A variety of catalases and bromoperoxidases in genus Pseudomonas and their characterization

Morinaga, Naoki; Nomura, Akihiko

doi:10.1016/0167-4838(92)90323-6

Cited by 15 publications

(7 citation statements)

References 22 publications

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“…3). From several Pseudomonas strains producing pyrrolnitrin, perhydrolases had been isolated using the monochlorodimedone assay (Wiesner et al 1988;Itoh et al 1992); these perhydrolases were believed to catalyze the two chlorination steps that occurred in pyrrolnitrin biosynthesis. However, disruption of the perhydrolase gene of Pseudomonas fluorescens had no influence on pyrrolnitrin biosynthesis, proving that this enzyme was not involved in pyrrolnitrin biosynthesis (Kirner et al 1996).…”

Section: Fadh 2 -Dependent Halogenasesmentioning

confidence: 99%

Microbial biosynthesis of halometabolites

Pée

2001

Archives of Microbiology

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Halometabolites are compounds that are commonly found in nature and they are produced by many different organisms. Whereas bromometabolites can mainly be found in the marine environment, chlorometabolites are predominately produced by terrestrial organisms; iodo- and fluorocompounds are only produced infrequently. The halogen atoms are incorporated into organic compounds by enzyme-catalyzed reactions with halide ions as the halogen source. For over 40 years haloperoxidases were thought to be responsible for the incorporation of halogen atoms into organic molecules. However, haloperoxidases lack substrate specificity and regioselectivity, and the connection of haloperoxidases with the in vivo formation of halometabolites has never been demonstrated. Recently, molecular genetic investigations showed that, at least in bacteria, a different class of halogenases is involved in halometabolite formation. These halogenases were found to require FADH2, which can be produced from FAD and NADH by unspecific flavin reductases. In addition to FADH2, oxygen and halide ions (chloride and bromide) are necessary for the halogenation reaction. The FADH2-dependent halogenases show substrate specificity and regioselectivity, and their genes have been detected in many halometabolite-producing bacteria, suggesting that this type of halogenating enzymes constitutes the major source for halometabolite formation in bacteria and possibly also in other organisms.

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Section: Fadh 2 -Dependent Halogenasesmentioning

confidence: 99%

Microbial biosynthesis of halometabolites

Pée

2001

Archives of Microbiology

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“…This was carried out with both purified enzyme and with purified enzyme recovered after catalytic turnover with the g-lactam substrate. Bromoperoxidase activity was assayed by the bromination of phenol red to bromophenol blue by a modification the method described by Itoh et al, 37 to use 1 ml reaction volumes and a pH value of pH 4.0. Bromoperoxidation was also measured by following the decomposition of monochlorodimedone at absorbance A 290 as described by Itoh et al 37 Cleavage of cyclic ethylene and propylene carbonate and the linear diethyl carbonate was assayed using an enzyme-linked method based on that described by Yang et al 32 Assays contained 50 mM Tris -HCl (pH 9.0), 100 mM cyclic carbonate, 2.5 mM NAD þ , one unit of horse liver alcohol dehydrogenase (ADH) and a suitable amount of (2 ) g-lactamase.…”

Section: Expression and Purificationmentioning

confidence: 99%

The Crystal Structure of a (−) γ-Lactamase from an Aureobacterium Species Reveals a Tetrahedral Intermediate in the Active Site

Line¹,

Isupov²,

Littlechild³

2004

Journal of Molecular Biology

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“…Loss of vanadate ions may occur during the purification process. Purification generally yields about 20% of the enzyme from the crude extract 26 . However, the mechanisms regulating the specific activity of the enzyme remain unclear.…”

Section: Discussionmentioning

confidence: 99%

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Kongkiattikajorn¹,

Pongdam²

2006

ScienceAsia

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In this study, we isolated a vanadium-haloperoxidase from a marine red alga, Gracilaria fisheri and characterized it. Gracilaria fisheri, was collected on the Southern Thailand coast, at Kohyor Beach in Songklha province. The enzyme was purified by homogenization and centrifugation, acetone fractionation, ionexchange and gel filtration chromatography. Molecular weight was determined by gel chromatography and found to be approximately 615 kDa. The UV spectrum of the peroxidase did not show absorbance in the Soret band indicating a non-heme protein, like a vanadium-dependent haloperoxidase. Reconstitution experiments in the presence of several metal ions confirmed haloperoxidase requires vanadium for enzyme activity and showed that only vanadium completely restored the enzyme activity. The enzyme was moderately thermostable, keeping full activity up to 40°C. Some preliminary steady-state kinetic studies were performed and apparent Michaelis-Menten kinetic parameters were determined for the substrates bromide and hydrogen peroxide.

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A variety of catalases and bromoperoxidases in genus Pseudomonas and their characterization

Cited by 15 publications

References 22 publications

Microbial biosynthesis of halometabolites

Microbial biosynthesis of halometabolites

The Crystal Structure of a (−) γ-Lactamase from an Aureobacterium Species Reveals a Tetrahedral Intermediate in the Active Site

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