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)

1. Eight mutants were isolated following mutagen treatment which are deficient in laccase formation. Seven of these had a pleiotropic effect and exhibited defects in growth rate and in mycelial and sexual morphology. 2. By means of tetrad analysis the mutations were assigned to 6 loci. Three mutations were in the incolora locus, the others were non-allelic. Only two of these loci were closely linked. 3. All genes exhibit numerous interactions. These concern the morphological expression of the laccase genes and also the laccase spectra. 4. The mutants could be separated into four classes on the basis of the amount and type of laccase produced. 5. Five of the loci studied appear to be structural genes because mutations alters the physical properties of the laccase protein. The sixth gene has a regulatory role.
Mol Gen Genet 1977 Nov 18
PMID:The phenoloxidases of the ascomycete Podospora anserina. XIII. Action and interaction of genes controlling the formation of laccase. 41 70

The gene encoding laccase in the chestnut blight fungus, Cryphonectria parasitica, has been cloned and characterized. The predicted C. parasitica laccase amino acid sequence (591 aa) was 57% identical to the Neurospora crassa laccase sequence and contained four potential copper-binding regions that are conserved in a number of copper-binding proteins. Treatment of a virulent C. parasitica strain with 3 microM cycloheximide resulted in a marked increase in laccase mRNA accumulation, whereas identical treatment of an isogenic strain that contained a hypovirulence-associated virus failed to significantly increase laccase mRNA levels. In contrast, the accumulation of mRNAs encoding beta-tubulin, actin, or glyceraldehyde-3-phosphate dehydrogenase was not appreciably altered by either the presence of a hypovirulence-associated virus or treatment with cycloheximide. These results provide evidence that the expression of a specific fungal gene encoding a known protein product is selectively modulated by a hypovirulence-associated virus.
Mol Plant Microbe Interact
PMID:Molecular analysis of the laccase gene from the chestnut blight fungus and selective suppression of its expression in an isogenic hypovirulent strain. 153 23

On the basis of the spatial structure of ascorbate oxidase [Messerschmidt, A., Rossi, A., Ladenstein, R., Huber, R., Bolognesi, M., Gatti, G., Marchesini, A., Petruzzelli, R. & Finazzi-Agro, A. (1989) J. Mol. Biol. 206, 513-529], an alignment of the amino acid sequence of the related blue oxidases, laccase and ceruloplasmin is proposed. This strongly suggests a three-domain structure for laccase closely related to ascorbate oxidase and a six-domain structure of ceruloplasmin. These domains demonstrate homology with the small blue copper proteins. The relationships suggest that laccase, like ascorbate oxidase, has a mononuclear blue copper in domain 3 and a trinuclear copper between domain 1 and 3 and ceruloplasmin has mononuclear copper ions in domains 2, 4 and 6 and a trinuclear copper between domains 1 and 6.
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PMID:The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships. 240 64

The application of scanning calorimetry to investigate laccase I from the lignin-degrading basidomycete PM1 (CECT 2971) showed three thermal transitions beneath the overall endotherm following the previous heating of the sample up to 60 degrees C. The thermodynamic parameters of these three transitions satisfy a model of two-state independent unfolding, supporting a three-domain organization of the enzyme. It is shown that the catalytic site of laccase I is located in the domain with the thermally-induced transition at 76 degrees C.
Biochem Mol Biol Int 1994 Dec
PMID:Domain structure of laccase I from the lignin-degrading basidiomycete PM1 revealed by differential scanning calorimetry. 769 81

The oxidative stability of rosmarinic acid (alpha-O-caffeoyl-3,4-dihydroxyphenyllactic acid) in lavandin (Lavandula x intermedia) cell cultures was studied in an attempt to explain the decrease in the rosmarinic acid content of aging cell cultures, a process which is associated with the appearance of brown pigments. The oxidation of rosmarinic acid by a partially purified protein fraction was followed spectrophotometrically and by HPLC. The results showed that rosmarinic acid oxidation was almost totally dependent on the presence of H2O2 and protein, and that brownish products were the results of this oxidation, resembling those shown by aging cell cultures. Since this protein fraction contains peroxidase activities and shows the total absence of tropolone-sensitive polyphenoloxidase (catecholase) and laccase activities, rosmarinic acid oxidation is tentatively proposed to be caused by a peroxidase-like activity. These results support the existence of a rosmarinic acid peroxidase in cell cultures of lavandin flowers, which may be involved in the oxidative destruction of rosmarinic acid, and which may also be responsible for the formation of brown pigments during aging, lowering the yields of rosmarinic acid.
Biochem Mol Biol Int 1994 Oct
PMID:Tentative evidence of a rosmarinic acid peroxidase in cell cultures from lavandin (Lavandula x intermedia) flowers. 786 8

Detailed investigations of the EPR-active copper ion in the trinuclear type 2/type 3 cluster site of T1Hg Rhus vernicifera laccase suggest that at least some inhibitor anions bind to what was an EPR-silent copper center of the resting enzyme. The key observation is that with [15N]azide the adduct exhibits remarkably well resolved ligand hyperfine structure indicative of splitting from three protein (histidine) nitrogens and one azide nitrogen. This accords nicely with recent X-ray diffraction studies of adducts of the related enzyme, ascorbate oxidase (A. Messerschmidt, H. Luecke, and R. Huber, 1993, J. Mol. Biol. 230, 997-1014). We have also characterized a previously unknown dicyanide adduct that exhibits an EPR signal with ligand hyperfine structure from two protein nitrogens and two cyanide carbons. Cyanide may bind to the same copper center as azide, but not without a structural reorganization of the cluster. The results also imply that the protonation of a bridging ligand within the type 2/type 3 cluster explains the pH dependence of anion binding. Imidazole interacts with the protein but does not bind to the EPR-active copper. In keeping with the function of the dioxygen reduction site, the type 2/type 3 cluster in laccase proves to be an extremely flexible host capable of accommodating a variety of ligands.
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PMID:EPR studies of ligand binding to the type 2/type 3 cluster in tree laccase. 797 82

A protein synthesis inhibitor, cycloheximide, induces excretion of laccase in Neurospora crassa. The lah-1 mutation results in excretion of a large amount of laccase even in the absence of cycloheximide. Ten mutations were induced that suppress derepressed excretion of laccase in the lah-1 mutant. Of these, seven second-site mutations were found to confer a laccase-noninducible phenotype, and were classified into two different complementation groups. Four mutations define a locus designated lni-1, found to be closely linked to ylo-1 on linkage group VI. The other three mutations were mapped to second locus, designated lni-2, that lies between nic-3 and thi-3 on linkage group VII. The lni-2 locus was shown to encode laccase by RFLP mapping of the DNA fragment encoding laccase and by transformation of the lni-2 mutant with plasmid pBL1 carrying the laccase gene (the locus encoding laccas is hereafter described as lacc). All lacc mutants examined (whether mutagen-induced or inactivated by repeat-induced point mutation) appeared to exhibit no phenotypic deficiency during both asexual and sexual cycles, suggesting that the laccase gene is dispensable in N. crassa. Northern analysis of total cellular RNA from the four lni-1 mutants demonstrated that the lni-1 mutations abolish increased transcription of the laccase gene under inducing conditions. Consequently, the lni-1 locus is inferred to encode a trans-acting positive regulator required for transcriptional activation of the laccase gene in response to cycloheximide. Possible functions of the lah-1 gene are also described.
Mol Gen Genet 1993 Aug
PMID:Isolation and characterization of mutants defective in production of laccase in Neurospora crassa. 810 79

Expression of the laccase gene (lacc) of Neurospora crassa is transcriptionally inducible by the protein synthesis inhibitor cycloheximide. A lni-1 mutation, conferring the laccase non-inducible phenotype, was found to be a cpc-1 allele. Northern blots probed with plasmid pLA1, which carries the lacc gene revealed that the cpc-1 mutation abolishes the induced transcription of the lacc gene, indicating requirement of the cpc-1 gene for transcriptional activation of the lacc gene. In Northern blots probed with plasmid pAB1, which bears arg-2 a gene whose transcription is under the control of CPC1, the level of the arg-2 transcript was shown to increase several-fold in wild-type mycelia but remained low in cpc-1 mycelia, after treatment with cycloheximide. This suggests that inhibition of protein synthesis with cycloheximide, as well as amino acid limitation, elicits the CPC1-mediated cross-pathway control. Characterization of the lacc upstream region using a series of 5'-deletion plasmids led to the identification of a 170 bp DNA region required for the induced lacc expression. Sequence analysis of this DNA region demonstrated that it includes a 9 bp sequence with dyad symmetry, ATGAATCAT, which differs only by a central base pair from ATGA(C/G)TCAT, the recognition sequence characteristic of CPC1 and GCN4 binding sites. Possible mechanisms by which CPC1 mediates transcriptional activation of the lacc gene are discussed.
Mol Gen Genet 1994 Jun 03
PMID:Transcriptional activation of a cycloheximide-inducible gene encoding laccase is mediated by cpc-1, the cross-pathway control gene, in Neurospora crassa. 820 46

The N-linked oligosaccharide moieties of sycamore (Acer pseudoplatanus L.) laccase are known to be highly heterogeneous. We confirmed that this oligosaccharide heterogeneity was caused not only during the oligosaccharide biosynthesis in Golgi apparatus, but also after the excretion of laccase protein into a culture medium. The culture medium for the sycamore cells (Acer pseudoplatanus L.) contained beta-galactosidase, alpha-L-fucosidase, beta-N-acetylglucosaminidase, alpha-mannosidase and beta-xylosidase activities. We showed that the largest sugar chain in laccase, oligosaccharide F, [formula: see text] was degraded to [formula: see text] by a crude exoglycosidase mixture in the culture medium.
Biochem Mol Biol Int 1993 Mar
PMID:Occurrence of heterogeneity of N-linked oligosaccharides attached to sycamore (Acer pseudoplatanus L.) laccase after excretion. 848 57

The genome of the filamentous ascomycete Podospora anserina contains at least four non-adjacent regions that are homologous to the laccase gene of Neurospora crassa. One of these regions contains a gene (lac2) encoding a protein that displays 62% identity with the N. crassa laccase. In shaken cultures, lac2 mRNA is present at low basal levels throughout the growth phase but increases at least 20-fold at the beginning of the autolytic phase and decreases again thereafter. Addition of aromatic xenobiotics (guaiacol, hydroquinone, benzoquinone) to the medium during the growth phase results in a rapid, drastic and temporary increase in the abundance of lac2 mRNA. The promoter region of lac2 contains two sequences which display complete homology with the eukaryotic Xenobiotic Responsive Element and two sequences homologous to the eukaryotic Antioxidant Responsive Element. The identity and function of the laccase encoded by lac2 are discussed.
Mol Gen Genet 1996 Oct 16
PMID:Isolation and characterization of a laccase gene from Podospora anserina. 891 15


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