Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “PEROXIDASES”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 1,009 records · Page 56Linked to original sources
PubMed1990

Iodothyronine-induced catalatic activity of thyroid peroxidase.

Iodothyronines induced catalatic (H2O2-decomposing) activity of thyroid peroxidase and lactoperoxidase, the effect increasing in the order of thyroxine (T4) greater than triiodothyronine (T3) greater than diiodothyronine (T2). The iodothyronines served as electron donors in the peroxidase reactions, and during the reactions the catalytic intermediate of thyroid peroxidase was confirmed to be Compound II for T4 and Compound I for T3 and T2 and from the Soret absorption spectra obtained by stopped-flow measurements. Rate constants for the reactions between T4 and Compound II, T3 and Compound I, and T2 and Compound I were estimated at 1.9 x 10(5), 1.3 x 10(6), and 7.1 x 10(5) M-1.s-1, respectively. Unlike the case of thyroid peroxidase, the catalytic intermediate of lactoperoxidase observed during the oxidation of iodothyronines was invariably Compound II. From these and other data it was concluded that thyroid peroxidase catalyzed one-electron oxidation of T4 and two-electron oxidations of T2 and T3 while lactoperoxidase catalyzed exclusively one-electron oxidation of the iodothyronines. Iodide was released during the enzymatic oxidation of iodothyronines, irrespective of the mechanism of one-electron and two-electron oxidations. The amount of released iodide increased in the order of T4 greater than T3 greater than T2. The iodothyronines-induced catalatic activity of these peroxidases was ascribable to the release of iodide, but it was also found that the iodide-enhanced catalatic activity was stimulated by iodothyronines. In this case the effect of iodothyronines was greater in the order of T2 greater than T3 greater than T4, which was consistent with the order of iodothyronine activation for the iodinium cation transfer from enzyme to acceptor.

Animals↗
PubMed1985

An improved assay method for thyroid peroxidase applicable for a few milligrams of abnormal human thyroid tissues.

A peroxidase assay method (Mini assay method) which is applicable for a minute amount (as small as a few mg) of thyroid tissue was developed, employing guaiacol or iodide as the second substrate. This method is a modification of the previous one (Ordinary assay method): the volume of the reaction mixture was reduced to about one-tenth with prior solubilization of the enzyme. The correlation between the Mini assay and Ordinary assay methods, and between the guaiacol and iodide assays by both methods were satisfactorily good, but the iodine content of thyroglobulin was found to be not directly correlated to the peroxidase activities. Protein-based specific activities of peroxidase from normal human thyroid tissue were about 0.030 guaiacol units/mg protein and 0.0066 iodide units/mg protein, which were slightly higher than those of porcine thyroid tissue. The Mini assay method developed in the present study was used for the determination of peroxidase activity in a small amount (1-8 mg) of thyroid tissue obtained by means of a needle biopsy from patients with thyroid disorders. One specimen (goitrous cretinism) showed no peroxidase activity in both the guaiacol and iodide assays, and three specimens (two chronic thyroiditis, one familial nontoxic goiter) possessed no ability to catalyze the oxidation of iodide in spite of the high reactivity towards guaiacol, suggesting the presence of an abnormal peroxidase in these tissues.

Animals↗
PubMed2002

Characterization of a Pinus pinaster cDNA encoding an auxin up-regulated putative peroxidase in roots.

As part of a study to identify host plant genes regulated by fungal auxin during ectomycorrhiza formation, we differentially screened a cDNA library constructed from roots of auxin-treated Pinus pinaster (Ait.) Sol. seedlings. We identified three cDNAs up-regulated by auxin. Sequence analysis of one of these cDNAs, PpPrx75, revealed the presence of an open reading frame of 216 amino acids with the characteristic consensus sequences of plant peroxidases. The deduced amino acid sequence showed homology with Arabidopsis thaliana (L.) Heynh., Arachis hypogaea L. and Stylosanthes humilis HBK cationic peroxidases. Amino acid sequence identities in the conserved domains of plant peroxidases ranged from 60 to 100%. In PpPrx75, there are five cysteine residues and one histidine residue that are found at conserved positions among other peroxidases. A potential glycosylation site (NTS) is present in the deduced sequence. Phylogenetic analysis showed that PpPrx75 is closely related to two A. thaliana peroxidases. The PpPrx75 cDNA was induced by active auxins, ethylene, abscisic acid and quercetin, a flavonoid possibly involved in plant-microorganism interactions. Transcript accumulation was detected within 3 h following root induction by auxin, and the amount of mRNA increased over the following 24 h. The protein synthesis inhibitor cycloheximide did not inhibit indole-3-acetic acid-induced transcript accumulation, suggesting that PpPrx75 induction is a primary (direct) response to auxin. This cDNA can be used to study expression of an auxin-regulated peroxidase during ectomycorrhiza formation.

Amino Acid Sequence↗
PubMed1997

Differential induction of a peroxidase gene family during infection of rice by Xanthomonas oryzae pv. oryzae.

Induction of peroxidase has been correlated with resistant interactions between rice and Xanthomonas oryzae pv. oryzae. To assist in analysis of the role of rice peroxidases in plant defense against the bacterial pathogen, three peroxidase genes, POX22.3, POX8.1, and POX5.1, were identified from a rice cDNA library that was constructed from leaves of plants undergoing a resistant reaction. These genes were highly similar in nucleic acid and amino acid sequences and belonged to a gene family. The three genes showed differential expression in infiltrated rice leaves during pathogen interactions and mechanical stress. Only two peroxidase genes, POX8.1 and POX22.3, were predominantly expressed during resistant interactions. These two genes also were expressed during susceptible interactions, but induction was delayed compared with resistant interactions. POXgX9, a fourth peroxidase gene that was isolated from a genomic library, is adjacent to POX22.3 in the rice genome and has greater than 90% similarity in nucleotide and amino acid sequence identity to POX22.3. Interestingly, POXgX9 was expressed only in the roots of rice plants. While POX22.3 was expressed in both leaves and roots, POX8.1 and POX5.1 were not detected in roots but were induced in leaves by mechanical wounding at different times after treatment. POX22.3, POX8.1, and POX5.1 were estimated to be present in single copies in rice haploid genome. These results indicate that different members of the rice peroxidase gene family are distinctly regulated in response to various environmental cues.

Amino Acid Sequence↗
PubMed2003

Activity of class III peroxidases in the defense of cotton to bacterial blight.

Cotton cotyledons displayed a hypersensitive reaction (HR) in the cultivar Réba B50 after infiltration with the avirulent race 18 from Xanthomonas campestris pv. malvacearum. Two sets of peroxidases were associated with the HR time course. Early but transient accumulation of peroxidase in material encapsulating the bacteria in intercellular areas was observed by immunocytochemistry at 3 h postinfection and coincided with the oxidative burst. Total guaiacol-peroxidase activity was highly increased in cells undergoing HR, from 12 h after treatment. Molecular characterization of seven cloned peroxidase genes revealed highly conserved B, D, and F domains, with similarities to plant class III peroxidases. Analysis of gene expression showed variation in transcript accumulation during both compatible (race 20) and incompatible interactions for four of these genes: pod2, pod3, pod4, and pod6. Pod4 and pod6 were more intensely up-regulated during resistance than during disease and in the control, while pod3 was specifically down-regulated during the HR after the oxidative burst. Pod2 was induced by pathogen infection and weakly stimulated in the control. These data suggest that cotton peroxidases may have various functions in the defense response to Xanthomonas infections.

Amino Acid Sequence↗
PubMed1996

KatP, a novel catalase-peroxidase encoded by the large plasmid of enterohaemorrhagic Escherichia coli O157:H7.

A gene coding for a catalase-peroxidase activity was identified on a 9-7 kb Smal DNA fragment derived from the large plasmid pO157 of enterohaemorrhagic Escherichia coli (EHEC) O157:H7 strain EDL 933. Nucleotide sequencing revealed an ORF of 2208 bp and predicted a 736 amino acid polypeptide with a molecular mass of 81.8 kDa. This putative protein was found to be highly homologous to members of the bacterial bifunctional catalase-peroxidase family. Analysis of its amino acid sequence revealed the presence of characteristic peroxidase 1 and 2 motifs. In addition, an N-terminal signal sequence was found, suggesting that the catalase-peroxidase is transported through the cytoplasmic membrane. EHEC catalase-peroxidase activities were investigated in cytoplasmic and periplasmic crude extracts as well as in culture supernatants from wild-type and recombinant E. coli strains. EHEC-specific catalase-peroxidase activity was detected primarily in the periplasm in strain EDL 933. The newly discovered enzyme was designated KatP, to indicate its plasmid origin. PCR analysis of representative strains of all enteric E. coli pathogroups (i.e. enterohaemorrhagic, enterotoxigenic, enteropathogenic, enteroaggregative and enteroinvasive E. coli) revealed a close association between the occurrence of EHEC-haemolysin and the katP gene in Shiga-like-toxin-producing E. coli O157 strains.

Amino Acid Sequence↗
PubMed2006

The role of hydrogen peroxide-producing and hydrogen peroxide-consuming peroxidases in the leaf apoplast of cowpea in manganese tolerance.

The apoplast is considered the leaf compartment decisive for manganese (Mn) toxicity and tolerance in cowpea (Vigna unguiculata). Particularly apoplastic peroxidases (PODs) were proposed to be key enzymes in Mn toxicity-induced processes. The presented work focuses on the characterization of the role of hydrogen peroxide (H2O2)-producing (NADH peroxidase) and H2O2-consuming peroxidase (guaiacol POD) in the apoplastic washing fluid (AWF) of leaves for early stages of Mn toxicity and genotypic differences in Mn tolerance of cowpea. Leaf AWF of the Mn-sensitive cultivar (cv) TVu 91 but not of the Mn-tolerant cv 1987 showed an increase of guaiacol-POD and NADH-peroxidase activities at elevated AWF Mn concentrations. two-dimensional resolutions of AWF proteins revealed that cv TVu 91 expressed more and additional proteins at high Mn treatment, whereas Mn-tolerant cv TVu 1987 remained nearly unaffected. In both cultivars, NADH-peroxidase activity and accompanied H2O2 formation rate in vitro were significantly affected by Mn2+, p-coumaric acid, and metabolites occurring in the AWF. The total phenol concentration in the AWF was indicative of advanced stages of Mn toxicity but was rather unrelated to early stages of Mn toxicity and genotypic differences in Mn tolerance. The NADH oxidation by AWF PODs was significantly delayed or enhanced in the presence of the protein-free AWF from cv TVu 1987 or cv TVu 91, respectively. High-performance liquid chromatography analysis of AWF indicates the presence of phenols in cv TVu 1987 not observed in cv TVu 91. We conclude from our studies that the H2O2-producing NADH peroxidase and its modulation by stimulating or inhibiting phenolic compounds in the leaf apoplast play a major role for Mn toxicity and Mn tolerance in cowpea.

Fabaceae↗
PubMed1998

Purification and characterization of peroxidases correlated with lignification in poplar xylem.

Lignin is an integral cell wall component of all vascular plants. Peroxidases are widely believed to catalyze the last enzymatic step in the biosynthesis of lignin, the dehydrogenation of the p-coumaryl alcohols. As the first stage in identifying lignin-specific peroxidase isoenzymes, the classical anionic peroxidases found in the xylem of poplar (Populus trichocarpa Trichobel) were purified and characterized. Five different poplar xylem peroxidases (PXP 1, PXP 2, PXP 3-4, PXP 5, and PXP 6) were isolated. All five peroxidases were strongly glycosylated (3.6% to 4.9% N-glucosamine), with apparent molecular masses between 46 and 54 kD and pI values between pH 3.1 and 3.8. Two of the five isolated peroxidases (PXP 3-4 and PXP 5) could oxidize the lignin monomer analog syringaldazine, an activity previously correlated with lignification in poplar. Because these isoenzymes were specifically or preferentially expressed in xylem, PXP 3-4 and PXP 5 are suggested to be involved in lignin polymerization.

Amino Acid Sequence↗
PubMed1979

Ultrastructural localization of peroxidases in 'undifferentiated' blasts during the blast crisis of chronic granulocytic leukaemia.

Twelve cases of Philadelphia chromosome positive chronic granulocytic leukaemia (CGL) in blast transformation have been investigated using ultrastructural peroxidase detection. In all cases, the leukaemic blasts were negative for myeloperoxidase on the basis of standard cytochemistry. In nine cases a variable proportion of blasts contained peroxidase activity detectable only by electron microscopy, permitting definition of their myeloid nature. By their distinct characteristics and localization, different peroxidase activities were recognized. Thus, several types of blasts were identified: megakaryoblasts (MKB), basophil promyelocytes (BPM), myeloid blasts with small granules containing peroxidase (MyB), and proerythroblasts (ProE). MKB were predominant in two cases and present in four cases, mixed with other myeloid blasts. BPM were abundant in one case and present in seven cases. MyB were identified as a majority in four cases. Three cases remained without any peroxidase. It is concluded that ultrastructural detection of peroxidases is of value for the identification of early myeloid blasts. Their high incidence and the simultaneous presence of several myeloid precursors suggest that during the blast crisis the target cell is frequently a pluripotent myeloid stem cell.

Bone Marrow↗
PubMed2006

Peroxidase-dependent apoplastic oxidative burst in Arabidopsis required for pathogen resistance.

The oxidative burst is an early response to pathogen attack leading to the production of reactive oxygen species (ROS) including hydrogen peroxide. Two major mechanisms involving either NADPH oxidases or peroxidases that may exist singly or in combination in different plant species have been proposed for the generation of ROS. We identified an Arabidopsis thaliana azide-sensitive but diphenylene iodonium-insensitive apoplastic oxidative burst that generates H(2)O(2) in response to a Fusarium oxysporum cell-wall preparation. Transgenic Arabidopsis plants expressing an anti-sense cDNA encoding a type III peroxidase, French bean peroxidase type 1 (FBP1) exhibited an impaired oxidative burst and were more susceptible than wild-type plants to both fungal and bacterial pathogens. Transcriptional profiling and RT-PCR analysis showed that the anti-sense (FBP1) transgenic plants had reduced levels of specific peroxidase-encoding mRNAs, including mRNAs corresponding to Arabidopsis genes At3g49120 (AtPCb) and At3g49110 (AtPCa) that encode two class III peroxidases with a high degree of homology to FBP1. These data indicate that peroxidases play a significant role in generating H(2)O(2) during the Arabidopsis defense response and in conferring resistance to a wide range of pathogens.

Arabidopsis↗
PubMed1994

The effect of the Asn82-->Asp mutation in yeast cytochrome c peroxidase studied by proton NMR spectroscopy.

Proton NMR studies of the mutant of baker's yeast cytochrome c peroxidase-cyanide with the Asn 82-->Asp mutation ([N82D]cytochrome c peroxidase-CN) are presented and compared to the wild-type enzyme. This mutation alters an amino acid that forms a hydrogen bond to His52, the distal histidine residue that interacts in the heme pocket with heme-bound ligands. His52 is an important participant in the initial hydrogen peroxide decomposition step of cytochrome c peroxidase. In wild-type cytochrome c peroxidase-CN, His52 hydrogen bonds to the neighboring Asn82 peptide carbonyl group and to heme-coordinated cyanide. His52 thus manifests itself as an extensively hydrogen bonded histidinium moiety. The principal result from this study is the observation that three hyperfine-shifted resonances disappear from the spectrum of [N82D] cytochrome c peroxidase-CN compared to the wild-type enzyme. All three absent resonances in [N82D]cytochrome c peroxidase-CN belong to His52 and this leads to the conclusion that the result of the mutation has been elimination of the His52-Asn82 and His52-heme-coordinated cyanide hydrogen bonds.

Asparagine↗
PubMed1995

Disulfide bonds and glycosylation in fungal peroxidases.

Four conserved disulfide bonds and N-linked and O-linked glycans of extracellular fungal peroxidases have been identified from studies of a lignin and a manganese peroxidase from Trametes versicolor, and from Coprinus cinereus peroxidase (CIP) and recombinant C. cinereus peroxidase (rCIP) expressed in Aspergillus oryzae. The eight cysteine residues are linked 1-3, 2-7, 4-5 and 6-8, and are located differently from the four conserved disulfide bridges present in the homologous plant peroxidases. CIP and rCIP were identical in their glycosylation pattern, although the extent of glycan chain heterogeneity depended on the fermentation batch. CIP and rCIP have one N-linked glycan composed only of GlcNAc and Man at residue Asn142, and two O-linked glycans near the C-terminus. The major glycoform consists of single Man residues at Thr331 and at Ser338. T. versicolor lignin isoperoxidase TvLP10 contains a single N-linked glycan composed of (GlcNAc)2Man5 bound to Asn103, whereas (GlcNAc)2Man3 was found in T. versicolor manganese isoperoxidase TvMP2 at the same position. In addition, mass spectrometry of the C-terminal peptide of TvMP2 indicated the presence of five Man residues in O-linked glycans. No phosphate was found in these fungal peroxidases.

Amino Acid Sequence↗
PubMed1996

Probing the aromatic-donor-binding site of horseradish peroxidase using site-directed mutagenesis and the suicide substrate phenylhydrazine.

The haem groups from two classes of site-directed mutants of horseradish peroxidase isoenzyme C (HRP-C) (distal haem pocket mutants, [H42L]HRP-C* and [R38K]-HRP-C* and peripheral-haem-access-channel mutants, [F142A]HRP-C* and [F143A]HRP-C*) were extracted and analysed by reverse-phase HPLC after phenylhydrazine-induced suicide inactivation. The relative abundance of the two covalently modified haems, C20-phenyl (delta-meso phenyl) and C18-hydroxymethyl haem, provided a sensitive topological probe for changes induced in the protein architecture in the vicinity of the haem active site and substrate-access channel. Although differing considerably in their efficiency as peroxidases ([H42L]HRP-C* exhibited only approximately 0.03% of the peroxidase activity of wild type), the variants studied gave rise to a modification pattern typical of an exposed haem edge thereby strengthening the argument that it is the overall protein topology rather than the intrinsic catalytic activity of the active site that determines the sites of covalent haem modification. Mutants which showed impaired ability to bind the aromatic donor benzhydroxamic acid were less readily modified by the phenyl radical at the haem C18-methyl position although the level of arylation at the haem C20 position remained remarkable constant. Our findings suggest that the overall efficacy of haem modification catalysed by HRP-C during turnover with phenylhydrazine and its vulnerability towards inactivation are related to its general ability to bind aromatic donor molecules. Results from phenylhydrazine treatment of HRP-C wild-type and mutant variants were compared with those obtained for Coprinus cinereus peroxidase, an enzyme which from its structure is known to have a remarkably open access channel to the haem edge. We show evidence that C. cinereus peroxidase is able to bind benzhydroxamic acid, albeit with a relatively high Kd (Kd 3.7 mM), a probe for aromatic-donor binding. We suggest reasons why phenylhydrazine-treated C. cinereus peroxidase was more resistant to haem modification and phenyl-radical-based inactivation than HRP-C.

Binding Sites↗
PubMed1993

Biliary hyperpressure in rat extrahepatic cholestasis alters horseradish peroxidase biliary excretion.

1. The authors investigated the effect of two extrahepatic cholestasis models (one by bile duct ligation and the other by choledocho-jugular fistula) on the hepatic clearance of horseradish peroxidase in male Sprague-Dawley rats divided into four groups. 2. In groups A (n = 5 rats) and B (n = 5), bile duct ligation was performed, while a choledocho-jugular fistula was created in groups C (n = 5) and D (n = 7). A 10 mg intravenous bolus of horseradish peroxidase was injected after 24 h (groups A and C), 48 h (groups B and D) or 1 h (Group E; five sham-operated rats). Serum and bile samples were then serially collected for 2 h. 3. In all groups, serum horseradish peroxidase levels increased soon after injection and then rapidly decreased, the curves being similar. Biliary excretion increased for 30 min and then slowly decreased. The highest horseradish peroxidase biliary concentrations and outputs were found in Group B followed by Group A; both groups had significantly higher levels than Group E. No difference was found between horseradish peroxidase biliary excretion of groups C and D and that of sham-operated rats. 4. When each group was considered separately, sampling times correlated with the corresponding ratios of bile/plasma HRP. Significant differences were found between the relative slopes of groups A, B and E, but not between those of groups C, D and E. 5. In conclusion, bile duct obstruction greatly affects the plasma-bile transfer of fluid phase markers, such as horseradish peroxidase, while single retention, caused by choledocho-jugular fistula, has no influence.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1994

Homologous expression of recombinant manganese peroxidase in Phanerochaete chrysosporium.

The promoter region of the glyceraldehyde-3-phosphate dehydrogenase gene (gpd) was used to drive expression of mnp1, the gene encoding Mn peroxidase isozyme 1, in primary metabolic cultures of Phanerochaete chrysosporium. A 1,100-bp fragment of the P. chrysosporium gpd promoter region was fused upstream of the mnp1 gene to construct plasmid pAGM1, which contained the Schizophyllum commune ade5 gene as a selectable marker. pAGM1 was used to transform a P. chrysosporium ade1 auxotroph to prototrophy. Ade+ transformants were screened for peroxidase activity on a solid medium containing high carbon and high nitrogen (2% glucose and 24 mM NH4 tartrate) and o-anisidine as the peroxidase substrate. Several transformants that expressed high peroxidase activities were purified and analyzed further in liquid cultures. Recombinant Mn peroxidase (rMnP) was expressed and secreted by transformant cultures on day 2 under primary metabolic growth conditions (high carbon and high nitrogen), whereas endogenous wild-type mnp genes were not expressed under these conditions. Expression of rMnP was not influenced by the level of Mn in the culture medium, as previously observed for the wild-type Mn peroxidase (wtMnP). The amount of active rMnP expressed and secreted in this system was comparable to the amount of enzyme expressed by the wild-type strain under ligninolytic conditions. rMnP was purified to homogeneity by using DEAE-Sepharose chromatography, Blue Agarose chromatography, and Mono Q column chromatography. The M(r) and absorption spectrum of rMnP were essentially identical to the M(r) and absorption spectrum of wtMnP, indicating that heme insertion, folding, and secretion were normal.(ABSTRACT TRUNCATED AT 250 WORDS)

Base Sequence↗
PubMed1998

Characterization of laccases and peroxidases from wood-rotting fungi (family Coprinaceae).

Panaeolus sphinctrinus, Panaeolus papilionaceus, and Coprinus friesii are described as producers of ligninolytic enzymes. P. papilionaceus and P. sphinctrinus both produced a laccase. In addition, P. sphinctrinus produced a manganese peroxidase. C. friesii secreted a laccase and two peroxidases similar to the peroxidase of Coprinus cinereus. The purified laccases and peroxidases were characterized by broad substrate specificities, significant enzyme activities at alkaline pH values, and remarkably high pH optima. The two peroxidases of C. friesii remained active at pH 7.0 and 60 degrees C for up to 60 min of incubation. The peroxidases were inhibited by sodium azide and ethylene glycol-bis (beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA), whereas the laccases were inhibited by sodium azide and N,N-diethyldithiocarbamic acid. As determined by native polyacrylamide gel electrophoresis and isoelectric focusing, all three fungi produced laccase isoenzymes.

Amino Acid Sequence↗
PubMed1999

Regulation of peroxidase transcript levels in liquid cultures of the ligninolytic fungus Pleurotus eryngii.

A versatile peroxidase able to oxidize Mn(2+) as well as phenolic and nonphenolic aromatic compounds is produced in peptone-containing liquid cultures of Pleurotus eryngii encoded by the gene mnpl. The regulation of its transcript levels was investigated by Northern blotting of total RNA. High-peroxidase transcripts and activity were found in cultures grown in glucose-peptone medium, whereas only basal levels were detected in glucose-ammonium medium. The addition of more than 25 microM Mn(2+) to the former medium did not result in detectable peroxidase transcripts or activity. Potential regulators were also added to isolated mycelium. In this way, it was shown that high transcript levels (in peroxidase-expressing mycelium) were maintained on peptone, whereas expression was not induced in short-term incubation experiments. Similar results were obtained with Mn(2+) ions. Strong induction of mnpl expression was caused by exogenous H(2)O(2) or by continuous H(2)O(2) generation during redox cycling of menadione. By the use of the latter system in the presence of Fe(3+), which catalyzes the reduction of H(2)O(2) to hydroxyl radical, it was shown for the first time that the presence of this strong oxidant causes a rapid increase of the transcripts of a ligninolytic peroxidase. In conclusion, peptone and Mn(2+) affect the levels of transcripts of this versatile peroxidase in culture, and reduced oxygen species induce short-term expression in isolated mycelium, probably via a stress response mechanism.

Gene Expression Regulation, Enzymologic↗
PubMed1972

Mouse splenic peroxidase and its role in bactericidal activity.

Spleen cell suspensions from AKR and CD-1 mice contain peroxidase activity as determined by guaiacol oxidation. This activity is found predominately in the 20,000 x g pellet fraction of spleen cell homogenates. In the presence of H(2)O(2) and chloride ion at acidic pH, splenic peroxidase mediates the oxidation of d- or l-alanine to CO(2), NH(3), and acetaldehyde. The same reaction mixture without added amino acid can kill both gram-positive and gram-negative bacteria. The conditions for both reactions are similar. Both have an absolute requirement for H(2)O(2) and chloride ion, neither is active at neutral or alkaline pH, and both are inhibited by the sulfonic amino acid taurine. In these aspects, splenic peroxidase is qualitatively similar in its activity to myeloperoxidase (MPO) from polymorphonuclear leukocytes. It is quantitatively different from MPO in that the latter is more potent on a per guaiacol unit basis with respect to both amino acid oxidation and bactericidal activity. Still another quantitative difference is that splenic peroxidase requires 0.1 m NaCl for activity, whereas MPO functions with as little as 0.005 m NaCl. Splenic peroxidase and MPO both appear to differ qualitatively from horseradish peroxidase in that the latter enzyme does not mediate amino acid oxidation.

Alanine↗