Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme

Ritch, Thomas G.; Nipper, Valerie; Akileswaran, Lakshmi; Smith, Alan Jay; Pribnow, David; Gold, Michael H.

doi:10.1016/0378-1119(91)90304-t

Cited by 49 publications

(30 citation statements)

References 55 publications

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“…DyP degraded phenolic compounds, such as 2,6-dimethoxyphenol and guaiacol, while it did not degrade nonphenolic veratryl alcohol (14). Considering its substrate specificity and molecular mass, DyP was found to be a novel peroxidase distinct from other peroxidases reported previously (25,26,28,41). Furthermore, the absorption spectrum of DyP exhibited a Soret band at 406 nm corresponding to a hemoprotein, and its Na 2 S 2 O 4 -reduced form revealed a peak at 556 nm that indicates the presence of a protoheme as its prosthetic group (14).…”

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confidence: 81%

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Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Sugano

Nakano

Sasaki

et al. 2000

Appl Environ Microbiol

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Efficient expression of the dye-decolorizing peroxidase, DyP, from Geotrichum candidum Dec 1 in Aspergillus oryzae M-2-3 was achieved by fusing mature cDNA encoding dyp with the A. oryzae ␣-amylase promoter (amyB). The activity yield of the purified recombinant DyP (rDyP) was 42-fold compared with that of the purified native DyP from Dec 1. No exogenous heme was necessary for the expression of rDyP in A. oryzae. From the N-terminal amino acid sequence analyses of native DyP and rDyP, the absence of a histidine residue in both DyPs, which was considered to be important for heme binding of DyP, was confirmed. These results suggest that rDyP without a typical heme-binding region produced by A. oryzae exhibits a function similar to that of native DyP.The newly isolated Geotrichum candidum Dec 1 was found to decolorize 21 kinds of synthetic dyes (13), and its degradation spectrum in relation to synthetic dyes is wider than that of any other decolorizing organisms reported so far. In our previous study, an extracellular enzyme, DyP (for dye-decolorizing peroxidase), was found to be responsible for the decolorization of dyes. DyP degraded phenolic compounds, such as 2,6-dimethoxyphenol and guaiacol, while it did not degrade nonphenolic veratryl alcohol (14). Considering its substrate specificity and molecular mass, DyP was found to be a novel peroxidase distinct from other peroxidases reported previously (25,26,28,41). Furthermore, the absorption spectrum of DyP exhibited a Soret band at 406 nm corresponding to a hemoprotein, and its Na 2 S 2 O 4 -reduced form revealed a peak at 556 nm that indicates the presence of a protoheme as its prosthetic group (14). We also reported the cloning of cDNA of the dyp gene (32).So far, several microorganisms capable of decolorizing some synthetic dyes have been reported (17-20, 22, 23). In particular, the white-rot fungus Phanerochaete chrysosporium was extensively studied as a dye-decolorizing fungus (5,9,19,20,21,30) and several lignin peroxidases (LiPs) of P. chrysosporium have been reported to show decolorizing activity. However, their decolorizing spectrum toward dyes is not extensively investigated, mainly because research on their lignin-degrading reaction is focused. Furthermore, although cloning and expression of several LiPs have been reported (6,11,29), there is no report on the enhancement of the yield of these enzymes by heterologous expression.Therefore, we focused on producing a large amount of DyP having dye-decolorizing activity in Aspergillus oryzae under the control of the amyB promoter. A. oryzae is known to exhibit a high growth rate and to be a safe host (1); furthermore, it can secrete gram-per-liter quantities of heterologous protein (4). From this study and our previous data, we show that DyP is a unique peroxidase.Chemicals, enzymes, and other materials. Ten kinds of synthetic dyes kindly provided by Nippon Kayaku Co., Ltd. (Tokyo, Japan), and Bayer Japan Co., Ltd. (Tokyo, Japan), were used. Cellulase and lysing enzymes were obtained from SigmaAldrich Japan...

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confidence: 81%

“…Class I peroxidases are from the procaryotic lineage (12,39). Class II peroxidases are secretory fungal peroxidases (25,26,28). Class III peroxidases are classical, secretory plant peroxidases (38,41).…”

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confidence: 99%

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Sugano

Nakano

Sasaki

et al. 2000

Appl Environ Microbiol

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“…Other authors [18,32] refer to the isoenzyme's pI ; LiP H8, with a pI of 4.15, is known as LIP415. Others use their own numbering scheme ; Ritch et al [33], for example, refer to LiP H8 (LIP415) as LiP2. This issue is further confused by reports that some isoenzymes are genetically distinct [34,35] while others differ solely in the degree of glycosylation or phosphorylation and may be interconverted [36].…”

Section: Introductionmentioning

confidence: 99%

Reversible alkaline inactivation of lignin peroxidase involves the release of both the distal and proximal site calcium ions and bishistidine co-ordination of the haem

George

Kvaratskhelia

Dilworth

et al. 1999

Biochemical Journal

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Phanerochaete chrysosporium lignin peroxidase isoenzyme H2 (LiP H2) exhibits a transition to a stable, inactive form at pH 9.0 with concomitant spectroscopic changes. The So$ ret peak intensity decreases some 55 % with a red shift from 408 to 412 nm ; the bands at 502 nm and 638 nm disappear and the peak at 536 nm increases. The EPR spectrum changes from a signal typical of high spin ferric haem to an exclusively low spin spectrum with g l 2.92, 2.27, 1.50. These data indicate that the active pentacoordinated haem is converted into a hexaco-ordinated species at alkaline pH. Room temperature near-IR MCD data coupled with the EPR spectrum allow us to assign the haem co-ordination of alkali-inactivated enzyme as bishistidine. Re-acidification of the alkali-inactivated enzyme to pH 6 induces further spectroscopic changes and generates an irreversibly inactivated species. By contrast, a pH shift from 9.0 to 6.0 with simultaneous addition of 50 mM CaCl # results in the recovery of the initial

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“…With respect to secretion, the cDNA sequences identified for lignin peroxidase Lip (Tien & Tu, 1987;De Boer et al, 1987;Holzbaur et al, 1989;Ritch et al, 1991) or MnP (Pribnow et al, 1989;Pease et al, 1989) of P. chrysosporium predict the synthesis of preproteins with hydrophobic signal peptides. In addition, a LIP isoenzyme has been shown to be synthesized as a preproprotein (Ritch et al, 1991).…”

Section: Introductionmentioning

confidence: 99%

“…In addition, a LIP isoenzyme has been shown to be synthesized as a preproprotein (Ritch et al, 1991). Enhanced secretion of peroxidases was observed by adding phospholipids to the medium and was correlated with proliferation of endoplasmic reticulum and mitochondria as shown by the activities of marker enzymes (Capdevila et al, 1990).…”

Section: Introductionmentioning

confidence: 99%

In situ localization of the secretion of lignin peroxidases in colonies of Phanerochaete chrysosporium using a sandwiched mode of culture

Moukha¹,

Wösten

Asther³

et al. 1993

Journal of General Microbiology

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~Protein secretion and growth were investigated in Phanerochaete chrysospovitlm by using cultures sandwiched between perforated polycarbonate membranes. Labelling of colonies with radioactive N-acetylglucosamine and Lmethionine indicated a close correlation between growth and general protein secretion, even in a central area of the colony secreting the idiophase enzymes lignin peroxidase (Lip) and manganese-dependent lignin peroxidase (MnP). Comparison of the sites of release into the medium of newly synthesized proteins and immuno-detected lignin peroxidases suggested that diffusion of the enzymes from the walls was a limiting step in the release of peroxidases into the medium. Microautoradiography of colonies exposed to N-a~etyl [~H]glucosamine revealed the apical growth of thin hyphae and branches (4 to 5 pm diameter on average) in the central secreting area. These secondary hyphae showed peroxidase activity and reacted with lignin peroxidase antibodies. Although it was not possible to directly visualize secretion at hyphal tips, the results suggest that peroxidases (Lip and MnP) are initially secreted at the apex of secondary growing hyphae and later slowly released into the surrounding medium.

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Lignin peroxidase from the basidiomycete Phanerochaete chrysosporium is synthesized as a preproenzyme

Cited by 49 publications

References 55 publications

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Efficient Heterologous Expression in Aspergillus oryzae of a Unique Dye-Decolorizing Peroxidase, DyP, of Geotrichum candidum Dec 1

Reversible alkaline inactivation of lignin peroxidase involves the release of both the distal and proximal site calcium ions and bishistidine co-ordination of the haem

In situ localization of the secretion of lignin peroxidases in colonies of Phanerochaete chrysosporium using a sandwiched mode of culture

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