Glutathione-independent Formaldehyde Dehydrogenase from<i>Pseudomons putida</i>: Survey of Functional Groups with Special Regard for Cysteine Residues

Tsuru, Daisuke; Oda, Nobuyuki; Matsuo, Yo; Ishikawa, Sara; Itō, Kiyoshi; Yoshimoto, Tadashi

doi:10.1271/bbb.61.1354

Cited by 9 publications

(9 citation statements)

References 3 publications

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“…The Cys-46 and His-67 residues are coordinated with the catalytic zinc ion, and the Cys-97, 100, 103, and 111 residues are associated with the structural one. 20,21) The mutants in region A are less stable than those in region C.…”

Section: Resultsmentioning

confidence: 99%

The Artificial Evolution of an Enzyme by Random Mutagenesis: The Development of Formaldehyde Dehydrogenase

Fujii

Yamasaki

Matsumoto

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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Section: Resultsmentioning

confidence: 99%

The Artificial Evolution of an Enzyme by Random Mutagenesis: The Development of Formaldehyde Dehydrogenase

Fujii

Yamasaki

Matsumoto

et al. 2004

Bioscience, Biotechnology, and Biochemistry

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“…Studies on formaldehyde-resistant, Gram-negative bacteria have revealed two enzymes which do not need the addition of thiols for in vitro activity: NAD-dependent formaldehyde dehydrogenase (ND-FalDH) [15] and formaldehyde dismutase (FDM) [2]. In principle, formaldehyde could be oxidized by these enzymes in its thiohemiketal form (as adduct with an internal cysteinyl group in the enzyme).…”

Section: Thiol-independent Formaldehyde Dehydrogenasesmentioning

confidence: 99%

Thiols in formaldehyde dissimilation and detoxification

Duine

1999

BioFactors

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Glutathione is not a universal coenzyme for formaldehyde oxidation. MySH (mycothiol, 1-O-(2'-[N-acetyl-L-cysteinyl]amido-2'-deoxy-alpha-D-glucopyranosyl)-D-m yo-inositol) is GSH's counterpart as coenzyme in formaldehyde dehydrogenase from certain gram-positive bacteria. However, formaldehyde dissimilation and detoxification not only proceed via thiol-dependent but also via thiol-independent dehydrogenases. The distinct structures and enzymatic properties of MySH-dependent and GSH-dependent formaldehyde dehydrogenases could provide clues for development of selective drugs against pathogenic Mycobacteria. It is to be expected that other new types of thiol-dependent formaldehyde dehydrogenases will be discovered in the future. Indications exist that the product of thiol-dependent formaldehyde oxidation, the thiol formate ester, is not only hydrolytically converted into thiol and formate but can also be oxidatively converted in some cases by a molybdoprotein aldehyde dehydrogenase into the corresponding carbonate ester, decomposing spontaneously into CO2 and the thiol.

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“…These pathways can also be found in non-methylotrophs, are often linear (Fig. 1), and may differ in their cofactor dependence, as some enzymes oxidize formaldehyde directly (Ando et al 1979;Tsuru et al 1997) while others use a carrier like glutathione (Gutheil et al 1992), mycothiol Misset-Smits et al 1997;Vogt et al 2003;Witthoff et al 2013), bacillithiol (Newton et al 2009), tetrahydrofolate (THF) (Kallen and Jencks 1966), or tetrahydromethanopterine (Maden 2000) before it is sequentially oxidized to CO 2 (Pomper et al 1999).…”

Section: Introductionmentioning

confidence: 99%

Production of carbon-13-labeled cadaverine by engineered Corynebacterium glutamicum using carbon-13-labeled methanol as co-substrate

Leßmeier

Pfeifenschneider

Carnicer

et al. 2015

Appl Microbiol Biotechnol

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Methanol, a one-carbon compound, can be utilized by a variety of bacteria and other organisms as carbon and energy source and is regarded as a promising substrate for biotechnological production. In this study, a strain of non-methylotrophic Corynebacterium glutamicum, which was able to produce the polyamide building block cadaverine as non-native product, was engineered for co-utilization of methanol. Expression of the gene encoding NAD+-dependent methanol dehydrogenase (Mdh) from the natural methylotroph Bacillus methanolicus increased methanol oxidation. Deletion of the endogenous aldehyde dehydrogenase genes ald and fadH prevented methanol oxidation to carbon dioxide and formaldehyde detoxification via the linear formaldehyde dissimilation pathway. Heterologous expression of genes for the key enzymes hexulose-6-phosphate synthase and 6-phospho-3-hexuloisomerase of the ribulose monophosphate (RuMP) pathway in this strain restored growth in the presence of methanol or formaldehyde, which suggested efficient formaldehyde detoxification involving RuMP key enzymes. While growth with methanol as sole carbon source was not observed, the fate of 13C-methanol added as co-substrate to sugars was followed and the isotopologue distribution indicated incorporation into central metabolites and in vivo activity of the RuMP pathway. In addition, 13C-label from methanol was traced to the secreted product cadaverine. Thus, this synthetic biology approach led to a C. glutamicum strain that converted the non-natural carbon substrate methanol at least partially to the non-native product cadaverine.

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Glutathione-independent Formaldehyde Dehydrogenase fromPseudomons putida: Survey of Functional Groups with Special Regard for Cysteine Residues

Cited by 9 publications

References 3 publications

The Artificial Evolution of an Enzyme by Random Mutagenesis: The Development of Formaldehyde Dehydrogenase

The Artificial Evolution of an Enzyme by Random Mutagenesis: The Development of Formaldehyde Dehydrogenase

Thiols in formaldehyde dissimilation and detoxification

Production of carbon-13-labeled cadaverine by engineered Corynebacterium glutamicum using carbon-13-labeled methanol as co-substrate

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