Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:1.10.3.2 (laccase)
4,656 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The optimum pH for ceruloplasmin as polyphenol oxidase (EC 1.10.3.2) activity was determined in human serum (pH 5.4) and the serum of conventional laboratory animals--the rat (pH 5.2), mouse (pH 5.2), hamster (pH 5.3), guinea pig (pH 5.4), multimammate mouse (pH 5.2) and rabbit (pH 5.4). Determined at the optimum pH in 0.1M acetate buffer polyphenol oxidase activity fell in the sequence: rat--man--rabbit--mouse--multimammate mouse--hamster--guinea pig. Ceruloplasmin polyphenol oxidase activity was inhibited by 0.1M phosphate buffer in the mouse, rat and multimammate mouse, but not in the other species. It was inhibited by 0.05M citrate and 0.1M phthalate buffer in all the species tested.
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PMID:Serum polyphenol oxidase activity (ceruloplasmin) in conventional laboratory animals and man. 2 13

Binuclear cupric ion clusters have been established in: human ceruloplasmin, hemocyanin, and mushroom tyrosinase. Substantial evidence makes it very probable that fungal laccase and zucchini ascorbate oxidase contain this cluster. Some evidence makes it possible that copper clusters function in the catalytic cycles of cytochrome oxidase (mammalian) and dopamine-beta-hydroxylase. These studies throw light on the criteria which must be employed to establish the existence of functional binuclear copper clusters in enzymes: (1) Stoichiometric Criteria: binding of O2 and CO with Cu/ligand = 2; redox titrations with n = 2; (2) Physical and Chemical Criteria: magnetic evidence of diminished paramagnetism of cupric centers, EPR evidence of broadened or absent absorptions, EPR evidence of magnetic dipolar interactions among cupric ions; absorption bands characteristic of Cu(II)-Cu(II) complexes; laser resonance raman scattering characteristic of peroxidic dioxygen in the oxyforms.
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PMID:Binuclear copper clusters as active sites for oxidases. 18 78

Phenol oxidase of Fasciola gigantica exists both as the soluble form as well as the membrane-bound form. The membrane-bound enzyme is considered to be a tyrosinase type because it is capable of oxidizing mono- and diphenol and is inefficient in oxidizing paraphenols. The soluble enzyme is a laccase type showing more affinity to various diphenols and paraphenols. Membrane-bound enzyme exists as isoenzymes, showing 3 fractions, of which the slow-moving fraction is capable of oxidizing both 4-methyl catechol and catechol, whereas the two remaining fractions are specific to 4-methyl catechol only. Soluble enzyme exists as a single homogeneous form showing affinity to both mono- and diphenols. Inhibition of the enzyme by potassium iodide and mercuric chloride indicates the active tyrosyl and SH groups of the enzyme. Inhibition of the enzyme by sodium diethyl dithiocarbamate and phenyl thiourea indicates that copper is the prosthetic group of the enzyme.
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PMID:Properties of phenol oxidase in Fasciola gigantica. 251 8

The influence of copper on the cycloheximide-induced synthesis of the copper-containing enzymes tyrosinase and laccase in Neurospora crassa was studied by enzyme activity measurements and immunological means. The amount of active enzyme molecules is far higher when the culture medium is copper-supplemented before cycloheximide induction. The synthesis of the apoproteins is not dependent on the presence of copper. This suggests the existence of a copper-storage protein for which metallothionein is a likely candidate.
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PMID:The influence of copper on the induction of tyrosinase and laccase in Neurospora crassa. 295 23

Golgi complex and endoplasmic reticulum (ER) were isolated from suspension-cultured cells of sycamore (Acer pseudoplatanus L.) by stepwise sucrose density gradient centrifugation using protoplasts as starting material. The purity of the two organelle fractions isolated was assessed by measuring marker enzyme activities. Localization of glycolipid and glycoprotein glycosyltransferase activities in the isolated Golgi and ER fractions was examined; three glycosyltransferases, i.e., galactosyltransferase, fucosyltransferase, and xylosyltransferase, proved to be almost exclusively confined to the Golgi, whereas the ER fractions contained glycolipid glycosyltransferase. The Golgi complex was further subfractionated on a discontinuous sucrose density gradient into two components, migrating at densities of 1.118 and 1.127 g/cm3. The two fractions differed in their compositional polypeptide bands discernible from Na-dodecylsulfate gel electrophoresis. Galactosyltransferase distributed nearly equally between the two protein peaks and xylosyltransferase activities using the endogenous acceptor also appeared to be localized in the two subcompartments. By contrast, fucosyltransferase, engaged in the terminal stage of glycosylation, banded in the lower density fractions. Golgi-specific alpha-mannosidase, which is presumably engaged in the sugar trimming of Asn-N-linked glycoprotein carbohydrate core, was enriched fourfold in specific activity in the fractions of the higher density. The overall experimental results indicate that the cotranslational glycosylation of Asn-N-linked glycoproteins, e.g., polyphenol oxidase (laccase), takes place in the ER, while subsequent post-translational processing of the oligosaccharide moiety proceeds successively in the two physically separable compartments of the Golgi complex.
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PMID:Golgi-specific localization of transglycosylases engaged in glycoprotein biosynthesis in suspension-cultured cells of sycamore (Acer pseudoplatanus L.). 309 42

The amino acid sequences of different copper proteins containing coupled binuclear copper centers are compared. Hemocyanins from arthropods and molluscs and tyrosinases from three different species were found to share a highly homologous region in the C-terminal parts. This region contains three invariant histidines previously identified as ligands to Cu(B) in Panulirus interruptus hemocyanin by X-ray crystallography (Gaykema et al., Nature 309, 23-29 (1984]. In contrast, the ligand environment for the second copper, Cu(A), proved to be quite variable. It is proposed that hemocyanin and tyrosinase have arisen from a common mononuclear copper protein with the typical Cu(B) site. From this ancestral protein two types of binuclear proteins evolved independently into a tyrosinase and an arthropodan hemocyanin type. The amino acid sequence comparison between human ceruloplasmin and Neurospora crassa laccase together with the results from a preliminary X-ray structure analysis of zucchini ascorbate oxidase showed a close relationship in primary and most likely also in tertiary structure in the C-terminal parts of these enzymes. It is suggested that the multicopper oxidases have evolved from an ancestral copper protein which presumably contained all the ligands required for the binding of one binuclear and two additional mononuclear metal centers.
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PMID:Evolutionary relationships among copper proteins containing coupled binuclear copper sites. 313 63

The ultrastructural localization of two types of biochemically characterized phenol oxidase activity is described in the larva of the sheep blowfly, Lucilia cuprina. Cuticular tyrosinase activity (enzyme A) is seen in epicuticular filaments and procuticle. Procuticle activity can be detected only after a presumed process of activation takes place in damaged cuticle. By using either the dopamine reaction or inducing melanization by hot-water treatment, tyrosinase is readily shown in haemopoietic tissue which, in L. cuprina, occurs subdermally as well as being associated with the dorsal vessel. The adaptation of the diaminobenzidine technique, used to stain laccase in electrophoretic gels, to ultrastructural cytochemistry has made it possible to demonstrate enzymic activity probably due to laccase (enzyme B). The laccase activity is present in the inner epicuticle of late wandering third instar larvae (about to pupariate) but is not present in the epicuticle of younger larvae.
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PMID:Ultrastructural localization of phenoloxidases in cuticle and haemopoietic tissue of the blowfly Lucilia cuprina. 314 10

Acanthamoeba castellanii has a phenol oxidase activity that is believed to be a laccase. Enzyme activity was found in the outer cyst wall, in the cytoplasm of encysting amoebae and in the encystment medium. Encystment procedures were modified to promote an increase in the amount of soluble enzyme secreted during encystation. Acanthamoeba polyphenol oxidase has a pH optimum of 6.0 and a Km value of 0.21 mM with dihydroxyphenylalanine. The enzyme does not oxidize tyrosine, and it is inhibited by chloride but not by inhibitors of peroxidase. Its synthesis coincides with encystation, and known inhibitors of polyphenol oxidase prevent encystation. Polyphenol oxidase may have a role in making the cyst resistant to mechanical and chemical breakdown.
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PMID:Polyphenol oxidase produced during encystation of Acanthamoeba castellanii. 393 Jul 6

Rapidly growing Neurospora crassa does not produce laccase (p-diphenol:oxygen oxidoreductase; EC 1.10.3.2). Low concentrations of cycloheximide induce the production of this enzyme, most of which is secreted into the media. In general, limited inhibition of protein synthesis seems to derepress laccase synthesis since actinomycin D and, to a limited extent, puromycin also induce laccase production. Similarities in the conditions of laccase and tyrosinase induction, plus investigations with two tyrosinase regulatory mutants, suggest that the production of these two phenol oxidases is controlled by the same mechanism. As shown by polyacrylamide gel electrophoresis, most of the 10 to 12 proteins normally present in the medium virtually disappear during cycloheximide treatment. In contrast, the amounts of two proteins that are present in only very minor quantities, if at all, in normal culture filtrates increase dramatically. One of these proteins co-migrates with laccase, whereas the other has not been identified.
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PMID:Induction of Neurospora crassa laccase with protein synthesis inhibitors. 427 35

The culture of Streptomyces galbus ISP-5089 has a yellow-green colour caused by the accumulation of actinomycin X when it is grown in synthetic media at 28 degrees C; the colour turns dark-brown at 42 degrees C due to the synthesis of melanoid pigments. The population composition does not undergo any noticeable changes in that case, an no specific melanin-synthesizing mutants appear as a result of autoselection . The biosynthesis of actinomycin X (at 28 degrees C) and melanoid pigments (at 42 degrees C) is regulated by temperature. At 42 degrees C, L-DOPA oxidase is synthesized and laccase is activated; these two enzymes are involved in the synthesis of melanoid pigments. The organism does not has tyrosinase. The synthesis of melanoid pigments, when the mesophilic culture of S. galbus ISP-5089 is grown in the regime of superoptimal temperatures (42 to 47 degrees C), may be considered as a protective ecological reaction of the organism to unfavourable conditions of the environment.
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PMID:[Nature of the brown pigment and the composition of the phenol oxidases of Streptomyces galbus]. 620 87


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