First characterization of extremely halophilic 2-deoxy-D-ribose-5-phosphate aldolase

Ohshida, Tatsuya; Hayashi, Junji; Satomura, Takenori; Kawakami, Retsuo; Ohshima, Toshihisa; Sakuraba, Haruhiko

doi:10.1016/j.pep.2016.05.009

Cited by 9 publications

(3 citation statements)

References 31 publications

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“… 0.02 1 c 46% retention of activity 20 h 300 mM 25 °C (Sakuraba et al 2007 ) Hyperthermus butylicus 26.4 5.5 80 0.15 0.5 c 75% retention of activity 8 h 300 mM 25 °C (Wang et al 2010 ) Aciduliprofundum boonei 26.6 7 80 0.12 n.s. 70% retention of activity 4 h 250 mM 25 °C (Yin et al 2011 ) Haloarcula japonica (Halophilic) 26.6 6.4 60 1.02 8.92 b 35% retention of activity 5 h 300 mM 25 °C (Ohshida et al 2016 ) n.s. not specified a Of monomer b V max c Specific activity d One unit is defined as the amount of DERA required to cleave 1 μmol DR5P per minute e Increase of activity till 65 °C; extreme loss in activity at 67 °C and 70 °C *Measured at 37 °C **Measured at 50 °C ***Measured at 95 °C …”

Section: Substrate Specificitymentioning

confidence: 99%

2-Deoxy-d-ribose-5-phosphate aldolase (DERA): applications and modifications

Haridas

Abdelraheem

Hanefeld

2018

Appl Microbiol Biotechnol

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2-Deoxy-d-ribose-5-phosphate aldolase (DERA) is a class I aldolase that offers access to several building blocks for organic synthesis. It catalyzes the stereoselective C–C bond formation between acetaldehyde and numerous other aldehydes. However, the practical application of DERA as a biocatalyst is limited by its poor tolerance towards industrially relevant concentrations of aldehydes, in particular acetaldehyde. Therefore, the development of proper experimental conditions, including protein engineering and/or immobilization on appropriate supports, is required. The present review is aimed to provide a brief overview of DERA, its history, and progress made in understanding the functioning of the enzyme. Furthermore, the current understanding regarding aldehyde resistance of DERA and the various optimizations carried out to modify this property are discussed.

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Section: Substrate Specificitymentioning

confidence: 99%

2-Deoxy-d-ribose-5-phosphate aldolase (DERA): applications and modifications

Haridas

Abdelraheem

Hanefeld

2018

Appl Microbiol Biotechnol

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“…[ 30 ], Paenibacillus sp. [ 31 ], and Haloarcula japonica [ 32 ]; Thermotoga maritima [ 29 ]; Aciduliprofundum boonei [ 33 ], and Rhodococcus erythropolis [ 34 ]; E . coli [ 29 ], Haemophilus influenzae [ 35 ], and Pseudomonas syringae [ 36 ], were 4.0, 5.5, 6.0, 6.5, 7.0, and 7.5, respectively.…”

Section: Resultsmentioning

confidence: 99%

In Vitro One-Pot 3-Hydroxypropanal Production from Cheap C1 and C2 Compounds

Seo

Yeom

2022

IJMS

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One- or two-carbon (C1 or C2) compounds have been considered attractive substrates because they are inexpensive and abundant. Methanol and ethanol are representative C1 and C2 compounds, which can be used as bio-renewable platform feedstocks for the biotechnological production of value-added natural chemicals. Methanol-derived formaldehyde and ethanol-derived acetaldehyde can be converted to 3-hydroxypropanal (3-HPA) via aldol condensation. 3-HPA is used in food preservation and as a precursor for 3-hydroxypropionic acid and 1,3-propanediol that are starting materials for manufacturing biocompatible plastic and polytrimethylene terephthalate. In this study, 3-HPA was biosynthesized from formaldehyde and acetaldehyde using deoxyribose-5-phosphate aldolase from Thermotoga maritima (DERATma) and cloned and expressed in Escherichia coli for 3-HPA production. Under optimum conditions, DERATma produced 7 mM 3-HPA from 25 mM substrate (formaldehyde and acetaldehyde) for 60 min with 520 mg/L/h productivity. To demonstrate the one-pot 3-HPA production from methanol and ethanol, we used methanol dehydrogenase from Lysinibacillus xylanilyticus (MDHLx) and DERATma. One-pot 3-HPA production via aldol condensation of formaldehyde and acetaldehyde from methanol and ethanol, respectively, was investigated under optimized reaction conditions. This is the first report on 3-HPA production from inexpensive alcohol substrates (methanol and ethanol) by cascade reaction using DERATma and MDHLx.

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“…The optimum conditions for the enzyme activity were 1 M NaCl and 60 C. The recombinant enzyme (29 kDa) was stable against the solvents acetonitrile and DMSO. In different organisms, 2-deoxy-D-ribose-5-phosphate aldolase is involved in carbon metabolism and could be used to produce pharmaceutically active compounds [283].…”

Section: Miscellaneous Enzymes From Haloarchaeamentioning

confidence: 99%

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

et al. 2017

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Halophilic archaea, also referred to as haloarchaea, dominate hypersaline environments. To survive under such extreme conditions, haloarchaea and their enzymes have evolved to function optimally in environments with high salt concentrations and, sometimes, with extreme pH and temperatures. These features make haloarchaea attractive sources of a wide variety of biotechnological products, such as hydrolytic enzymes, with numerous potential applications in biotechnology. The unique trait of haloarchaeal enzymes, haloenzymes, to sustain activity under hypersaline conditions has extended the range of already-available biocatalysts and industrial processes in which high salt concentrations inhibit the activity of regular enzymes. In addition to their halostable properties, haloenzymes can also withstand other conditions such as extreme pH and temperature. In spite of these benefits, the industrial potential of these natural catalysts remains largely unexplored, with only a few characterized extracellular hydrolases. Because of the applied impact of haloarchaea and their specific ability to live in the presence of high salt concentrations, studies on their systematics have intensified in recent years, identifying many new genera and species. This review summarizes the current status of the haloarchaeal genera and species, and discusses the properties of haloenzymes and their potential industrial applications. SYSTEMATICS OF HALOPHILIC ARCHAEAHalophilic micro-organisms are found in the three domains of life, and are extremophiles living in hypersaline environments in the presence of salt (generally NaCl) as a specific requisite for their growth [1]. Hypersaline environments contain higher salt concentrations than seawater (3.5 % total dissolved salts) [2]. According to the optimum NaCl concentration for growth, micro-organisms fall into one of the following categories: extreme halophiles with optimum growth at 15-30 % (2.5-5.2 M) NaCl; moderate halophiles with optimum growth at 3-15 % (0.5-2.5 M) NaCl; slight halophiles with optimum growth at 1-3 % (0.2-0.5 M) NaCl; non-halophiles with optimum growth at less than 1 % (0.2 M) NaCl; and halotolerant micro-organisms which are non-halophiles showing the ability to tolerate high NaCl concentrations [3]. Halophiles can live in hypersaline environments because they are able to sustain osmotic balance. They use two main strategies to withstand the adverse consequences of water loss when exposed to high salt concentrations. The first strategy used by extremely halophilic archaea (haloarchaea) and halophilic anaerobic bacteria such as members of Halanaerobiales is known as the 'salt-in-cytoplasm' strategy, during which salts such as NaCl or KCl accumulate in the cytoplasm at concentrations similar to the extracellular ones [4,5]. Another mechanism to cope with high salt concentrations is the accumulation of organic molecules such as amino acids, sugars and polyols, known as compatible solutes or osmolytes. Compatible solutes are small and highly soluble molecules that can...

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First characterization of extremely halophilic 2-deoxy-D-ribose-5-phosphate aldolase

Cited by 9 publications

References 31 publications

2-Deoxy-d-ribose-5-phosphate aldolase (DERA): applications and modifications

2-Deoxy-d-ribose-5-phosphate aldolase (DERA): applications and modifications

In Vitro One-Pot 3-Hydroxypropanal Production from Cheap C1 and C2 Compounds

Systematics of haloarchaea and biotechnological potential of their hydrolytic enzymes

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