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Methanol dehydrogenase

In enzymology, a methanol dehydrogenase (MDH) is an enzyme that catalyzes the chemical reaction:

PQQ-MDH enzyme structure, with PQQ in the center. The yellow sphere represents a La3+ ion.[1]
CH3OH CH2O + 2 electrons + 2H+

How the electrons are captured and transported depends upon the kind of methanol dehydrogenase. There are three main types of MDHs: NAD+-dependent MDH, pyrrolo-quinoline quinone dependent MDH, and oxygen-dependent alcohol oxidase.[2]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is methanol:NAD+ oxidoreductase. This enzyme participates in methane metabolism.

Classes of Methanol Dehydrogenase edit

 
Shows the reaction of methanol to formaldehyde catalyzed by MDH.[2]

NAD+ Dependent MDH edit

A common electron acceptor in biological systems is nicotinamide adenine dinucleotide (NAD+); some enzymes use a related molecule called nicotinamide adenine dinucleotide phosphate (NADP+). An NAD+-dependent methanol dehydrogenase(EC 1.1.1.244) was first reported in a Gram-positive methylotroph[3] and is an enzyme that catalyzes the chemical reaction:

CH3OH + NAD+   CH2O + NADH + H+

Thus, the two substrates of this enzyme are methanol and NAD+, whereas its 3 products are formaldehyde (CH2O), NADH, and H+. This can be performed under both aerobic and anaerobic conditions.[2]

NAD+ -dependent MDHs are found in thermophilic, Gram positive methlyotrophs, but can also been obtained from some non-methylotrophic bacteria. NAD+-dependent MDHs have so far been found in Bacillus sp., Lysinibacillus sp.,and Cupriavidus sp.[2]

PQQ-Dependent MDH edit

For Gram-negative bacteria, methanol oxidation occurs in the periplasmic space, facilitated by PQQ-dependent MDH. PQQ-dependent MDHs contain a PQQ prosthetic group, which has the role of capturing electrons from methanol oxidation and passing them to the cytochrome.[2]

MxaFI and XoxF are the genes that encode for PQQ-dependent MDHs. In MxaFI-type MDH, calcium (Ca2+) is encoded as the cofactor for PQQ-dependent methylotrophy.[2] XoxF-type MDHs use lanthanides (Ln3+) as cofactors and are highly selective towards early lanthanides (typically La-Nd). Sm3+, Eu3+, and Gd3+ can support some XoxF-type organisms, but less effectively. Pm3+ and Tb-Lu have shown no evidence of utilization so far.[2]

Many methylotrophs encode both MxaFI and XoxF, but those that encode only one will encode exclusively for XoxF.[4]

O2-Dependent Alcohol Oxidase edit

Oxygen-dependent alcohol oxidase (AOX) can be obtained from eukaryotic methylotrophs in the peroxisome of yeasts. Formaldehyde and hydrogen peroxide (H2O2) are formed through the oxidation of methanol. Dihydroxyacetone synthase (DAS) and catalase (CTA) must then transform these toxic chemicals into non-toxic forms to protect the cell. In this process, electrons from methanol are not captured as usable energy by the cell, and are thus lost.[2]

References edit

  1. ^ Deng YW, Ro SY, Rosenzweig AC (October 2018). "Structure and function of the lanthanide-dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C". Journal of Biological Inorganic Chemistry. 23 (7): 1037–1047. doi:10.1007/s00775-018-1604-2. PMC 6370294. PMID 30132076.
  2. ^ a b c d e f g h Le TK, Lee YJ, Han GH, Yeom SJ (2021). "Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy". Frontiers in Bioengineering and Biotechnology. 9: 787791. doi:10.3389/fbioe.2021.787791. PMC 8741260. PMID 35004648.
  3. ^ Arfman N, Watling EM, Clement W, van Oosterwijk RJ, de Vries GE, Harder W, et al. (1989). "Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme". Archives of Microbiology. 152 (3): 280–288. doi:10.1007/BF00409664. PMID 2673121.
  4. ^ Chistoserdova L, Kalyuzhnaya MG (August 2018). "Current Trends in Methylotrophy". Trends in Microbiology. 26 (8): 703–714. doi:10.1016/j.tim.2018.01.011. PMID 29471983.

Further reading edit

  • Arfman N, Watling EM, Clement W, van Oosterwijk RJ, de Vries GE, Harder W, et al. (1989). "Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD-dependent methanol dehydrogenase as a key enzyme". Archives of Microbiology. 152 (3): 280–288. doi:10.1007/BF00409664. PMID 2673121.


methanol, dehydrogenase, enzymology, methanol, dehydrogenase, enzyme, that, catalyzes, chemical, reaction, enzyme, structure, with, center, yellow, sphere, represents, ch3oh, displaystyle, rightleftharpoons, ch2o, electrons, electrons, captured, transported, d. In enzymology a methanol dehydrogenase MDH is an enzyme that catalyzes the chemical reaction PQQ MDH enzyme structure with PQQ in the center The yellow sphere represents a La3 ion 1 CH3OH displaystyle rightleftharpoons CH2O 2 electrons 2H How the electrons are captured and transported depends upon the kind of methanol dehydrogenase There are three main types of MDHs NAD dependent MDH pyrrolo quinoline quinone dependent MDH and oxygen dependent alcohol oxidase 2 This enzyme belongs to the family of oxidoreductases specifically those acting on the CH OH group of donor with NAD or NADP as acceptor The systematic name of this enzyme class is methanol NAD oxidoreductase This enzyme participates in methane metabolism Contents 1 Classes of Methanol Dehydrogenase 1 1 NAD Dependent MDH 1 2 PQQ Dependent MDH 1 3 O2 Dependent Alcohol Oxidase 2 References 3 Further readingClasses of Methanol Dehydrogenase edit nbsp Shows the reaction of methanol to formaldehyde catalyzed by MDH 2 NAD Dependent MDH edit A common electron acceptor in biological systems is nicotinamide adenine dinucleotide NAD some enzymes use a related molecule called nicotinamide adenine dinucleotide phosphate NADP An NAD dependent methanol dehydrogenase EC 1 1 1 244 was first reported in a Gram positive methylotroph 3 and is an enzyme that catalyzes the chemical reaction CH3OH NAD displaystyle rightleftharpoons nbsp CH2O NADH H Thus the two substrates of this enzyme are methanol and NAD whereas its 3 products are formaldehyde CH2O NADH and H This can be performed under both aerobic and anaerobic conditions 2 NAD dependent MDHs are found in thermophilic Gram positive methlyotrophs but can also been obtained from some non methylotrophic bacteria NAD dependent MDHs have so far been found in Bacillus sp Lysinibacillus sp and Cupriavidus sp 2 PQQ Dependent MDH edit For Gram negative bacteria methanol oxidation occurs in the periplasmic space facilitated by PQQ dependent MDH PQQ dependent MDHs contain a PQQ prosthetic group which has the role of capturing electrons from methanol oxidation and passing them to the cytochrome 2 MxaFI and XoxF are the genes that encode for PQQ dependent MDHs In MxaFI type MDH calcium Ca2 is encoded as the cofactor for PQQ dependent methylotrophy 2 XoxF type MDHs use lanthanides Ln3 as cofactors and are highly selective towards early lanthanides typically La Nd Sm3 Eu3 and Gd3 can support some XoxF type organisms but less effectively Pm3 and Tb Lu have shown no evidence of utilization so far 2 Many methylotrophs encode both MxaFI and XoxF but those that encode only one will encode exclusively for XoxF 4 O2 Dependent Alcohol Oxidase edit Oxygen dependent alcohol oxidase AOX can be obtained from eukaryotic methylotrophs in the peroxisome of yeasts Formaldehyde and hydrogen peroxide H2O2 are formed through the oxidation of methanol Dihydroxyacetone synthase DAS and catalase CTA must then transform these toxic chemicals into non toxic forms to protect the cell In this process electrons from methanol are not captured as usable energy by the cell and are thus lost 2 References edit Deng YW Ro SY Rosenzweig AC October 2018 Structure and function of the lanthanide dependent methanol dehydrogenase XoxF from the methanotroph Methylomicrobium buryatense 5GB1C Journal of Biological Inorganic Chemistry 23 7 1037 1047 doi 10 1007 s00775 018 1604 2 PMC 6370294 PMID 30132076 a b c d e f g h Le TK Lee YJ Han GH Yeom SJ 2021 Methanol Dehydrogenases as a Key Biocatalysts for Synthetic Methylotrophy Frontiers in Bioengineering and Biotechnology 9 787791 doi 10 3389 fbioe 2021 787791 PMC 8741260 PMID 35004648 Arfman N Watling EM Clement W van Oosterwijk RJ de Vries GE Harder W et al 1989 Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD dependent methanol dehydrogenase as a key enzyme Archives of Microbiology 152 3 280 288 doi 10 1007 BF00409664 PMID 2673121 Chistoserdova L Kalyuzhnaya MG August 2018 Current Trends in Methylotrophy Trends in Microbiology 26 8 703 714 doi 10 1016 j tim 2018 01 011 PMID 29471983 Further reading editArfman N Watling EM Clement W van Oosterwijk RJ de Vries GE Harder W et al 1989 Methanol metabolism in thermotolerant methylotrophic Bacillus strains involving a novel catabolic NAD dependent methanol dehydrogenase as a key enzyme Archives of Microbiology 152 3 280 288 doi 10 1007 BF00409664 PMID 2673121 Portal nbsp Biology This EC 1 1 1 enzyme related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Methanol dehydrogenase amp oldid 1197729481, wikipedia, wiki, book, books, library,

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