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Enzyme Name | UniProtKB | KEGG |
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| P37064 |
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Protein name | L-ascorbate oxidase | L-ascorbate oxidaseascorbaseascorbic acid oxidaseascorbate oxidaseascorbic oxidaseascorbate dehydrogenaseL-ascorbic acid oxidaseAAOL-ascorbate:O2 oxidoreductaseAA oxidase |
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Synonyms | AscorbaseASOEC 1.10.3.3 |
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Pfam | PF00394 (Cu-oxidase) PF07731 (Cu-oxidase_2) PF07732 (Cu-oxidase_3) [Graphical view]
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KEGG pathways | MAP code | Pathways |
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MAP00053 | Ascorbate and aldarate metabolism |
UniProtKB:Accession Number | P37064 |
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Entry name | ASO_CUCPM |
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Activity | 2 L-ascorbate + O(2) = 2 dehydroascorbate + 2 H(2)O. |
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Subunit | Dimer. |
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Subcellular location | Secreted (Potential). |
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Cofactor | Binds 4 copper ions per monomer. The copper ions are bound as 3 distinct copper centers known as type 1 or blue, type 2 or normal, and type 3 or coupled binuclear. |
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Compound table: links to PDB-related databases & PoSSuM |
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| Cofactors | Substrates | Products | intermediates |
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KEGG-id | C00070 | C00072 | C00007 | C05422 | C00001 |
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Compound | Copper | L-Ascorbate | O2 | Dehydroascorbate | H2O | Hydro-peroxide intermediate | Oxygen radical intermediate |
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Type | heavy metal | carbohydrate,aromatic ring (with hetero atoms other than nitrogen atoms) | others | carbohydrate | H2O |
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ChEBI | 28694 30052
| 29073
| 27140 26689 15379
| 27956
| 15377
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PubChem | 23978
| 54670067
| 977
| 440667
| 962 22247451
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| | | | | | | | | | | | | | |
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1aozA01 |  |  |  |  |  |  |  | Analogue:C2O | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aozB01 |  |  |  |  |  |  |  | Analogue:C2O | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asoA01 |  |  |  |  |  |  |  | Bound:_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asoB01 |  |  |  |  |  |  |  | Bound:_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aspA01 |  |  |  |  |  |  |  | Bound:_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aspB01 |  |  |  |  |  |  |  | Bound:_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asqA01 |  |  |  |  |  |  |  | Bound:_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asqB01 |  |  |  |  |  |  |  | Bound:_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aozA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aozB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asoA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asoB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aspA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aspB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asqA02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asqB02 |  |  |  |  |  |  |  | Unbound | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aozA03 |  |  |  |  |  |  |  | Bound:_CU,Analogue;C1O | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aozB03 |  |  |  |  |  |  |  | Bound:_CU,Analogue;C1O | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asoA03 |  |  |  |  |  |  |  | Bound:3x_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1asoB03 |  |  |  |  |  |  |  | Bound:3x_CU | Unbound | Unbound | Unbound | | Unbound | Unbound |
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1aspA03 |  |  |  |  |  |  |  | Bound:3x_CU | Unbound | Unbound | Unbound | | Bound:PEO | Unbound |
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1aspB03 |  |  |  |  |  |  |  | Bound:3x_CU | Unbound | Unbound | Unbound | | Bound:PEO | Unbound |
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1asqA03 |  |  |  |  |  |  |  | Bound:3x_CU | Unbound | Unbound | Unbound | | Analogue:AZI 2 | Unbound |
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1asqB03 |  |  |  |  |  |  |  | Bound:3x_CU | Unbound | Unbound | Unbound | | Analogue:AZI 2 | Unbound |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[7] | Fig.19, p.199-203 |
| [8] | Fig.13, p.1012-1013 |
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references | [1] |
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PubMed ID | 510553 |
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Journal | FEBS Lett |
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Year | 1979 |
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Volume | 107 |
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Pages | 407-8 |
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Authors | Ladenstein R, Marchesini A, Palmieri S |
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Title | Preliminary crystallographic study of ascorbic acid oxidase from green zucchini squash. |
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[2] |
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PubMed ID | 6620382 |
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Journal | J Mol Biol |
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Year | 1983 |
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Volume | 169 |
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Pages | 351-2 |
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Authors | Bolognesi M, Gatti G, Coda A, Avigliano L, Marcozzi G, Finazzi-Agro A |
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Title | A new crystalline modification of the copper enzyme ascorbate oxidase. |
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[3] |
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PubMed ID | 3406029 |
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Journal | Prog Clin Biol Res |
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Year | 1988 |
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Volume | 274 |
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Pages | 285-8 |
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Authors | Messerschmidt A, Rossi A, Ladenstein R, Huber R, Bolognesi M, Marchesini A, Petruzelli R, Finazzi-Agro A |
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Title | Preliminary X-ray crystal structure and partial cDNA-sequence of ascorbate oxidase from zucchini. |
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[4] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
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Medline ID | 89236417 |
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PubMed ID | 2716059 |
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Journal | J Mol Biol |
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Year | 1989 |
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Volume | 206 |
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Pages | 513-29 |
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Authors | Messerschmidt A, Rossi A, Ladenstein R, Huber R, Bolognesi M, Gatti G, Marchesini A, Petruzzelli R, Finazzi-Agro A |
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Title | X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands. |
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Related UniProtKB | P37064 |
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[5] |
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PubMed ID | 2373076 |
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Journal | Eur J Biochem |
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Year | 1990 |
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Volume | 190 |
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Pages | 491-5 |
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Authors | Savini I, D'Alessio S, Giartosio A, Morpurgo L, Avigliano L |
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Title | The role of copper in the stability of ascorbate oxidase towards denaturing agents. |
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[6] |
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PubMed ID | 1330552 |
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Journal | Eur J Biochem |
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Year | 1992 |
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Volume | 209 |
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Pages | 597-602 |
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Authors | Messerschmidt A, Steigemann W, Huber R, Lang G, Kroneck PM |
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Title | X-ray crystallographic characterisation of type-2-depleted ascorbate oxidase from zucchini. |
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[7] |
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Comments | X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) |
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Medline ID | 92194315 |
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PubMed ID | 1548698 |
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Journal | J Mol Biol |
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Year | 1992 |
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Volume | 224 |
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Pages | 179-205 |
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Authors | Messerschmidt A, Ladenstein R, Huber R, Bolognesi M, Avigliano L, Petruzzelli R, Rossi A, Finazzi-Agro A |
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Title | Refined crystal structure of ascorbate oxidase at 1.9 A resolution. |
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Related PDB | 1aoz |
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Related UniProtKB | P37064 |
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[8] |
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Comments | X-ray crystallography |
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PubMed ID | 8478945 |
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Journal | J Mol Biol |
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Year | 1993 |
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Volume | 230 |
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Pages | 997-1014 |
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Authors | Messerschmidt A, Luecke H, Huber R |
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Title | X-ray structures and mechanistic implications of three functional derivatives of ascorbate oxidase from zucchini. Reduced, peroxide and azide forms. |
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Related PDB | 1aso,1asp,1asq |
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[9] |
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PubMed ID | 7748896 |
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Journal | Biochim Biophys Acta |
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Year | 1995 |
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Volume | 1248 |
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Pages | 143-8 |
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Authors | Sakurai T, Takahashi J |
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Title | EPR spectra of type 3 copper centers in Rhus vernicifera laccase and Cucumis sativus ascorbate oxidase. |
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[10] |
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PubMed ID | 9125505 |
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Journal | Biochemistry |
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Year | 1997 |
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Volume | 36 |
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Pages | 4852-9 |
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Authors | Gaspard S, Monzani E, Casella L, Gullotti M, Maritano S, Marchesini A |
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Title | Inhibition of ascorbate oxidase by phenolic compounds. Enzymatic and spectroscopic studies. |
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[11] |
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PubMed ID | 9283082 |
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Journal | Biochemistry |
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Year | 1997 |
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Volume | 36 |
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Pages | 10917-22 |
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Authors | Mei G, Di Venere A, Buganza M, Vecchini P, Rosato N, Finazzi-Agro' A |
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Title | Role of quaternary structure in the stability of dimeric proteins: the case of ascorbate oxidase. |
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[12] |
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PubMed ID | 9048895 |
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Journal | Biochim Biophys Acta |
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Year | 1997 |
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Volume | 1337 |
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Pages | 191-7 |
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Authors | Reinhammar B, Aasa R, Vanngard T, Maritano S, Marchesini A |
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Title | The type 2 copper of ascorbate oxidase. |
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[13] |
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PubMed ID | 9602107 |
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Journal | Biochim Biophys Acta |
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Year | 1998 |
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Volume | 1384 |
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Pages | 160-70 |
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Authors | Huang HW, Sakurai T, Monjushiro H, Takeda S |
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Title | Magnetic studies of the trinuclear center in laccase and ascorbate oxidase approached by EPR spectroscopy and magnetic susceptibility measurements. |
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[14] |
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PubMed ID | 9781686 |
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Journal | FEBS Lett |
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Year | 1998 |
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Volume | 436 |
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Pages | 239-42 |
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Authors | Farver O, Eady RR, Abraham ZH, Pecht I |
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Title | The intramolecular electron transfer between copper sites of nitrite reductase: a comparison with ascorbate oxidase. |
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[15] |
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PubMed ID | 10813026 |
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Journal | Appl Biochem Biotechnol |
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Year | 1999 |
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Volume | 82 |
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Pages | 227-41 |
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Authors | Savini I, Santucci R, Di Venere A, Rosato N, Strukul G, Pinna F, Avigliano L |
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Title | Catalytic and spectroscopic properties of cytochrome-c, horseradish peroxidase, and ascorbate oxidase embedded in a sol-gel silica matrix as a function of gelation time. |
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[16] |
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PubMed ID | 10583375 |
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Journal | Eur J Biochem |
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Year | 1999 |
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Volume | 266 |
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Pages | 820-30 |
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Authors | Gromov I, Marchesini A, Farver O, Pecht I, Goldfarb D |
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Title | Azide binding to the trinuclear copper center in laccase and ascorbate oxidase. |
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[17] |
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PubMed ID | 10860754 |
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Journal | J Mol Biol |
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Year | 2000 |
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Volume | 299 |
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Pages | 487-98 |
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Authors | Fleming PJ, Richards FM |
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Title | Protein packing: dependence on protein size, secondary structure and amino acid composition. |
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[18] |
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PubMed ID | 11983419 |
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Journal | Biochim Biophys Acta |
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Year | 2002 |
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Volume | 1596 |
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Pages | 36-46 |
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Authors | Sugino M, Kajita S, Banno K, Shirai T, Yamane T, Kato M, Kobayashi T, Tsukagoshi N |
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Title | Upward shift of the pH optimum of Acremonium ascorbate oxidase. |
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[19] |
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PubMed ID | 15006640 |
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Journal | Int J Biochem Cell Biol |
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Year | 2004 |
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Volume | 36 |
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Pages | 881-92 |
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Authors | Santagostini L, Gullotti M, De Gioia L, Fantucci P, Franzini E, Marchesini A, Monzani E, Casella L |
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Title | Probing the location of the substrate binding site of ascorbate oxidase near type 1 copper: an investigation through spectroscopic, inhibition and docking studies. |
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comments | Coppers can be classified into three types (see literature [7], [8] & laccase;T00215 in EzCatDB): Type I copper (blue copper); Copper-1 in this enzyme Type II copper (non-blue copper); Copper-2 Type III copper (EPR-non-detectable copper); Copper-3a & copper-3b in this enzyme. The copper-2, -3a and -3b form a trinuclear copper site, to which an oxygen is bound, whereas the cooper-1 is a monocuclear copper site, to which an organic substrate is bound (see laccase;T00215). This enzyme catalyzes the following reactions: (A) Oxidation (dehydrogenation) of organic substrate at mononuclear coper site: (B) Electron transfer from mononuclear copper site to trinuclear copper site: (C) O2 reduction to produce H2O at trinuclear copper site:
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created | updated |
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2005-04-22 | 2009-02-26 |
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