Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties

Yamanaka, Yuko; Kazuoka, Takayuki; Yoshida, Masahiro; Yamanaka, Kazuya; Oikawa, Tadao; Soda, Kenji

doi:10.1016/s0006-291x(02)02523-8

Cited by 32 publications

(19 citation statements)

References 33 publications

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“…In addition to having high activity at 4 °C, it also has significant stability at 37 °C, retaining activity for 3 weeks. This finding suggests that recombinant C. psychrerythraea GR has relatively high thermostability compared to the other reported psychrophilic enzymes (Cavicchioli et al 2002;Yamanaka et al 2002;Oikawa et al 2005). A more specific comparison that demonstrates its high thermostability is that GR from an Antarctic ice microalga, Chlamydomonas sp., retains only about 5 % activity after incubation at 4 °C for the same period of time (Ding et al 2007).…”

Section: Discussionmentioning

confidence: 86%

Characterization of recombinant glutathione reductase from the psychrophilic Antarctic bacterium Colwellia psychrerythraea

Barnwell

Grunden

2015

Extremophiles

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Glutathione reductases catalyze the reduction of oxidized glutathione (glutathione disulfide, GSSG) using NADPH as the substrate to produce reduced glutathione (GSH), which is an important antioxidant molecule that helps maintain the proper reducing environment of the cell. A recombinant form of glutathione reductase from Colwellia psychrerythraea, a marine psychrophilic bacterium, has been biochemically characterized to determine its molecular and enzymatic properties. C. psychrerythraea glutathione reductase was shown to be a homodimer with a molecular weight of 48.7 kDa using SDS-PAGE, MALDI-TOF mass spectrometry and gel filtration. The C. psychrerythraea glutathione reductase sequence shows significant homology to that of Escherichia coli glutathione reductase (66 % identity), and it possesses the FAD and NADPH binding motifs, as well as absorption spectrum features which are characteristic of flavoenzymes such as glutathione reductase. The psychrophilic C. psychrerythraea glutathione reductase exhibits higher k cat and k cat/K m at lower temperatures (4 °C) compared to mesophilic Baker's yeast glutathione reductase. However, C. psychrerythraea glutathione reductase was able to complement an E. coli glutathione reductase deletion strain in oxidative stress growth assays, demonstrating the functionality of C. psychrerythraea glutathione reductase over a broad temperature range, which suggests its potential utility as an antioxidant enzyme in heterologous systems.

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Section: Discussionmentioning

confidence: 86%

Characterization of recombinant glutathione reductase from the psychrophilic Antarctic bacterium Colwellia psychrerythraea

Barnwell

Grunden

2015

Extremophiles

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“…strain KUC-1 isolated from Antarctic seawater, grows optimally at 15°C and cannot grow above 30°C. This organism produces abundantly the paradoxical thermophilic NAD(P) ϩ -dependent aldehyde dehydrogenase and aspartase (21,41). From an evolutionary point of view, Rhizobium sp.…”

Section: Discussionmentioning

confidence: 99%

Thermophilic, Reversible γ-Resorcylate Decarboxylase from Rhizobium sp. Strain MTP-10005: Purification, Molecular Characterization, and Expression

2004

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We found the occurrence of thermophilic reversible ␥-resorcylate decarboxylase (␥-RDC) in the cell extract of a bacterium isolated from natural water, Rhizobium sp. strain MTP-10005, and purified the enzyme to homogeneity. The molecular mass of the enzyme was determined to be about 151 kDa by gel filtration, and that of the subunit was 37.5 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; in other words, the enzyme was a homotetramer. The enzyme was induced specifically by the addition of ␥-resorcylate to the medium. The enzyme required no coenzyme and did not act on 2,4-dihydroxybenzoate, 2,5-dihydroxybenzoate, 3,4-dihydroxybenzoate, 3,5-dihydroxybenzoate, 2-hydroxybenzoate, or 3-hydroxybenzoate. It was relatively thermostable to heat treatment, and its half-life at 50°C was estimated to be 122 min; furthermore, it catalyzed the reverse carboxylation of resorcinol. The values of k cat /K m (m⌴ ؊1 ⅐ s ؊1 ) for ␥-resorcylate and resorcinol at 30°C and pH 7 were 13.4 and 0.098, respectively. The enzyme contains 327 amino acid residues, and sequence identities were found with those of hypothetical protein AGR C 4595p from Agrobacterium tumefaciens strain C58 (96% identity), 5-carboxyvanillate decarboxylase from Sphingomonas paucimobilis (32%), and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylases from

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“…A high level of global stability has been reported for enzymes from psychrophiles, [33][34][35][36] indicating that a low level of global stability is not a prerequisite for cold-activity. Optimization of catalytic activity at low temperatures in psychrophilic enzymes is known to be caused either through a global loss of stability or flexibility in the active site regions.…”

Section: Biochemical Characterizationmentioning

confidence: 99%

Structural and Functional Properties of Isocitrate Dehydrogenase from the Psychrophilic Bacterium Desulfotalea psychrophila Reveal a Cold-active Enzyme with an Unusual High Thermal Stability

Fedøy

Yang

Martı́nez

et al. 2007

Journal of Molecular Biology

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Thermostable aldehyde dehydrogenase from psychrophile, Cytophaga sp. KUC-1: enzymological characteristics and functional properties

Cited by 32 publications

References 33 publications

Characterization of recombinant glutathione reductase from the psychrophilic Antarctic bacterium Colwellia psychrerythraea

Characterization of recombinant glutathione reductase from the psychrophilic Antarctic bacterium Colwellia psychrerythraea

Thermophilic, Reversible γ-Resorcylate Decarboxylase from Rhizobium sp. Strain MTP-10005: Purification, Molecular Characterization, and Expression

Structural and Functional Properties of Isocitrate Dehydrogenase from the Psychrophilic Bacterium Desulfotalea psychrophila Reveal a Cold-active Enzyme with an Unusual High Thermal Stability

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