Hydrogenase

5-amino-1-[4-(trifluoromethyl)phenyl]-1H-pyrazole-4-carbonitrile is a compound used as a molecular structural unit and is considered to be an inhibitor of enzymes such as COX-2, 5-LOX, etc., and possesses a wide range of biochemical and physiological effects including antitumor activity, anti-inflammatory effects and antioxidant activity.

12α-Hydroxysteroid dehydrogenase, an NAD-dependent enzyme expressed in Bacillus sphaericus, actively processes both free and conjugated bile salts. It is utilized to determine the levels of 12α-hydroxy bile acids in serum.

Sorbitol-6-phosphate 2-dehydrogenase, a dehydrogenase enzyme produced by Escherichia coli, catalyzes the interconversion of D-sorbitol 6-phosphate and D-fructose 6-phosphate. The enzyme oxidizes D-sorbitol 6-phosphate at a rate ten times faster than it reduces D-fructose 6-phosphate, playing a role in various cellular processes.

Galactose 1-dehydrogenase, pseudomonas fluorescens, a dehydrogenase found in Pseudomonas fluorescens, facilitates the oxidation of L-arabinose and D-galactose, utilizing NADP+ NAD+ as a cofactor. This enzyme is employed in diagnostic assays to quantify total galactose levels and serves as a biocatalyst in the production of galacturonic acid salts.

Succinate dehydrogenase-IN-4 (Compound 4b) is an inhibitor of succinate dehydrogenase with an IC50 value of 3.38 μM. It exhibits antifungal activity against Physalospora piricola and Colletotrichum orbiculare, with EC50 values of 16.33 μM and 18.06 μM, respectively.

Succinate dehydrogenase-IN-5 (Compound M8) acts as an inhibitor of succinate dehydrogenase. It disrupts energy metabolism and growth in fungi and is effective against Rhizoctonia solani, Sclerotinia sclerotiorum, Botrytis cinerea, and Fusarium graminearum, with an EC50 of less than 0.3 μg mL.

Succinate dehydrogenase-IN-7 (Compound 2f) is a succinate dehydrogenase inhibitor with an IC50 value of 2.51 μM and exhibits bactericidal properties.

Succinate dehydrogenase-IN-6 (Compound E23) is an inhibitor of succinate dehydrogenase (SDH), effectively hindering SDH in Rhizoctonia solani with an IC50 of 11.76 μM. This compound disrupts fungal cell membranes and exhibits broad-spectrum antifungal activity, capable of inhibiting R. solani, V. dahliae, A. solani, and C. gloeosporioides with EC50 values of 0.41, 0.27, 1.15, and 0.27 μg mL, respectively. Furthermore, Succinate dehydrogenase-IN-6 shows no significant toxicity in rice and zebrafish (LC50 > 12.5 μg mL).

Glutamate dehydrogenase NAD(P) (GLDH), a mitochondrial enzyme found in hepatocytes, renal tissue, brain, muscle, and intestinal cells, catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate (α-KG), playing a critical role in the urea cycle [1], and is frequently utilized in biochemical research.

Glucose-6-phosphate dehydrogenase is a rate-controlling enzyme of the pentose phosphate pathway (PPP) that catalyzes the oxidative dehydrogenation of glucose-6-phosphate to produce glucose-6-phosphate and NADPH.It is a sex-linked metabolic enzyme involved in the shunting of hexose monophosphate.

Glucose 1-dehydrogenase, also known as glucose dehydrogenase (FAD) Pseudomonas glucose dehydrogenase, is an enzyme that catalyzes the conversion of glucose and NAD(P) into NAD(P)H and gluconic acid, serving as a cofactor regeneration mechanism [1].

Alcohol dehydrogenase is a zinc-containing enzyme found widely in plants and animals, involved in the detoxification of environmental alcohols.

Glycerol phosphate dehydrogenase catalyzes the conversion of dihydroxyacetone phosphate to α-glycerol phosphate [1] .

Leucine dehydrogenase, purified from Bacillus spheroides, catalyzes the oxidative deamination of L-leucine, L-valine, L-isoleucine, L-norvaline, L-alpha-aminobutyrate, and L-norleucine and the reductive amination of their keto analogues [1].

L-Lactate dehydrogenase (LAD) is an oxidoreductase enzyme in the anaerobic metabolic pathway and the gluconeogenic pathway, and is found in a wide range of tissues in the body.

Malate dehydrogenase catalyzes the mutual conversion of oxaloacetate and malate, and is associated with the oxidation reduction of dinucleotide coenzymes [1] .

D-Lactate dehydrogenase (D-LDH), an oxidoreductase, catalyzes the oxidation of D-lactate to pyruvate leveraging NAD+ or NADP+ as acceptors and acting on the donor CH-OH group. Predominantly found in bacteria and fungi, it is frequently utilized in biochemical research [1].

3α-Hydroxysteroid dehydrogenase (3α-HSD), encoded by the AKR1C4 gene, is responsible for catalyzing the transformation of 3-ketosteroids into 3α-hydroxy compounds. This enzyme significantly contributes to the inactivation of the androgen DHT by converting it into 3α-androstanediol, which exhibits reduced androgen activity. Such conversions are crucial in hirsutism research [1].

Formate dehydrogenase, a widely present enzyme in both prokaryotes and eukaryotes, facilitates the reversible oxidation of formate to carbon dioxide. Based on its metal content, structure, and catalytic approach, it is classified into two groups: non-metallic and metal-containing, frequently utilized in biochemical research [1].

Aldehyde dehydrogenase NAD(P) (ALDH) is an enzyme that facilitates the conversion of aldehydes into their respective carboxylic acids while simultaneously reducing the cofactor NAD(P) to NAD(P)H, making it a key component in biochemical research. This enzyme plays a crucial role in mitigating aldehyde stress by being part of the body's array of enzymatic defenses [1].

Isocitrate dehydrogenase (ICDH), a critical enzyme in the citric acid or tricarboxylic acid cycle, facilitates the oxidative decarboxylation of isocitrate to α-ketoglutarate while reducing NAD(P)+ to NAD(P)H, thus playing pivotal roles in cellular metabolism [1].

3-Hydroxybutyrate dehydrogenase (3-HBDH), a mitochondrial enzyme, plays a crucial role in the metabolism of ketone bodies and butanoate, catalyzing the conversion of (R)-3-hydroxybutanoate into acetoacetate [1]. This enzyme is frequently utilized in biochemical studies due to its involvement in both the synthesis and degradation of key metabolic substances.

Beta-Galactose dehydrogenase catalyzes the conversion of galactose into galactonolactone, simultaneously reducing NAD to fluorescent NADH. This enzyme is useful for the determination of galactose [1].

Glucose dehydrogenase (GDH) is an oxidoreductase enzyme that facilitates the oxidation of β-D-glucose into β-D-glucono-1,5-lactone, while concurrently reducing cofactor NADP+ to NADPH, and to a lesser degree, NAD+ to NADH. It can utilize both NAD+ and NADP+ as cofactors and serves in the regeneration of NADH and NADPH [1] [2].