.5 With a quinone or similar compound as acceptor EC 1.6.6 With a nitrogenous group as acceptor EC 1.6.7 With an iron-sulfur protein as acceptor EC 1.6.8 With a flavin as acceptor EC 1.6.99 With other acceptors
	EC 1.7 Acting on other nitrogenous compounds as donors EC 1.7.1 With NAD+ or NADP+ as acceptor EC 1.7.2 With a cytochrome as acceptor EC 1.7.3 With oxygen as acceptor EC 1.7.5 With miscellaneous acceptora EC 1.7.6 With hydrogen as acceptor EC 1.7.7 With an iron-sulfur protein as acceptor EC 1.7.99 With other acceptors
	EC 1.8 Acting on a sulfur group of donors EC 1.8.1 With NAD or NADP as acceptor EC 1.8.2 With a cytochrome as acceptor EC 1.8.3 With oxygen as acceptor EC 1.8.4 With a disulfide as acceptor EC 1.8.5 With a quinone or similar compound as acceptor EC 1.8.6 With a nitrogenous group as acceptor EC 1.8.7 With an iron-sulfur protein as acceptor EC 1.8.98 With other, known, acceptors EC 1.8.99 With other acceptors

Each subclass includes a wide variety of acceptors (NAD/NADP, cytochrome, oxygen, disulfide, flavins, quinones, iron-sulfur proteins, etc.), all of which we are equipped to analyze with high sensitivity and precision.

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Why Choose Creative Enzymes

Representative Case Studies

FAQs

• Q: Why are specialized methods required for nitrogen- and sulfur-based oxidoreductases?

  A: Because these substrates often have strong UV/visible absorbance, they interfere with standard NAD(P)H-based spectrophotometric assays. Our proprietary methods overcome this challenge, ensuring accurate and reliable results.

• Q: Can you customize assays for novel or rare oxidoreductases?

  A: Yes. We specialize in developing tailored protocols for both well-characterized and novel enzymes, ensuring optimal assay conditions for your unique research needs.

• Q: Do you offer kinetic characterization in addition to activity measurement?

  A: Absolutely. We provide full kinetic profiling, including determination of K_m, V_max, turnover numbers, and inhibitor effects.

• Q: What industries can benefit from your services?

  A: Our assays are widely applied in pharmaceutical R&D, agriculture, environmental biotechnology, personal care, and industrial biocatalysis.

• Q: How fast can I expect results?

  A: Turnaround time depends on project complexity, but most assays are completed within 2–4 weeks, with expedited options available for urgent projects.