Soluble quinoprotein glucose dehydrogenase

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Soluble quinoprotein glucose dehydrogenase
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EC no. 1.1.99.35
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Soluble quinoprotein glucose dehydrogenase (EC 1.1.99.35, soluble glucose dehydrogenase, sGDH, glucose dehydrogenase (PQQ-dependent)) is an enzyme with systematic name D-glucose:acceptor oxidoreductase. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

D-glucose + acceptor D-glucono-1,5-lactone + reduced acceptor

This soluble periplasmic enzyme contains PQQ as prosthetic group, and is bound to a calcium ion. Electron acceptor is not known.

Related Research Articles

<span class="mw-page-title-main">Pyrroloquinoline quinone</span> Chemical compound

Pyrroloquinoline quinone (PQQ), also called methoxatin, is a redox cofactor and antioxidant. Produced by bacteria, it is found in soil and foods such as kiwifruit, as well as human breast milk. Enzymes using PQQ as a redox cofactor are called quinoproteins and play a variety of redox roles. Quinoprotein glucose dehydrogenase is used as a glucose sensor in bacteria. PQQ stimulates growth in bacteria. Eukaryote targets, including mammalian lactate dehydrogenase, are of more interest to health. It is suggested that PQQ taken as a dietary supplement could promote mitochondrial biogenesis via this pathway as well as PGC-1α.

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<span class="mw-page-title-main">Formate dehydrogenase</span>

Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.17.1.9) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1). This family of enzymes has attracted attention as inspiration or guidance on methods for the carbon dioxide fixation, relevant to global warming.

In enzymology, a glucose 1-dehydrogenase (NADP+) (EC 1.1.1.119) is an enzyme that catalyzes the chemical reaction

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In enzymology, a choline dehydrogenase is an enzyme that catalyzes the chemical reaction

In enzymology, a gluconate 2-dehydrogenase (acceptor) is an enzyme that catalyzes the chemical reaction

In enzymology, a glycerol dehydrogenase (acceptor) (EC 1.1.99.22) is an enzyme that catalyzes the chemical reaction

In enzymology, a quinoprotein glucose dehydrogenase is an enzyme that catalyzes the chemical reaction

In enzymology, an aldehyde dehydrogenase (NADP+) (EC 1.2.1.4) is an enzyme that catalyzes the chemical reaction

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<span class="mw-page-title-main">Amine oxidase (copper-containing)</span>

Amine oxidase (copper-containing) (AOC) (EC 1.4.3.21 and EC 1.4.3.22; formerly EC 1.4.3.6) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:

<span class="mw-page-title-main">Methanol dehydrogenase (cytochrome c)</span>

Methanol dehydrogenase (cytochrome c) (EC 1.1.2.7, methanol dehydrogenase, MDH) is an enzyme with systematic name methanol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol dehydrogenase (cytochrome c) (EC 1.1.2.8, type I quinoprotein alcohol dehydrogenase, quinoprotein ethanol dehydrogenase) is an enzyme with systematic name alcohol:cytochrome c oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol dehydrogenase (quinone) (EC 1.1.5.5, type III ADH, membrane associated quinohaemoprotein alcohol dehydrogenase) is an enzyme with systematic name alcohol:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

Cyclic alcohol dehydrogenase (quinone) (EC 1.1.5.7, cyclic alcohol dehydrogenase, MCAD) is an enzyme with systematic name cyclic alcohol:quinone oxidoreductase. This enzyme catalyses the following chemical reaction

Quinate dehydrogenase (quinone) (EC 1.1.5.8, NAD(P)+-independent quinate dehydrogenase, quinate:pyrroloquinoline-quinone 5-oxidoreductase) is an enzyme with systematic name quinate:quinol 3-oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol dehydrogenase (azurin) (EC 1.1.9.1, type II quinoprotein alcohol dehydrogenase, quinohaemoprotein ethanol dehydrogenase, QHEDH, ADHIIB) is an enzyme with systematic name alcohol:azurin oxidoreductase. This enzyme catalyses the following chemical reaction

Mycofactocin (MFT) is a family of small molecules derived from a peptide of the type known as RiPP (ribosomally synthesized and post-translationally modified peptides), naturally occurring in many types of Mycobacterium. It was discovered in a bioinformatics study in 2011. All mycofactocins share a precursor in the form of premycofactocin (PMFT); they differ by the cellulose tail added. Being redox active, both PMFT and MFT have an oxidized dione (mycofactocinone) form and a reduced diol (mycofactocinol) form, respectively termed PMFTH2 and MFTH2.

References

  1. ↑ Geiger O, Gorisch H (1986). "Crystalline quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus". Biochemistry. 25: 6043–6048. doi:10.1021/bi00368a031.
  2. ↑ Dokter P, Frank J, Duine JA (October 1986). "Purification and characterization of quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus L.M.D. 79.41". The Biochemical Journal. 239 (1): 163–7. PMC   1147254 . PMID   3800975.
  3. ↑ Cleton-Jansen AM, Goosen N, Wenzel TJ, van de Putte P (May 1988). "Cloning of the gene encoding quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus: evidence for the presence of a second enzyme". Journal of Bacteriology. 170 (5): 2121–5. PMC   211095 . PMID   2834325.
  4. ↑ Matsushita K, Shinagawa E, Adachi O, Ameyama M (July 1989). "Quinoprotein D-glucose dehydrogenase of the Acinetobacter calcoaceticus respiratory chain: membrane-bound and soluble forms are different molecular species". Biochemistry. 28 (15): 6276–80. doi:10.1021/bi00441a020. PMID   2551369.
  5. ↑ Oubrie A, Dijkstra BW (July 2000). "Structural requirements of pyrroloquinoline quinone dependent enzymatic reactions". Protein Science. 9 (7): 1265–73. doi:10.1110/ps.9.7.1265. PMC   2144678 . PMID   10933491.
  6. ↑ Matsushita, K.; Toyama, H.; Ameyama, M.; Adachi, O.; Dewanti, A.; Duine, J.A. (1995). "Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus : the binding process of PQQ to the apoenzymes". Biosci. Biotechnol. Biochem. 59: 1548–1555. doi:10.1271/bbb.59.1548.
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