DB code: T00024
| RLCP classification | 10.21021.100.10205 : Electron transfer | |
|---|---|---|
| 10.21001.100.10900 : Electron transfer | ||
| CATH domain | 3.90.380.10 : Naphthalene 1,2-dioxygenase Alpha Subunit; Chain A, domain 1 | Catalytic domain |
| 2.102.10.10 : Rieske Iron-sulfur Protein | Catalytic domain | |
| 3.10.450.50 : Nuclear Transport Factor 2; Chain | ||
| E.C. | 1.14.12.12 | |
| CSA | 1ndo | |
| M-CSA | 1ndo | |
| MACiE | M0130 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 2.102.10.10 : Rieske Iron-sulfur Protein | M00222 |
| 3.10.450.50 : Nuclear Transport Factor 2; Chain | S00176 S00545 S00177 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0A110 |
Naphthalene 1,2-dioxygenase subunit alpha
|
EC
1.14.12.12
Naphthalene 1,2-dioxygenase ISP alpha |
NP_863072.1
(Protein)
NC_004999.1 (DNA/RNA sequence) YP_534822.1 (Protein) NC_007926.1 (DNA/RNA sequence) |
PF00355
(Rieske)
PF00848 (Ring_hydroxyl_A) [Graphical View] |
| P0A111 |
Naphthalene 1,2-dioxygenase subunit alpha
|
EC
1.14.12.12
Naphthalene 1,2-dioxygenase ISP alpha |
PF00355
(Rieske)
PF00848 (Ring_hydroxyl_A) [Graphical View] |
|
| P0A112 |
Naphthalene 1,2-dioxygenase subunit beta
|
EC
1.14.12.12
Naphthalene 1,2-dioxygenase ISP beta |
NP_863073.1
(Protein)
NC_004999.1 (DNA/RNA sequence) YP_534823.1 (Protein) NC_007926.1 (DNA/RNA sequence) |
PF00866
(Ring_hydroxyl_B)
[Graphical View] |
| P0A113 |
Naphthalene 1,2-dioxygenase subunit beta
|
EC
1.14.12.12
Naphthalene 1,2-dioxygenase ISP beta |
PF00866
(Ring_hydroxyl_B)
[Graphical View] |
| KEGG enzyme name |
|---|
|
naphthalene 1,2-dioxygenase
naphthalene dioxygenase naphthalene oxygenase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0A110 | NDOB_PSEPU | Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). | Naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase (ndoR) and ferredoxin (ndoA), and ISP is composed of a large alpha subunit (ndoB) and a small beta subunit (ndoC). | Binds 1 2Fe-2S cluster (Probable). Binds 1 iron ion (Probable). | |
| P0A111 | NDOB_PSEU8 | Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). | Naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase and ferredoxin (doxA), and ISP is composed of a large alpha subunit (doxB) and a small beta subunit (doxD) (Probable). | Binds 1 2Fe-2S cluster (By similarity). Binds 1 iron ion (By similarity). | |
| P0A112 | NDOC_PSEPU | Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). | The naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase (ndoR) and ferredoxin (ndoA), and ISP is composed of a hexamer of three large alpha subunits (ndoB) and three small beta subunits (ndoC). | Binds 1 2Fe-2S cluster (Probable). Binds 1 iron ion (Probable). | |
| P0A113 | NDOC_PSEU8 | Naphthalene + NADH + O(2) = (1R,2S)-1,2- dihydronaphthalene-1,2-diol + NAD(+). | Naphthalene dioxygenase (NDO) multicomponent enzyme system is composed of an electron transfer component and an iron sulfur protein (ISP). The electron transfer component is composed of ferredoxin reductase and ferredoxin (doxA), and ISP is composed of a large alpha subunit (doxB) and a small beta subunit (doxD) (Probable). | Binds 1 2Fe-2S cluster (By similarity). Binds 1 iron ion (By similarity). |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00624 | 1- and 2-Methylnaphthalene degradation | |
| MAP00626 | Naphthalene and anthracene degradation | |
| MAP00628 | Fluorene degradation | |
| MAP00642 | Ethylbenzene degradation |
| Compound table | ||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||
| KEGG-id | L00023 | C00023 | C00829 | C00004 | C00007 | C00080 | C04314 | C00003 | ||||||
| E.C. | ||||||||||||||
| Compound | [2Fe-2S] | Iron | Naphthalene | NADH | O2 | H+ | (1R,2S)-1,2-dihydronaphthalene-1,2-diol | NAD+ | ||||||
| Type | heavy metal,sulfide group | heavy metal | aromatic ring (only carbon atom) | amide group,amine group,nucleotide | others | others | aromatic ring (only carbon atom),carbohydrate | amide group,amine group,nucleotide | ||||||
| ChEBI |
33739 33739 |
18248 82664 18248 82664 |
16482 16482 |
16908 16908 |
15379 26689 27140 15379 26689 27140 |
15378 15378 |
44343 44343 |
15846 15846 |
||||||
| PubChem |
23925 23925 |
931 931 |
439153 439153 |
977 977 |
1038 1038 |
440294 440294 |
5893 5893 |
|||||||
| 1eg9A01 |
|
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Unbound | Bound:_FE | Analogue:IND | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoA01 |
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|
|
Unbound | Bound:_FE | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoC01 |
|
|
|
|
|
Unbound | Bound:_FE | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoE01 |
|
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|
Unbound | Bound:_FE | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7gA01 |
|
|
|
|
|
Unbound | Bound:_FE | Bound:NPY | Unbound | Unbound | Unbound | Unbound | ||
| 1o7hA01 |
|
|
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|
|
Unbound | Bound:_FE | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7mA01 |
|
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|
Unbound | Bound:_FE | Unbound | Unbound | Bound:OXY | Unbound | Unbound | ||
| 1o7nA01 |
|
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|
|
Unbound | Bound:_FE | Analogue:IND | Unbound | Bound:OXY | Unbound | Unbound | ||
| 1o7pA01 |
|
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Unbound | Bound:_FE | Unbound | Unbound | Unbound | Bound:NDH | Unbound | ||
| 1o7wA01 |
|
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Unbound | Bound:_FE | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1uuvA01 |
|
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Unbound | Bound:_FE | Analogue:IND | Unbound | Analogue:_NO | Unbound | Unbound | ||
| 1uuwA01 |
|
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Unbound | Bound:_FE | Unbound | Unbound | Analogue:_NO | Unbound | Unbound | ||
| 1eg9A02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoA02 |
|
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|
Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoC02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoE02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7gA02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7hA02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7mA02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7nA02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7pA02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7wA02 |
|
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1uuvA02 |
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1uuwA02 |
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Bound:FES | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1eg9B |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoD |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1ndoF |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7gB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7hB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7mB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7nB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7pB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1o7wB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1uuvB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| 1uuwB |
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Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P0A110, P0A111 & literature [4], [7], [9], [11], [17], [18] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1eg9A01 |
|
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|
ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1ndoA01 |
|
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1ndoC01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1ndoE01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1o7gA01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1o7hA01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1o7mA01 |
|
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1o7nA01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1o7pA01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1o7wA01 |
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1uuvA01 |
|
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1uuwA01 |
|
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ASP 205;HIS 208 | HIS 208;HIS 213;ASP 362(Iron binding) | |||
| 1eg9A02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1ndoA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1ndoC02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1ndoE02 |
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1o7gA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1o7hA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1o7mA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1o7nA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1o7pA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1o7wA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1uuvA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1uuwA02 |
|
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HIS 104 | CYS 81;HIS 83;CYS 101;HIS 104(2Fe-2S cluster binding) | |||
| 1eg9B |
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| 1ndoB |
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| 1ndoD |
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| 1ndoF |
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| 1o7gB |
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| 1o7hB |
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| 1o7mB |
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| 1o7nB |
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| 1o7pB |
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| 1o7wB |
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| 1uuvB |
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| 1uuwB |
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| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
|
SCHEME I, p.30257-30260 | |
|
[4]
|
p.575-582 | |
|
[5]
|
p.11068-11070 | |
|
[7]
|
Fig.1, p.1835-1836 | |
|
[9]
|
Fig.2 | |
|
[11]
|
Scheme 1, p.706-709 | |
|
[14]
|
Scheme 2, p.1952 | |
|
[17]
|
Fig.1, P.7065-7066 | |
|
[18]
|
p.272-274 | |
|
[19]
|
Fig.2 | |
|
[20]
|
Fig | |
|
[21]
|
Scheme 2, Scheme 3, Fig.7, Fig.9, p.443-451 | |
|
[22]
|
||
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7858982 |
| Journal | Bioorg Med Chem |
| Year | 1994 |
| Volume | 2 |
| Pages | 727-34 |
| Authors | Whited GM, Downie JC, Hudlicky T, Fearnley SP, Dudding TC, Olivo HF, Parker D |
| Title |
Oxidation of 2-methoxynaphthalene by toluene, |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8899998 |
| Journal | Appl Environ Microbiol |
| Year | 1996 |
| Volume | 62 |
| Pages | 4073-80 |
| Authors | Resnick SM, Gibson DT |
| Title |
Regio- and stereospecific oxidation of fluorene, |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9374510 |
| Journal | J Biol Chem |
| Year | 1997 |
| Volume | 272 |
| Pages | 30254-60 |
| Authors | Di Gennaro P, Sello G, Bianchi D, D'Amico P |
| Title | Specificity of substrate recognition by Pseudomonas fluorescens N3 dioxygenase.@The role of the oxidation potential and molecular geometry. |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) |
| Medline ID | 98298434 |
| PubMed ID | 9634695 |
| Journal | Structure |
| Year | 1998 |
| Volume | 6 |
| Pages | 571-86 |
| Authors | Kauppi B, Lee K, Carredano E, Parales RE, Gibson DT, Eklund H, Ramaswamy S |
| Title | Structure of an aromatic-ring-hydroxylating dioxygenase-naphthalene 1,2-dioxygenase. |
| Related PDB | 1ndo |
| Related UniProtKB | P0A110 P0A111 P23094 P23095 |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10390817 |
| Journal | Appl Microbiol Biotechnol |
| Year | 1999 |
| Volume | 51 |
| Pages | 592-7 |
| Authors | Barriault D, Sylvestre M |
| Title | Functionality of biphenyl 2,3-dioxygenase components in naphthalene 1,2-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10460161 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 11062-72 |
| Authors | Coulter ED, Moon N, Batie CJ, Dunham WR, Ballou DP |
| Title | Electron paramagnetic resonance measurements of the ferrous mononuclear site of phthalate dioxygenase substituted with alternate divalent metal ions: direct evidence for ligation of two histidines in the copper(II)-reconstituted protein. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10074076 |
| Journal | J Bacteriol |
| Year | 1999 |
| Volume | 181 |
| Pages | 1831-7 |
| Authors | Parales RE, Parales JV, Gibson DT |
| Title | Aspartate 205 in the catalytic domain of naphthalene dioxygenase is essential for activity. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10713518 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2000 |
| Volume | 56 |
| Pages | 313-21 |
| Authors | Carredano E, Kauppi B, Choudhury D, Ramaswamy S |
| Title | Pseudo-symmetry characterization and refinement of a trigonal crystal form of naphthalene 1,2-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10692370 |
| Journal | J Bacteriol |
| Year | 2000 |
| Volume | 182 |
| Pages | 1641-9 |
| Authors | Parales RE, Lee K, Resnick SM, Jiang H, Lessner DJ, Gibson DT |
| Title | Substrate specificity of naphthalene dioxygenase: effect of specific amino acids at the active site of the enzyme. |
| Related PDB | |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10986254 |
| Journal | J Bacteriol |
| Year | 2000 |
| Volume | 182 |
| Pages | 5495-504 |
| Authors | Parales RE, Resnick SM, Yu CL, Boyd DR, Sharma ND, Gibson DT |
| Title | Regioselectivity and enantioselectivity of naphthalene dioxygenase during arene cis-dihydroxylation: control by phenylalanine 352 in the alpha subunit. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10669618 |
| Journal | J Mol Biol |
| Year | 2000 |
| Volume | 296 |
| Pages | 701-12 |
| Authors | Carredano E, Karlsson A, Kauppi B, Choudhury D, Parales RE, Parales JV, Lee K, Gibson DT, Eklund H, Ramaswamy S |
| Title | Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding. |
| Related PDB | 1eg9 |
| Related UniProtKB | |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10919518 |
| Journal | Res Microbiol |
| Year | 2000 |
| Volume | 151 |
| Pages | 383-91 |
| Authors | Gennaro PD, Galli E, Orsini F, Pelizzoni F, Sello G, Bestetti G |
| Title | Development of biocatalysts carrying naphthalene dioxygenase and dihydrodiol dehydrogenase genes inducible in aerobic and anaerobic conditions. |
| Related PDB | |
| Related UniProtKB | |
| [13] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11849939 |
| Journal | Curr Opin Biotechnol |
| Year | 2001 |
| Volume | 12 |
| Pages | 564-73 |
| Authors | Boyd DR, Sharma ND, Allen CC |
| Title | Aromatic dioxygenases: molecular biocatalysis and applications. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11056161 |
| Journal | J Biol Chem |
| Year | 2001 |
| Volume | 276 |
| Pages | 1945-53 |
| Authors | Wolfe MD, Parales JV, Gibson DT, Lipscomb JD |
| Title | Single turnover chemistry and regulation of O2 activation by the oxygenase component of naphthalene 1,2-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11641767 |
| Journal | J Ind Microbiol Biotechnol |
| Year | 2001 |
| Volume | 27 |
| Pages | 94-103 |
| Authors | Yu CL, Parales RE, Gibson DT |
| Title | Multiple mutations at the active site of naphthalene dioxygenase affect regioselectivity and enantioselectivity. |
| Related PDB | |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12189839 |
| Journal | Chem Commun (Camb) |
| Year | 2002 |
| Volume | (14) |
| Pages | 1452-3 |
| Authors | Boyd DR, Sharma ND, Kennedy MA, Shepherd SD, Malone JF, Alves-Areias A, Holt R, Allenmark SG, Lemurell MA, Dalton H, Luckarift H |
| Title | Enzyme-catalysed oxygenation and deoxygenation routes to chiral thiosulfinates. |
| Related PDB | |
| Related UniProtKB | |
| [17] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12783560 |
| Journal | J Am Chem Soc |
| Year | 2003 |
| Volume | 125 |
| Pages | 7056-66 |
| Authors | Yang TC, Wolfe MD, Neibergall MB, Mekmouche Y, Lipscomb JD, Hoffman BM |
| Title | Substrate binding to NO-ferro-naphthalene 1,2-dioxygenase studied by high-resolution Q-band pulsed 2H-ENDOR spectroscopy. |
| Related PDB | |
| Related UniProtKB | |
| [18] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12695887 |
| Journal | J Ind Microbiol Biotechnol |
| Year | 2003 |
| Volume | 30 |
| Pages | 271-8 |
| Authors | Parales RE |
| Title | The role of active-site residues in naphthalene dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [19] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 12586937 |
| Journal | Science |
| Year | 2003 |
| Volume | 299 |
| Pages | 1039-42 |
| Authors | Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S |
| Title | Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. |
| Related PDB | 1ndo 1o7g 1o7h 1o7m 1o7n 1o7p 1o7w |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12586930 |
| Journal | Science |
| Year | 2003 |
| Volume | 299 |
| Pages | 1024-5 |
| Authors | Kovacs JA |
| Title |
Biochemistry. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15042436 |
| Journal | J Biol Inorg Chem |
| Year | 2004 |
| Volume | 9 |
| Pages | 439-52 |
| Authors | Bassan A, Blomberg MR, Siegbahn PE |
| Title | A theoretical study of the cis-dihydroxylation mechanism in naphthalene 1,2-dioxygenase. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15942729 |
| Journal | J Biol Inorg Chem |
| Year | 2005 |
| Volume | 10 |
| Pages | 483-9 |
| Authors | Karlsson A, Parales JV, Parales RE, Gibson DT, Eklund H, Ramaswamy S |
| Title | NO binding to naphthalene dioxygenase. |
| Related PDB | 1uuv 1uuw |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to a large family of bacterial Rieske non-heme iron oxygenases. Although NADH and NAD+ are included as a substrate and a product, (#) Ferredoxin-NAD+ reductase (cf. (A) Electron transfer from Ferredoxin to the FE2S2 (Iron-sulfur) of the oxidized form of this enzyme. (A1) Indirect transfer through Trp211 from the adjacent alpha-subunit and Val100, (B) Electron transfer from the FE2S2 to the mononuclear iron center of the adjacent subunit of this enzyme. (B1) Indirect transfer through His104 bound to the FE2S2, (C) Oxygenation of naphthalene at the mononuclear iron center. |
| Created | Updated |
|---|---|
| 2005-05-31 | 2009-02-26 |