Purification and Properties of Glycine Oxidase from &lt;i&gt;Pseudomonas putida&lt;/i&gt; KT2440

Equar, Messele Yohannes; Tani, Yasuhiro; Mihara, Hisaaki

doi:10.3177/jnsv.61.506

Cited by 7 publications

(3 citation statements)

References 14 publications

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“…Traditional glycine oxidases (EC 1.4.3.19) contain noncovalently bound FAD. They have been previously described in microorganisms of the genera Bacillus , − Geobacillus , and Pseudomonas . Glycine oxidase from Bacillus subtilis (ThiO) participates in the biosynthesis of the thiazole moiety of the thiamin .…”

Section: Discussionmentioning

confidence: 99%

“…They have been previously described in microorganisms of the genera Bacillus, 42−44 Geobacillus, 45 and Pseudomonas. 46 Glycine oxidase from Bacillus subtilis (ThiO) participates in the biosynthesis of the thiazole moiety of the thiamin. 47 This class of enzymes has been used for a variety of applications such as the design of biosensors, agricultural biotechnology, and industrial biocatalysis.…”

Section: ■ Discussionmentioning

confidence: 99%

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Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea

et al. 2018

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Glycine oxidase from Pseudoalteromonas luteoviolacea (PlGoxA) is a cysteine tryptophylquinone (CTQ)-dependent enzyme. Sequence analysis and phylogenetic analysis place it in a newly designated subgroup (group IID) of a recently identified family of LodA-like proteins, which are predicted to possess CTQ. The crystal structure of PlGoxA reveals that it is a homotetramer. It possesses an N-terminal domain with no close structural homologues in the Protein Data Bank. The active site is quite small because of intersubunit interactions, which may account for the observed cooperativy toward glycine. Steady-state kinetic analysis yielded the following values: k = 6.0 ± 0.2 s, K = 187 ± 18 μM, and h = 1.77 ± 0.27. In contrast to other quinoprotein amine dehydrogenases and oxidases that exhibit anomalously large primary kinetic isotope effects on the rate of reduction of the quinone cofactor by the amine substrate, no significant primary kinetic isotope effect was observed for this reaction of PlGoxA. The absorbance spectrum of glycine-reduced PlGoxA exhibits features in the range of 400-650 nm that have not previously been seen in other quinoproteins. Thus, in addition to the unusual structural features of PlGoxA, the kinetic and chemical reaction mechanisms of the reductive half-reaction of PlGoxA appear to be distinct from those of other amine dehydrogenases and amine oxidases that use tryptophylquinone and tyrosylquinone cofactors.

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Section: Discussionmentioning

confidence: 99%

Section: ■ Discussionmentioning

confidence: 99%

Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea

et al. 2018

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“…GO from Bacillus subtilis (BsGO) was first cloned in 1998 . GOs have been reported from several microorganisms, including Pseudomonas putida KT2440, Geobacillus kaustophilus HTA426, B. cereus ATCC 14579, and B. licheniformis . In this study, based on the functional annotation of the whole genome sequence and the alignment with the reported glyphosate degradation genes, a potential glyphosate degradation enzyme gene in strain Y16C was predicted and named goW , and it is a glycine oxidase in the FAD-dependent oxidoreductase class.…”

Section: Discussionmentioning

confidence: 99%

Cellular Response and Molecular Mechanism of Glyphosate Degradation by Chryseobacterium sp. Y16C

Zhang

Chen

et al. 2023

J. Agric. Food Chem.

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Glyphosate is one of the most widely used herbicides worldwide. Unfortunately, the continuous use of glyphosate has resulted in serious environmental contamination and raised public concern about its impact on human health. In our previous study, Chryseobacterium sp. Y16C was isolated and characterized as an efficient degrader that can completely degrade glyphosate. However, the biochemical and molecular mechanisms underlying its glyphosate biodegradation ability remain unclear. In this study, the physiological response of Y16C to glyphosate stimulation was characterized at the cellular level. The results indicated that, in the process of glyphosate degradation, Y16C induced a series of physiological responses in the membrane potential, reactive oxygen species levels, and apoptosis. The antioxidant system of Y16C was activated to alleviate the oxidative damage caused by glyphosate. Furthermore, a novel gene, goW, was expressed in response to glyphosate. The gene product, GOW, is an enzyme that catalyzes glyphosate degradation, with putative structural similarities to glycine oxidase. GOW encodes 508 amino acids, with an isoelectric point of 5.33 and a molecular weight of 57.2 kDa, which indicates that it is a glycine oxidase. GOW displays maximum enzyme activity at 30 °C and pH 7.0. Additionally, most of the metal ions exhibited little influence on the enzyme activity except for Cu2+. Finally, with glyphosate as the substrate, the catalytic efficiency of GOW was higher than that of glycine, although opposite results were observed for the affinity. Taken together, the current study provides new insights to deeply understand and reveal the mechanisms of glyphosate degradation in bacteria.

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Enzymes in Metabolic Anticancer Therapy

Maggi

Scotti

2019

Advances in Experimental Medicine and Biology

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Purification and Properties of Glycine Oxidase from <i>Pseudomonas putida</i> KT2440

Cited by 7 publications

References 14 publications

Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea

Structure and Enzymatic Properties of an Unusual Cysteine Tryptophylquinone-Dependent Glycine Oxidase from Pseudoalteromonas luteoviolacea

Cellular Response and Molecular Mechanism of Glyphosate Degradation by Chryseobacterium sp. Y16C

Enzymes in Metabolic Anticancer Therapy

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