Alcohol dehydrogenase (azurin)

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Alcohol dehydrogenase (azurin)
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EC no. 1.1.9.1
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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. [1] [2] [3] [4] [5] [6] This enzyme catalyses the following chemical reaction

primary alcohol + azurin aldehyde + reduced azurin

This enzyme is a periplasmic PQQ-containing quinohemoprotein.

Related Research Articles

<span class="mw-page-title-main">Alcohol dehydrogenase</span> Group of dehydrogenase enzymes

Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. In humans and many other animals, they serve to break down alcohols that are otherwise toxic, and they also participate in the generation of useful aldehyde, ketone, or alcohol groups during the biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.

<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.

In enzymology, a cis-2,3-dihydrobiphenyl-2,3-diol dehydrogenase (EC 1.3.1.56) is an enzyme that catalyzes the chemical reaction

In enzymology, a quinoline 2-oxidoreductase (EC 1.3.99.17) is an enzyme that catalyzes the chemical reaction

In enzymology, an alcohol dehydrogenase (acceptor) (EC 1.1.99.8) is an enzyme that catalyzes the chemical reaction

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

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

In enzymology, a mycothiol-dependent formaldehyde dehydrogenase (EC 1.1.1.306) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Steroid Delta-isomerase</span>

In enzymology, a steroid Δ5-isomerase is an enzyme that catalyzes the chemical reaction

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

Azurin is a small, periplasmic, bacterial blue copper protein found in Pseudomonas, Bordetella, or Alcaligenes bacteria. Azurin moderates single-electron transfer between enzymes associated with the cytochrome chain by undergoing oxidation-reduction between Cu(I) and Cu(II). Each monomer of an azurin tetramer has a molecular weight of approximately 14kDa, contains a single copper atom, is intensively blue, and has a fluorescence emission band centered at 308 nm.

<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

Soluble quinoprotein glucose dehydrogenase is an enzyme with systematic name D-glucose:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction

Alcohol dehydrogenase (nicotinoprotein) (EC 1.1.99.36, NDMA-dependent alcohol dehydrogenase, nicotinoprotein alcohol dehydrogenase, np-ADH, ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase) is an enzyme with systematic name ethanol:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction

Methylamine dehydrogenase (amicyanin) (EC 1.4.9.1, amine dehydrogenase, primary-amine dehydrogenase) is an enzyme with systematic name methylamine:amicyanin oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction:

Aralkylamine dehydrogenase (azurin) (EC 1.4.9.2, aromatic amine dehydrogenase, arylamine dehydrogenase, tyramine dehydrogenase) is an enzyme with the systematic name aralkylamine:azurin oxidoreductase (deaminating). This enzyme catalyses the following chemical reaction:

Lupanine 17-hydroxylase (cytochrome c) (EC 1.17.2.2, lupanine dehydrogenase (cytochrome c)) is an enzyme with systematic name lupanine:cytochrome c-oxidoreductase (17-hydroxylating). This enzyme catalyses the following chemical reaction

References

  1. ↑ Groen BW, van Kleef MA, Duine JA (March 1986). "Quinohaemoprotein alcohol dehydrogenase apoenzyme from Pseudomonas testosteroni". The Biochemical Journal. 234 (3): 611–5. doi:10.1042/bj2340611. PMC   1146615 . PMID   3521592.
  2. ↑ de Jong GA, Caldeira J, Sun J, Jongejan JA, de Vries S, Loehr TM, Moura I, Moura JJ, Duine JA (July 1995). "Characterization of the interaction between PQQ and heme c in the quinohemoprotein ethanol dehydrogenase from Comamonas testosteroni". Biochemistry. 34 (29): 9451–8. doi:10.1021/bi00029a021. PMID   7626615.
  3. ↑ Toyama H, Fujii A, Matsushita K, Shinagawa E, Ameyama M, Adachi O (May 1995). "Three distinct quinoprotein alcohol dehydrogenases are expressed when Pseudomonas putida is grown on different alcohols". Journal of Bacteriology. 177 (9): 2442–50. doi:10.1128/jb.177.9.2442-2450.1995. PMC   176903 . PMID   7730276.
  4. ↑ Matsushita K, Yamashita T, Aoki N, Toyama H, Adachi O (May 1999). "Electron transfer from quinohemoprotein alcohol dehydrogenase to blue copper protein azurin in the alcohol oxidase respiratory chain of Pseudomonas putida HK5". Biochemistry. 38 (19): 6111–8. doi:10.1021/bi990121f. PMID   10320337.
  5. ↑ Chen ZW, Matsushita K, Yamashita T, Fujii TA, Toyama H, Adachi O, Bellamy HD, Mathews FS (June 2002). "Structure at 1.9 A resolution of a quinohemoprotein alcohol dehydrogenase from Pseudomonas putida HK5". Structure. 10 (6): 837–49. doi: 10.1016/s0969-2126(02)00774-8 . PMID   12057198.
  6. ↑ Oubrie A, Rozeboom HJ, Kalk KH, Huizinga EG, Dijkstra BW (February 2002). "Crystal structure of quinohemoprotein alcohol dehydrogenase from Comamonas testosteroni: structural basis for substrate oxidation and electron transfer". The Journal of Biological Chemistry. 277 (5): 3727–32. doi: 10.1074/jbc.M109403200 . PMID   11714714.
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