Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene

Bantleon, Rüdiger; Altenbuchner, Josef; Pée, K.-H. Van

doi:10.1128/jb.176.8.2339-2347.1994

Cited by 60 publications

(27 citation statements)

References 39 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Three classes of haloperoxidases have been identified. One of these consists of enzymes without a prosthetic group and as such have been detected in a number of bacteria (1,2). The remaining two classes are the so-called heme-containing haloperoxidases-exemplified by the CPO from the fungus Caldariomyces fumago (3) or myeloperoxidase which is present in white blood cells (4)-and the vanadium-containing haloperoxidases that bind a vanadate ion (VO 4 3Ϫ ) as a prosthetic group.…”

mentioning

confidence: 99%

From phosphatases to vanadium peroxidases: A similar architecture of the active site

Hemrika¹,

Renirie²,

Dekker³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

173

164

View full text Add to dashboard Cite

We show here that the amino acid residues contributing to the active sites of the vanadate containing haloperoxidases are conserved within three families of acid phosphatases; this suggests that the active sites of these enzymes are very similar. This is confirmed by activity measurements showing that apochloroperoxidase exhibits phosphatase activity. These observations not only reveal interesting evolutionary relationships between these groups of enzymes but may also have important implications for the research on acid phosphatases, especially glucose-6-phosphatase-the enzyme affected in von Gierke disease-of which the predicted membrane topology may have to be reconsidered.Haloperoxidases are enzymes catalyzing the two electron oxidation of a halide (X Ϫ ) to the corresponding hypohalous acid according to Eq. 1.HOX may further react with a broad range of nucleophilic acceptors to form a diversity of halogenated compounds. These haloperoxidases are named after the most electronegative halide they are able to oxidize, and thus a chloroperoxidase (CPO) is able to oxidize chloride, bromide, and iodide. Three classes of haloperoxidases have been identified. One of these consists of enzymes without a prosthetic group and as such have been detected in a number of bacteria (1, 2). The remaining two classes are the so-called heme-containing haloperoxidases-exemplified by the CPO from the fungus Caldariomyces fumago (3) or myeloperoxidase which is present in white blood cells (4)-and the vanadium-containing haloperoxidases that bind a vanadate ion (VO 4 3Ϫ ) as a prosthetic group. Enzymes representing these two classes not only differ in the nature of their prosthetic group but also in at least two other aspects: catalytic mechanism and stability. Hemecontaining peroxidases catalyze the formation of the hypohalous acid by a redox mechanism, whereas in vanadatecontaining peroxidases the transition metal does not change its redox state (5, 6) but may function as a Lewis acid. Vanadatecontaining haloperoxidases not only posses a very high stability (7, 8) but they also resist a high concentration of their substrate (H 2 O 2 ) (9) and their product (HOX) (7) that would readily inactivate the heme-containing peroxidases.Vanadate-containing peroxidases were first discovered in seaweeds about a decade ago (10, 11); at present they are being discovered not only in an increasing number of seaweeds (12, 13) but also in fungi (8) and in a lichen (14).The fungus Curvularia inaequalis has been shown to express a vanadium-containing CPO (V-CPO) (15), and recently the gene encoding this enzyme was cloned and sequenced (16). The V-CPO gene codes for a protein of 609 amino acids with a calculated molecular mass of 67,488 kDa. Database searches using the entire V-CPO sequence showed very little sequence similarity to other known proteins (16). The recent determination of the crystal structure of this enzyme at 2.1-Å resolution (17) revealed that the protein has an overall cylindrical shape and measures approximately 50 ϫ 80 Å. Th...

show abstract

mentioning

confidence: 99%

From phosphatases to vanadium peroxidases: A similar architecture of the active site

Hemrika¹,

Renirie²,

Dekker³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

173

164

View full text Add to dashboard Cite

show abstract

“…Chlorination of indole to 3-chloroindole by CPO-F. Chlorination of indole was performed as described by Bantleon et al (1994) with 0.1 mM indole, 100 mM NaC1, 29 mM H 2 0 2 in a total volume of 10 ml of 1 M sodium acetate buffer, pH 4.5. The reaction was started by addition of 1 U of brominating activity of CPO-F and incubated at room temperature.…”

Section: Nucleotide [Ttt(c)tat(c)aaa(g)gat(c)tgg Gg] Thatmentioning

confidence: 99%

The non-haem chloroperoxidase from Pseudomonas fluorescens and its relationship to pyrrolnitrin biosynthesis

et al. 1996

View full text Add to dashboard Cite

The non-haem chloroperoxidase gene (cpoF) from the pyrrolnitrin producer Pseudomonas fluorescens BL914 was cloned using an oligonucleotide derived from part of the N-terminal amino acid sequence of chloroperoxidase (CPO-P) from Pseudomonas pyrrocina as a probe. Based on the overexpression of cpoF in Escherichia coli and the stabilty of CPO-F against higher temperatures and proteases, the enzyme was purified to homogeneity. Partial characterization of the enzyme showed that it belongs to the class of bacterial non-haem CPOs. To investigate the role of CPO-F in pyrrolnitrin biosynthesis, the cpof gene was inactivated by insertion of a kanamycin cassette. Exchange of the chromosomal cpoF gene against the disrupted copy had no influence on pyrrolnitrin production demonstrating that CPO-F was not involved in pyrrolnitrin biosynthesis.

show abstract

“…For example, the chloroperoxidase from Streptomyces Zividans does not contain metal ions and in the absence of absorption in the Soret band of the spectrum is assumed not to contain protoporphyrin [ 11]. In addition, it is not associated with the synthesis of chlorinated metabolites.…”

Section: Fadh 2 -Dependent Chlorohalogenasesmentioning

confidence: 97%

“…4. Even when enzymatic activity is present, there may be no evidence for the presence of halogenated metabolites in the organism, for example, the Chloroperoxidase from Streptomyces Zividans [11].…”

Section: Pyrrociniacus Streptomycesmentioning

confidence: 98%

Biological Effects and Biosynthesis of Brominated Metabolites

Neilson

2003

The Handbook of Environmental Chemistry

View full text Add to dashboard Cite

Abstract. On the basis of halogenated metabolites assembled by Gribble, an attempt is made to provide a hypothesis for the biosynthesis of representative groups. Examples of brominated and iodinated metabolites are drawn from the major classes of terpenoids and acetogenins, and related to the biosynthesis of their putative precursors. Brominated and iodinated carbocyclic and heterocyclic aromatic compounds are discussed as weil as mechanisms for the oxidative coupling of phenolic substrates. A few chlorinated metabolites are introduced for additional illustration. Halogenation by cationoid (Hai+) reactions catalyzed by haloperoxidases is discussed, and attention drawn to the alternative role of anionoid (Hal-) halogenation. The presentation is extended to the biosynthesis of isonitriles and dichloroimines by anionoid reaction of precursors with cyanide. The range of biota that produce brominated substrates is briefly indicated, and comments made on the ecological significance of metabolites and associations among biota.

show abstract

Chloroperoxidase from Streptomyces lividans: isolation and characterization of the enzyme and the corresponding gene

Cited by 60 publications

References 39 publications

From phosphatases to vanadium peroxidases: A similar architecture of the active site

From phosphatases to vanadium peroxidases: A similar architecture of the active site

The non-haem chloroperoxidase from Pseudomonas fluorescens and its relationship to pyrrolnitrin biosynthesis

Biological Effects and Biosynthesis of Brominated Metabolites

Contact Info

Product

Resources

About