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Literature summary for 1.14.18.1 extracted from

  • Agarwal, P.; Singh, J.; Singh, R.P.
    Molecular cloning and characteristic features of a novel extracellular tyrosinase from Aspergillus niger PA2 (2017), Appl. Biochem. Biotechnol., 182, 1-15 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha Aspergillus niger

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
Aspergillus niger
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ required, activates, copper is an essential constituent of tyrosinase active site. Tyrosinase is a type-3 copper protein with two putative conserved copper-binding sites comprising of six histidines, tyrosinase has a di-copper active site Aspergillus niger

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 L-tyrosine + O2 Aspergillus niger
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2 L-dopa
-
?
2 L-tyrosine + O2 Aspergillus niger PA2
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2 L-dopa
-
?
L-tyrosine + O2 Aspergillus niger
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dopaquinone + H2O
-
?
L-tyrosine + O2 Aspergillus niger PA2
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dopaquinone + H2O
-
?
additional information Aspergillus niger tyrosinase is a bifunctional enzyme that catalyzes the o-monohydroxylation of monophenols (phenols) to their corresponding o-diphenols (o-cresolase or monophenolase, EC 1.14.18.1) and their subsequent oxidation (catechol oxidase or diphenolase, EC 1.103.1) into reactive o-quinones. Molecular oxygen is used as an electron acceptor, and it is reduced to water in both the reactions. Subsequently, the resulting o-quinones undergo non-enzymatic oxido-reduction reactions with various nucleophilic moieties, producing intermediates which auto-polymerize spontaneously in dark brown pigments. The monophenolase activity is the initial rate-determining reaction in the process ?
-
?
additional information Aspergillus niger PA2 tyrosinase is a bifunctional enzyme that catalyzes the o-monohydroxylation of monophenols (phenols) to their corresponding o-diphenols (o-cresolase or monophenolase, EC 1.14.18.1) and their subsequent oxidation (catechol oxidase or diphenolase, EC 1.103.1) into reactive o-quinones. Molecular oxygen is used as an electron acceptor, and it is reduced to water in both the reactions. Subsequently, the resulting o-quinones undergo non-enzymatic oxido-reduction reactions with various nucleophilic moieties, producing intermediates which auto-polymerize spontaneously in dark brown pigments. The monophenolase activity is the initial rate-determining reaction in the process ?
-
?

Organism

Organism UniProt Comment Textmining
Aspergillus niger A0A140CTD1 isolated from waste effluents of food industry
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Aspergillus niger PA2 A0A140CTD1 isolated from waste effluents of food industry
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Source Tissue

Source Tissue Comment Organism Textmining
additional information extracellular enzyme activity and L-DOPA production are maximal when glucose and peptone are employed as carbon source and nitrogen source, respectively, in the medium, and are enhanced notably when Cu2+ is supplemented Aspergillus niger
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 L-tyrosine + O2
-
Aspergillus niger 2 L-dopa
-
?
2 L-tyrosine + O2
-
Aspergillus niger PA2 2 L-dopa
-
?
L-tyrosine + O2
-
Aspergillus niger dopaquinone + H2O
-
?
L-tyrosine + O2
-
Aspergillus niger PA2 dopaquinone + H2O
-
?
additional information tyrosinase is a bifunctional enzyme that catalyzes the o-monohydroxylation of monophenols (phenols) to their corresponding o-diphenols (o-cresolase or monophenolase, EC 1.14.18.1) and their subsequent oxidation (catechol oxidase or diphenolase, EC 1.103.1) into reactive o-quinones. Molecular oxygen is used as an electron acceptor, and it is reduced to water in both the reactions. Subsequently, the resulting o-quinones undergo non-enzymatic oxido-reduction reactions with various nucleophilic moieties, producing intermediates which auto-polymerize spontaneously in dark brown pigments. The monophenolase activity is the initial rate-determining reaction in the process Aspergillus niger ?
-
?
additional information tyrosinase catalyzes the conversion of L-tyrosine to L-DOPA and then to dopachrome, which is subsequently polymerized spontaneously to melanin via a series of non-enzymatic reactions Aspergillus niger ?
-
?
additional information tyrosinase is a bifunctional enzyme that catalyzes the o-monohydroxylation of monophenols (phenols) to their corresponding o-diphenols (o-cresolase or monophenolase, EC 1.14.18.1) and their subsequent oxidation (catechol oxidase or diphenolase, EC 1.103.1) into reactive o-quinones. Molecular oxygen is used as an electron acceptor, and it is reduced to water in both the reactions. Subsequently, the resulting o-quinones undergo non-enzymatic oxido-reduction reactions with various nucleophilic moieties, producing intermediates which auto-polymerize spontaneously in dark brown pigments. The monophenolase activity is the initial rate-determining reaction in the process Aspergillus niger PA2 ?
-
?
additional information tyrosinase catalyzes the conversion of L-tyrosine to L-DOPA and then to dopachrome, which is subsequently polymerized spontaneously to melanin via a series of non-enzymatic reactions Aspergillus niger PA2 ?
-
?

Subunits

Subunits Comment Organism
? x * 42300, about, sequence calculation Aspergillus niger
More three-dimensional structure of tyrosinase, homolgy modeling crystal structure PDB ID 3W6W as template, overview Aspergillus niger

pI Value

Organism Comment pI Value Maximum pI Value
Aspergillus niger sequence calculation
-
4.8

General Information

General Information Comment Organism
evolution the primary sequence of Aspergillus niger PA2 tyrosinase has approximately 99% identity with that of Aspergillus niger CBS 513.88, phylogenetic analysis. Tyrosinase belongs to a large group of proteins termed as type-3 copper proteins Aspergillus niger
metabolism tyrosinase is a key enzyme involved in the melanin biosynthesis Aspergillus niger
additional information tyrosinase has a di-copper active site, homology modeling using crystal structure PDB ID 3W6W as template. The L-tyrosine-binding residues of tyrosinase active site pocket are highly conserved Aspergillus niger
physiological function tyrosinase is a key enzyme involved in the melanin biosynthesis Aspergillus niger