Target intelligence / Profile preview

Sulfhydryl-containing enzymes

Molecular classification
Enzyme (the group includes oxidoreductases, proteases, kinases, acyltransferases, deubiquitinases, and others)
01

Overview

Sulfhydryl-containing enzymes are a heterogeneous group of proteins defined by the presence of free or reactive thiol (–SH) groups, primarily from cysteine residues. These enzymes are functionally diverse and play crucial roles in catalysis, redox balance, and regulation of cellular processes. Reactive sulfhydryl groups enable catalytic activity, mediate redox reactions, contribute to protein folding via disulfide bonds, and serve as sensors for oxidative or electrophilic stress. Given the ubiquity and importance of cysteine residues, these enzymes are implicated in numerous biological pathways and diseases. However, "sulfhydryl-containing enzymes" is a non-specific, category-level descriptor rather than a precise molecular target.

Other names
Thiol-containing enzymesSH-containing enzymesSulfhydryl enzymes
02

Mechanism of action

Covalent modification of active site cysteines (inhibition or modulation of enzyme function); Oxidation/reduction of sulfhydryl groups (regulation of activity); Formation of disulfide bonds (altering enzyme structure and function)

03

Biological functions

Redox regulationProtein folding (e.g., disulfide bond formation)Catalysis (nucleophilic reactions)Regulation of cell signaling through reactive cysteinesMaintenance of cellular redox homeostasis
04

Disease associations

Oxidative stress-related diseasesCancer (redox-sensitive enzymes)Neurodegenerative disease (due to dysregulated redox biology)Inflammation (redox imbalance)Other (broad relevance given functional diversity of cysteine-containing enzymes)
05

Safety considerations

Lack of specificity: Many thiol-modifying agents indiscriminately react with sulfhydryl groups, leading to potential off-target effectsToxicity: Modulating cellular redox environments can disrupt critical physiological processes and lead to cytotoxicityReactivity: Some compounds (e.g., mercury, electrophiles) can irreversibly damage proteins by modifying sulfhydryl groups
06

Interacting drugs

There is no single set of drugs; many covalent inhibitors and redox-active small molecules can broadly target enzymes with reactive cysteines (e.g., alkylating agents, selenium-based drugs, thiol-reactive probes)
07

Biomarkers

No universal biomarker; cysteine oxidation state or protein adducts may be used in specific contexts for redox-regulated enzymes

Beyond the preview

Go deeper on Sulfhydryl-containing enzymes.

Explore the evidence, development activity, and competitive landscape with Gosset’s full data platform.

Drug pipeline

Full profile access

Explore the programs pursuing this target and their development progress.

  • Drug candidates
  • Developers
  • Development stage

Clinical trials

Full profile access

Follow the clinical studies evaluating therapies directed at this target.

  • Trial design
  • Status
  • Readouts

Competitive landscape

Full profile access

Compare approaches across drug candidates, modalities, and indications.

  • Programs
  • Modalities
  • Indications

Literature & evidence

Full profile access

Investigate the research and source evidence behind target biology and development.

  • Publications
  • Sources
  • Analysis

Patents

Full profile access

Explore patent activity around therapies and technologies addressing this target.

  • Patents
  • Assignees
  • Technologies

Research & analysis

Full profile access

Connect target biology, drug development, and emerging evidence in your research.

  • Biology
  • Development news
  • Analysis

Bring the full picture into focus.

See how Gosset can support your research on Sulfhydryl-containing enzymes.

Explore the full profile

Gosset Free

Get started with Gosset.

Enter your work email and we’ll be in touch with next steps.

Work email preferred.

Book a call