DHDH Antibodies

Structure of DHDH

Myoglobin is a relatively small protein with a molecular weight of approximately 16.7 kDa. This weight may slightly vary between species due to minor differences in amino acid sequence.

DHDH is typically composed of about 300 amino acids and features a typical Rossmann folding structure, forming NAD+ binding domains and substrate binding domains. Its active center contains key tyrosine (Tyr) and lysine (Lys) residues, which are responsible for catalyzing the oxidation of dihydrodiol to catechol. The tertiary structure of this enzyme is presented as an α/β fold, with the β sheet forming the core and surrounded by an α helix, ensuring the efficient binding of coenzyme (NAD+).The catalytic mechanism of DHDH relies on the oxidation of NAD+, and its substrate specificity enables it to play a key role in the metabolism of aromatic hydrocarbons and the degradation of environmental toxins. The DHDH of some bacteria (such as Pseudomonas) has been evolved and optimized to efficiently decompose polycyclic aromatic hydrocarbons (PAHs), thus having significant application value in the field of bioreremediation.

Fig. 1 Conformation simulation comparison diagram of DHDH substrates (androsterone and benzo [a] pyrene dihydrodiol).¹

Key structural properties of DHDH:

• Typical Rossmann folded conformation (α/β alternating structure)
• Conservative NAD+ binding domain (Gly-X-Gly-X-X-Gly mode)
• Catalytic triplet (Tyr - Lys - Ser/Thr) is in charge of the proton transfer
• Hydrophobic substrate binding pocket (adapted to aromatic compounds)

Functions of DHDH

DHDH is a key metabolic enzyme that mainly participates in the degradation and detoxification processes of aromatic compounds, and also plays an important role in various physiological and pathological processes.

The kinetic characteristics of DHDH are manifested as broad-spectrum catalytic ability for a variety of dihydrodiol substrates, but its efficiency is affected by the NAD+/NADH ratio and the substrate structure. In synergy with monooxygenases (such as cytochrome P450), DHDH plays a key role in the balance of carcinogen activation/detoxification.

Applications of DHDH and DHDH Antibody in Literature

1. Smithgall, T. E., R. G. Harvey, and T. M. Penning. "Regio-and stereospecificity of homogeneous 3 alpha-hydroxysteroid-dihydrodiol dehydrogenase for trans-dihydrodiol metabolites of polycyclic aromatic hydrocarbons." Journal of Biological Chemistry 261.14 (1986): 6184-6191. https://doi.org/10.1016/S0021-9258(19)84546-5

Studies have confirmed that dihydrodiol dehydrogenase (DHDH) in rat liver has 3α -hydroxysteroid dehydrogenase activity, which can efficiently oxidize the non-K-region trans dihydrodiol metabolites of polycyclic aromatic hydrocarbons such as benzo [a] pyrene, and shows strict regioselectivity and stereoselectivity preferences, indicating that it plays a key role in the metabolism of polycyclic aromatic hydrocarbon carcinogens.

2. Zhuo, Weibin, et al. "Signature of immune-related metabolic genes predicts the prognosis of hepatocellular carcinoma." Frontiers in Immunology 15 (2024): 1481331. https://doi.org/10.1038/s41467-025-56353-4

This article demonstrates that myoglobin plays a central role in rhabdomyolysis- and crush syndrome-associated acute kidney injury (RM/CS-AKI), and highlights the potential of a high-affinity anti-myoglobin rabbit monoclonal antibody (RabMAb) as an effective emergency treatment that blocks myoglobin-induced kidney toxicity.

3. Huang, Shanzhou, et al. "Genome-wide CRISPR/Cas9 library screening identified that DUSP4 deficiency induces lenvatinib resistance in hepatocellular carcinoma." International Journal of Biological Sciences 18.11 (2022): 4357. https://www.ijbs.com/v18p4357.htm

The article found through CRISPR screening that six genes including DHDH are associated with lenvatinib resistance in liver cancer. Among them, the deletion of DUSP4 promotes resistance by activating the MAPK/ERK pathway, and the combination with MEK inhibitors can reverse the resistance effect.

4. Li, Ding, et al. "A distinct glucose metabolism signature of lung adenocarcinoma with prognostic value." Frontiers in Genetics 13 (2022): 860677. https://doi.org/10.3389/fgene.2022.860677

Based on the TCGA database, this study screened out 10 genes related to glucose metabolism including DHDH and constructed a prognostic model for lung adenocarcinoma. The high-risk group had a poor survival rate and a low response rate to immunotherapy. This model provides a new strategy for individualized treatment targeting glucose metabolism.

5. Vogel, Klaus, et al. "Rat liver cytoplasmic dihydrodiol dehydrogenase. Purification to apparent homogeneity and properties." Journal of Biological Chemistry 255.20 (1980): 9621-9625. https://doi.org/10.1016/S0021-9258(18)43437-0

In this study, dihydrodiol dehydrogenase (DHDH) was successfully purified from rat livers. This enzyme can specifically catalyze the conversion of phenyldihydrodiol to catechol, with a molecular weight of 35kDa and an optimal pH of 6.2. It has a high affinity for NADP+ (Km=7.7μM) and a narrow substrate specificity, and may be involved in the metabolic process of polycyclic aromatic hydrocarbon carcinogens.

Creative Biolabs: DHDH Antibodies for Research

Creative Biolabs specializes in the production of high-quality DHDH antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

• Custom DHDH Antibody Development: Tailor-made solutions to meet specific research requirements.
• Bulk Production: Large-scale antibody manufacturing for industry partners.
• Technical Support: Expert consultation for protocol optimization and troubleshooting.
• Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our DHDH antibodies, custom preparations, or technical support, please contact us.