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Literature summary extracted from
- Molecular cloning and characteristic features of a novel extracellular tyrosinase from Aspergillus niger PA2 (2017), Appl. Biochem. Biotechnol., 182, 1-15 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.18.1 | DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant expression in Escherichia coli strain DH5alpha | Aspergillus niger |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 1.14.18.1 | extracellular | - |
Aspergillus niger | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 1.14.18.1 | 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)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.18.1 | 2 L-tyrosine + O2 | Aspergillus niger | - |
2 L-dopa | - |
? | |
| 1.14.18.1 | 2 L-tyrosine + O2 | Aspergillus niger PA2 | - |
2 L-dopa | - |
? | |
| 1.14.18.1 | L-tyrosine + O2 | Aspergillus niger | - |
dopaquinone + H2O | - |
? | |
| 1.14.18.1 | L-tyrosine + O2 | Aspergillus niger PA2 | - |
dopaquinone + H2O | - |
? | |
| 1.14.18.1 | 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 | ? | - |
? | |
| 1.14.18.1 | 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
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.18.1 | Aspergillus niger | A0A140CTD1 | isolated from waste effluents of food industry | - |
| 1.14.18.1 | Aspergillus niger PA2 | A0A140CTD1 | isolated from waste effluents of food industry | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 1.14.18.1 | 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 | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 1.14.18.1 | 2 L-tyrosine + O2 | - |
Aspergillus niger | 2 L-dopa | - |
? | |
| 1.14.18.1 | 2 L-tyrosine + O2 | - |
Aspergillus niger PA2 | 2 L-dopa | - |
? | |
| 1.14.18.1 | L-tyrosine + O2 | - |
Aspergillus niger | dopaquinone + H2O | - |
? | |
| 1.14.18.1 | L-tyrosine + O2 | - |
Aspergillus niger PA2 | dopaquinone + H2O | - |
? | |
| 1.14.18.1 | 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 | ? | - |
? | |
| 1.14.18.1 | 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 | ? | - |
? | |
| 1.14.18.1 | 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 | ? | - |
? | |
| 1.14.18.1 | 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
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 1.14.18.1 | ? | x * 42300, about, sequence calculation | Aspergillus niger |
| 1.14.18.1 | More | three-dimensional structure of tyrosinase, homolgy modeling crystal structure PDB ID 3W6W as template, overview | Aspergillus niger |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 1.14.18.1 | Aspergillus niger | sequence calculation | - |
4.8 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 1.14.18.1 | 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 |
| 1.14.18.1 | metabolism | tyrosinase is a key enzyme involved in the melanin biosynthesis | Aspergillus niger |
| 1.14.18.1 | 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 |
| 1.14.18.1 | physiological function | tyrosinase is a key enzyme involved in the melanin biosynthesis | Aspergillus niger |
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