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:1.10.3.1 (tyrosinase)
9,065 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three adhesive polyoctapeptides (X/Y-Gly-Tyr-Ser-Ala-Gly-Tyr-Lys)n (X, Thr and Ala: Y, Thr:Ala = 3:2), which are the C-terminal octapeptide sequences shared by all those consensus motifs of a ribbed mussel Geukensia demissa adhesive protein (RMAP), have been synthesized by the polycondensation of the active esters. The correlation between wettability and adhesion with the alternative substitution by hydrophobic Ala and hydrophilic Thr in the synthetic RMAPs in aqueous solution and as films on high and low surface free energy (sfe) surfaces has been investigated by surface chemical approaches. The side chain moieties of RMAPs arrange their local conformation to adapt to the inherent surface character, and they orientate on high and low sfe surfaces. On a high sfe glass the hydrophilic side chains of the RMAP molecules face toward the surface, and on a low sfe polyethylene (HDPE) the hydrophobic side chains face toward the surface. The bonding strengths of synthetic RMAPs on glass and HDPE with and without enzymatic oxidation have been examined. Increased starting concentration exhibited the strongest adhesive capability (7.5 kgf/cm2) on alumina due to the increased cohesion among RMAP molecules. As another factor to increase adhesive ability, the intermolecular cross-linking among RMAP molecules by tyrosinase increases their adhesive capability by about 20% on HDPE, glass, and alumina except iron.
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PMID:Synthesis and wettability characteristics of model adhesive protein sequences inspired by a marine mussel. 1171 Jan 79

Hydroxylation of peptidyl-3,4-dihydroxyphenyl-l-alanine (Dopa) was observed during tyrosinase incubation of a decapeptide related to the mussel adhesive protein mefp1. The reaction was carried out at high enzyme concentrations (700 units tyrosinase/micromol of tyrosine). The hydroxylation of tyrosines in the decapeptide proceeds sequentially. First, Tyr-9 is hydroxylated to Dopa, followed by hydroxylation of Tyr-5; finally, Dopa-9 is hydroxylated to Topa. Topa was identified as 3,4,5-trihydroxyphenylalanine (3,4,5-Topa) by comparison to known standards using amino acid analysis, derivatization with phenylisothiocyanate in combination with Edman sequencing, and matrix-assisted laser desorption mass spectrometry with time-of-flight. Two other peptides, not related to mussel proteins, were also found to form peptidyl-Topa upon incubation with tyrosinase. Although 3,4,5-Topa has been reported in the primary sequence of several peptides, its formation in vitro from tyrosine-containing peptides is novel. The formation of Topa would appear to be a function of tyrosinase rather than the nucleophilic addition of water to dopaquinone.
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PMID:The other Topa: formation of 3,4,5-trihydroxyphenylalanine in peptides. 1206 21

The present study deals with the microbiological transformation of L-tyrosine to 3,4-dihydroxyphenyl L-alanine by a mutant strain of Aspergillus oryzae UV-7. Sixteen different mutant strains of Aspergillus oryzae (GCB-6) were isolated through UV-irradiation. These mutant strains were screened for the production of mold mycelia by submerged fermentation in 250-ml Erlenmeyer flasks. Of all the mutant strains examined, UV-7 gave maximum production of L-dopa (1.28 mg/ml). The reaction was carried out using mold mycelium as a source of enzyme tyrosinase in shake flasks. The maximum production of L-dopa was obtained when glucose (25 mg/ml) was used as the carbon source and NH(4)Cl (3 mg/ml) was used as the nitrogen source. The optimum pH for mycelium development was 5.0; L-dopa production was maximum at pH 3.5 of the reaction mixture. The reaction by mold mycelium (75 mg/ml) was carried out under acidic conditions. Optimum temp, time, and L-tyrosine concentration were 55 degrees C, 60 min, and 3.0 mg/ml, respectively.
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PMID:Microbiological transformation of L-tyrosine to 3,4-dihydroxyphenyl L-alanine (L-dopa) by a mutant strain of Aspergillus oryzae UV-7. 1207 Jun 84

The present investigation deals with the biosynthesis of L-DOPA by parental (GCB-6) and mutant (UV-7) strains of Aspergillus oryzae. There was a marked difference between the mycelial morphology and pellet type of parental and UV-irradiated mutant culture. The mutant strain of A. oryzae UV-6 exhibited pellet-like mycelial morphology and improved tyrosinase activity. Mould mycelium was used for biochemical conversion of L-tyrosine to L-DOPA because tyrosinase is an intracellular enzyme. The mutant was found to yield 3.72 fold higher production of L-DOPA than the parental strain. The mutant strain is stable and D-glc-resistant. The comparison of kinetic parameters was also done which showed the greater ability of the mutant to yield L-DOPA (i.e., Yp/x 40.00+/-0.01 d mg/mg with parent and 182.86+/-0.02a mg/mg in case of mutant). When cultures grown for various incubation periods, were monitored for Qp, Qs and q(p), there was significant enhancement (p < 0.0025-0.005) in these variables by the mutant strain of A. oryzae UV-7 over GCB-6 on all the rates. L-DOPA (3,4-dihydroxy phenyl L-alanine) is a drug of choice in the treatment of Parkinson's disease and myocardium following neurogenic injury.
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PMID:Biosynthesis of L-DOPA by Aspergillus oryzae. 1214 38

Amino-(3,4-dihydroxyphenyl)methyl phosphonic acid, the phosphonic analog of 3,4-dihydroxyphenylglycine, had been previously reported as a potent inhibitor of tyrosinase. The mechanism of the apparent enzyme inhibition by this compound has now been established. Amino-(3,4-dihydroxyphenyl)methyl phosphonic acid turned out to be a substrate and was oxidized to o-quinone, which evolved to a final product identified as 3,4-dihydroxybenzaldehyde, the same as for 3,4-dihydroxyphenylglycine. Monohydroxylated compounds (amino-(3-hydroxyphenyl)methyl phosphonic acid and amino-(4-hydroxyphenyl)methyl phosphonic acid) were not oxidized, neither was 4-hydroxy-l-phenylglycine. However, the relatively high Km for amino-(3,4-dihydroxyphenyl)methyl phosphonic acid (0.52 mm) indicated that competitive inhibition could not entirely explain the previously reported strong inhibitory effect (Ki = 50 and 97 micro m for tyrosine and 3-(3,4-dihydroxyphenyl)alanine (Dopa) as substrates, respectively). Neither was the enzyme covalently inactivated to a significant degree. Spectroscopic and electrochemical analysis of the oxidation of a mixture of Dopa and the inhibitor demonstrated that the phosphonic compound reduced dopaquinone back to Dopa, thus diminishing and delaying the formation of dopachrome. This produces an apparent strong inhibitory effect when the reaction is monitored spectrophotometrically at 475 nm. In this peculiar case Dopa acts as a redox shuttle mediating the oxidation of the shorter phosphonic homolog. Decomposition of the phosphonic o-quinone to 3,4-dihydroxybenzaldehyde drives the reaction against the slightly unfavorable difference in redox potentials.
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PMID:Redox reaction between amino-(3,4-dihydroxyphenyl)methyl phosphonic acid and dopaquinone is responsible for the apparent inhibitory effect on tyrosinase. 1218 Sep 86

A tyrosinase inhibitor was isolated from the seeds of Euphorbia lathyris L. by bioassay-guided fractionation and purification, using silica gel column chromatography. It was identified as esculetin by comparing its physical properties and spectral data with those of an authentic sample. The IC50 value of esculetin in the mushroom tyrosinase activity test was 43 microM. The kinetic study indicates that esculetin exhibited competitive inhibition against the oxidation of 3-(3,4-dihydroxyphenyl)-alanine by mushroom tyrosinase. The structure-activity relationships among five esculetin analogs suggest that hydroxyl groups at the C6 and C7 positions of the coumarin skeleton played an important role in the expression of tyrosinase inhibitory activity.
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PMID:Mushroom tyrosinase inhibitory activity of esculetin isolated from seeds of Euphorbia lathyris L. 1272 15

Recent population studies have demonstrated an association with the red-hair and fair-skin phenotype with variant alleles of the melanocortin-1 receptor (MC1R) which result in amino acid substitutions within the coding region leading to an altered receptor activity. In particular, Arg151Cys, Arg160Trp and Asp294His were the most commonly associated variants seen in the south-east Queensland population with at least one of these alleles found in 93% of those with red hair. In order to study the individual effects of these variants on melanocyte biology and melanocytic pigmentation, we established a series of human melanocyte strains genotyped for the MC1R receptor which included wild-type consensus, variant heterozygotes, compound heterozygotes and homozygotes for Arg151Cys, Arg160Trp, Val60Leu and Val92Met alleles. These strains ranged from darkly pigmented to amelanotic, with all strains of consensus sequence having dark pigmentation. UV sensitivity was found not to be associated with either MC1R genotype or the level of pigmentation with a range of sensitivities seen across all genotypes. Ultrastructural analysis demonstrated that while consensus strains contained stage IV melanosomes in their terminal dendrites, Arg151Cys and Arg160Trp homozygote strains contained only stage II melanosomes. This was despite being able to show expression of tyrosinase and tyrosinase-related protein-1 markers, although at reduced levels and an ability to convert exogenous 3,4-dihydroxyphenyl-alanine (DOPA) to melanin in these strains.
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PMID:Screening of human primary melanocytes of defined melanocortin-1 receptor genotype: pigmentation marker, ultrastructural and UV-survival studies. 1275 86

Tyrosinase was used to initiate the grafting of peptides onto the amine-containing polysaccharide chitosan. Chemical evidence for covalent grafting was obtained from electrospray mass spectrometry for products formed from reactions with glucosamine (the monomeric unit of chitosan) and the model dipeptide Tyr-Ala. When this model dipeptide was incubated with tyrosinase and chitosan, there was a marked increase in the viscosity of the solution. This viscosity increase provides physical evidence that tyrosinase can initiate peptide grafting onto the chitosan backbone. A peptide-modified chitosan derivative was generated by reacting chitosan (0.32 w/v%) with acid-hydrolyzed casein (0.5 w/v %) using tyrosinase. After reaction, the peptide-modified chitosan was partially purified and dissolved in an aqueous acetic acid solution. Low concentrations of this peptide-modified chitosan were observed to confer viscoelastic properties to the solutions. Specifically they conferred high viscosities and shear thinning properties to the solutions, and solutions containing only 1 w/w % of the peptide-modified chitosan behaved as weak gels. Thus, tyrosinase provides a simple and safe way to convert food-processing byproducts into environmentally friendly products that offer useful functional properties. The selectivity of tyrosinase and the relatively high reactivity of chitosan's amines allow grafting to be performed with uncharacterized peptide mixtures present in crude hydrolysates.
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PMID:Enzymatic grafting of peptides from casein hydrolysate to chitosan. Potential for value-added byproducts from food-processing wastes. 1496 32

The reactions of phosphorus trichloride with various amino acids afford the pentacoordinated spirophosphoranes. The reaction procedures were traced by (31)P NMR spectra techniques. A new crystal structure of alanine derivative was characterized, which is a slightly distorted TBP structure. Besides, this kind of spirophosphoranes are potent inhibitors to tyrosinase.
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PMID:Synthesis, characteristics and biological activity of pentacoordinated spirophosphoranes derived from amino acids. 1588 20

The protein family known as fp-1 provides mussel byssus with a protective outer coating and has drawn much attention for its water resistant bioadhesive properties in vitro. A new fp-l isolated from the green shell mussel Perna canaliculus (pcfp-1) reveals a composition dominated by only four amino acids: 3,4-dihydroxyphenyl-L-alanine (dopa), lysine, proline, and valine at approximately 20 mol % each. SDS-PAGE and MALDI-TOF mass spectrometry detected size variants at 48 and 52 kDa in preparations of purified Pcfp-1. The N-terminal sequence enabled construction of oligonucleotide primers for PCR and RACE-derived cDNAs from which the complete sequence of four variants was deduced. pcfp-1 deviates from all known homologues in other mussels in several notable respects: its mass is half, most of its sequence is represented by 75 tandem repeats of a tetrapeptide, i.e., PY*VK, in which Y* is dopa, prolines are not hydroxylated, and thiolate cysteines are clustered in homologous sequences at both the amino and carboxy termini. Amino acids in the repeat sequence show a striking resemblance to proline-rich cell wall proteins with tandemly repeated PPVYK pentapeptides [Hong, J. C., Nagao, R. T., and Key, J. L. (1987) J. Biol. Chem. 262, 8367-8376]. Cysteine plays a key role in cross-linking pcfp-1 by forming adducts with dopaquinone. Significant 5-S-cysteinyldopa and smaller amounts of 2-S-cysteinyldopa were detected in hydrolysates of the byssal threads of P. canaliculus. The cross-links could also be formed by oxidation of pcfp-1 in vitro using mushroom tyrosinase. Cysteinyldopa cross-links were present in trace amounts only in the byssus of other mussel species.
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PMID:Coating proteins: structure and cross-linking in fp-1 from the green shell mussel Perna canaliculus. 1631 94


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