DB code: D00064
| CATH domain | 3.50.50.60 : FAD/NAD(P)-binding domain | |
|---|---|---|
| 3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2 | Catalytic domain | |
| E.C. | 1.14.13.2 | |
| CSA | 1dod | |
| M-CSA | 1dod | |
| MACiE | M0131 | |
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.30.9.10 : D-Amino Acid Oxidase; Chain A, domain 2 | D00037 D00041 D00494 T00025 |
| 3.50.50.60 : FAD/NAD(P)-binding domain | M00163 D00015 D00041 D00042 D00045 D00071 T00004 T00015 T00017 T00025 T00211 T00213 T00233 T00242 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P20586 |
P-hydroxybenzoate hydroxylase
|
PHBH
EC 1.14.13.2 4-hydroxybenzoate 3-monooxygenase |
NP_248938.1
(Protein)
NC_002516.2 (DNA/RNA sequence) |
PF01494
(FAD_binding_3)
[Graphical View] |
| P00438 |
P-hydroxybenzoate hydroxylase
|
EC
1.14.13.2
4-hydroxybenzoate 3-monooxygenase |
PF01494
(FAD_binding_3)
[Graphical View] |
| KEGG enzyme name |
|---|
|
4-hydroxybenzoate 3-monooxygenase
p-hydroxybenzoate hydrolyase p-hydroxybenzoate hydroxylase 4-hydroxybenzoate 3-hydroxylase 4-hydroxybenzoate monooxygenase 4-hydroxybenzoic hydroxylase p-hydroxybenzoate-3-hydroxylase p-hydroxybenzoic acid hydrolase p-hydroxybenzoic acid hydroxylase p-hydroxybenzoic hydroxylase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P20586 | PHHY_PSEAE | 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O. | Homodimer. | FAD. | |
| P00438 | PHHY_PSEFL | 4-hydroxybenzoate + NADPH + O(2) = protocatechuate + NADP(+) + H(2)O. | Homodimer. | FAD. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00362 | Benzoate degradation via hydroxylation | |
| MAP00623 | 2,4-Dichlorobenzoate degradation |
| Compound table | |||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | ||||||||||||
| KEGG-id | C00016 | C00156 | C00005 | C00007 | C00080 | C00230 | C00006 | C00001 | |||||||
| E.C. | |||||||||||||||
| Compound | FAD | 4-Hydroxybenzoate | NADPH | O2 | H+ | Protocatechuate | NADP+ | H2O | Flavin 4a-hydroperoxide intermediate | Flavin 4a-hydroxide intermediate | |||||
| Type | amide group,amine group,aromatic ring (only carbon atom),aromatic ring (with nitrogen atoms),carbohydrate,nucleotide | aromatic ring (only carbon atom),carboxyl group | amide group,amine group,nucleotide | others | others | aromatic ring (only carbon atom),carboxyl group | amide group,amine group,nucleotide | H2O | |||||||
| ChEBI |
16238 16238 |
30763 30763 |
16474 16474 |
15379 26689 27140 15379 26689 27140 |
15378 15378 |
36062 36062 |
18009 18009 |
15377 15377 |
|||||||
| PubChem |
643975 643975 |
135 3702506 135 3702506 |
5884 5884 |
977 977 |
1038 1038 |
72 72 |
5886 5886 |
22247451 962 22247451 962 |
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| 1bf3A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1bgjA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1bgnA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1bkwA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1cc4A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1cc6A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1cj2A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1cj3A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1cj4A01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1d7lA01 |
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Analogue:RFL | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1dobA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1docA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1dodA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1doeA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1iusA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1iutA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuuA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuvA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuwA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuxA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbbA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbcA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbdA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbeA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbfA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pdhA01 |
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Analogue:FAS | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1phhA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pxaA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pxbA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1pxcA01 |
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Bound:FAD | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 2phhA01 |
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Analogue:APR | Unbound | Unbound | Unbound | Unbound | Unbound | ||||
| 1bf3A02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1bgjA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1bgnA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1bkwA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1cc4A02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1cc6A02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1cj2A02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1cj3A02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1cj4A02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1d7lA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1dobA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1docA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1dodA02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:DOB | Unbound | ||||
| 1doeA02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:DOB | Unbound | ||||
| 1iusA02 |
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Unbound | Analogue:PAB | Unbound | Unbound | Unbound | Unbound | ||||
| 1iutA02 |
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Unbound | Analogue:PAB | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuuA02 |
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Unbound | Analogue:PAB | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuvA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuwA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1iuxA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbbA02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:DOB | Unbound | ||||
| 1pbcA02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:BHA | Unbound | ||||
| 1pbdA02 |
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Unbound | Analogue:PAB | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbeA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1pbfA02 |
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Unbound | Unbound | Unbound | Unbound | Analogue:BHA | Unbound | ||||
| 1pdhA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1phhA02 |
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Unbound | Unbound | Unbound | Unbound | Bound:DHB | Unbound | ||||
| 1pxaA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1pxbA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 1pxcA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| 2phhA02 |
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Unbound | Bound:PHB | Unbound | Unbound | Unbound | Unbound | ||||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| PDB;1cc4, 1cc6 & literature [12] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1bf3A01 |
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mutant R42K, C116S | ||||
| 1bgjA01 |
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mutant C116S, H162R | ||||
| 1bgnA01 |
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mutant C116S | ||||
| 1bkwA01 |
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mutant R44K, C116S | ||||
| 1cc4A01 |
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mutant C116S, F161A | ||||
| 1cc6A01 |
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mutant C116S, R166S | ||||
| 1cj2A01 |
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mutant Q34R | ||||
| 1cj3A01 |
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mutant Y38E | ||||
| 1cj4A01 |
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mutant Q34T | ||||
| 1d7lA01 |
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| 1dobA01 |
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| 1docA01 |
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| 1dodA01 |
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| 1doeA01 |
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| 1iusA01 |
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| 1iutA01 |
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| 1iuuA01 |
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| 1iuvA01 |
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| 1iuwA01 |
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| 1iuxA01 |
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| 1pbbA01 |
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mutant C116S | ||||
| 1pbcA01 |
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mutant C116S | ||||
| 1pbdA01 |
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mutant C116S | ||||
| 1pbeA01 |
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| 1pbfA01 |
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mutant C116S | ||||
| 1pdhA01 |
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| 1phhA01 |
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| 1pxaA01 |
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mutant N300D | ||||
| 1pxbA01 |
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| 1pxcA01 |
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| 2phhA01 |
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| 1bf3A02 |
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TYR 201;TYR 385 | invisible Y385 | |||
| 1bgjA02 |
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TYR 201;TYR 385 | ||||
| 1bgnA02 |
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TYR 201;TYR 385 | mutant R269T | |||
| 1bkwA02 |
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TYR 201;TYR 385 | ||||
| 1cc4A02 |
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TYR 201;TYR 385 | ||||
| 1cc6A02 |
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TYR 201;TYR 385 | ||||
| 1cj2A02 |
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TYR 201;TYR 385 | ||||
| 1cj3A02 |
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TYR 201;TYR 385 | ||||
| 1cj4A02 |
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TYR 201;TYR 385 | ||||
| 1d7lA02 |
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TYR 201;TYR 385 | ||||
| 1dobA02 |
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TYR 201;TYR 385 | mutant Y222F | |||
| 1docA02 |
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TYR 201;TYR 385 | ||||
| 1dodA02 |
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TYR 201;TYR 385 | ||||
| 1doeA02 |
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TYR 201;TYR 385 | ||||
| 1iusA02 |
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TYR 201;TYR 385 | ||||
| 1iutA02 |
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TYR 201;TYR 385 | ||||
| 1iuuA02 |
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TYR 201;TYR 385 | ||||
| 1iuvA02 |
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TYR 201;TYR 385 | ||||
| 1iuwA02 |
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TYR 201;TYR 385 | ||||
| 1iuxA02 |
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TYR 201;TYR 385 | ||||
| 1pbbA02 |
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TYR 201;TYR 385 | ||||
| 1pbcA02 |
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TYR 201;TYR 385 | ||||
| 1pbdA02 |
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TYR 201;TYR 385 | ||||
| 1pbeA02 |
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TYR 201;TYR 385 | ||||
| 1pbfA02 |
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TYR 201;TYR 385 | mutant Y222A | |||
| 1pdhA02 |
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TYR 201;TYR 385 | ||||
| 1phhA02 |
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TYR 201;TYR 385 | ||||
| 1pxaA02 |
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TYR 201;TYR 385 | ||||
| 1pxbA02 |
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;TYR 385 | mutant Y201F | |||
| 1pxcA02 |
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TYR 201; | mutant Y385F | |||
| 2phhA02 |
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TYR 201;TYR 385 | ||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
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p.72-73 | |
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[4]
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Fig.3, Fig.4 | |
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[5]
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Fig.3 | |
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[7]
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Fig.1, p.647 | |
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[10]
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Fig.1, Fig.2, Fig.6, Fig.7, Fig.8, p.3104-3106 | |
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[12]
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p.144-145 | |
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[13]
|
Fig.1 | |
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[14]
|
Scheme 1 | |
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[16]
|
Fig.1 | |
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[18]
|
Scheme 1, Scheme 2, Scheme 3, p.574-578 | |
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[24]
|
Fig.1, Scheme 1, p.6294-6298 | |
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[25]
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Scheme 1, p.16641-16646 | |
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[30]
|
Fig.1, p.170-172 | |
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[33]
|
Scheme 2, Scheme 7 | |
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[36]
|
Fig.1 | |
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[37]
|
Fig.1, p.22212-22215 | |
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[38]
|
Fig.1, p.1573-1579 | |
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[39]
|
Fig.1 | |
|
[40]
|
Fig.1, p.305-309 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 807574 |
| Journal | J Biol Chem |
| Year | 1975 |
| Volume | 250 |
| Pages | 5268-9 |
| Authors | Drenth J, Hol WG, Wierenga RK |
| Title | Crystallization and preliminary x-ray investigation of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 819305 |
| Journal | FEBS Lett |
| Year | 1976 |
| Volume | 65 |
| Pages | 84-6 |
| Authors | Marius A, Schepman, Schutter WG, van Bruggen EF |
| Title | Electron microscopic studies on microcrystals of parahydroxybenzoate hydroxylase from Pseudomonas fluorescens. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
| Medline ID | 80029705 |
| PubMed ID | 40036 |
| Journal | J Mol Biol |
| Year | 1979 |
| Volume | 131 |
| Pages | 55-73 |
| Authors | Wierenga RK, de Jong RJ, Kalk KH, Hol WG, Drenth J |
| Title | Crystal structure of p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | P00438 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6617648 |
| Journal | Eur J Biochem |
| Year | 1983 |
| Volume | 135 |
| Pages | 543-8 |
| Authors | Visser CM |
| Title |
Reaction mechanism of flavin-dependent hydroxylation. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 6235473 |
| Journal | Orig Life |
| Year | 1984 |
| Volume | 14 |
| Pages | 699-705 |
| Authors | Visser CM |
| Title |
Evolution of biocatalysis 4. |
| Related PDB | |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 3343242 |
| Journal | J Biol Chem |
| Year | 1988 |
| Volume | 263 |
| Pages | 3131-6 |
| Authors | Schreuder HA, Hol WG, Drenth J |
| Title | Molecular modeling reveals the possible importance of a carbonyl oxygen binding pocket for the catalytic mechanism of p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) |
| Medline ID | 88172509 |
| PubMed ID | 3351945 |
| Journal | J Mol Biol |
| Year | 1988 |
| Volume | 199 |
| Pages | 637-48 |
| Authors | Schreuder HA, van der Laan JM, Hol WG, Drenth J |
| Title | Crystal structure of p-hydroxybenzoate hydroxylase complexed with its reaction product 3,4-dihydroxybenzoate. |
| Related PDB | 1phh |
| Related UniProtKB | P00438 |
| [8] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 2819062 |
| Journal | Biochemistry |
| Year | 1989 |
| Volume | 28 |
| Pages | 7199-205 |
| Authors | van der Laan JM, Schreuder HA, Swarte MB, Wierenga RK, Kalk KH, Hol WG, Drenth J |
| Title |
The coenzyme analogue adenosine 5-diphosphoribose displaces FAD in the active site of p-hydroxybenzoate hydroxylase. |
| Related PDB | 2phh |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 2553983 |
| Journal | J Mol Biol |
| Year | 1989 |
| Volume | 208 |
| Pages | 679-96 |
| Authors | Schreuder HA, Prick PA, Wierenga RK, Vriend G, Wilson KS, Hol WG, Drenth J |
| Title |
Crystal structure of the p-hydroxybenzoate hydroxylase-substrate complex refined at 1.9 A resolution. |
| Related PDB | 1pbe |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2337581 |
| Journal | Biochemistry |
| Year | 1990 |
| Volume | 29 |
| Pages | 3101-8 |
| Authors | Schreuder HA, Hol WG, Drenth J |
| Title | Analysis of the active site of the flavoprotein p-hydroxybenzoate hydroxylase and some ideas with respect to its reaction mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [11] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF REDUCED FORM |
| Medline ID | 93028353 |
| PubMed ID | 1409567 |
| Journal | Proteins |
| Year | 1992 |
| Volume | 14 |
| Pages | 178-90 |
| Authors | Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG, Drenth J |
| Title | Crystal structure of the reduced form of p-hydroxybenzoate hydroxylase refined at 2.3 A resolution. |
| Related PDB | |
| Related UniProtKB | P00438 |
| [12] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 8365400 |
| Journal | Eur J Biochem |
| Year | 1993 |
| Volume | 216 |
| Pages | 137-46 |
| Authors | Eschrich K, van der Bolt FJ, de Kok A, van Berkel WJ |
| Title | Role of Tyr201 and Tyr385 in substrate activation by p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens. |
| Related PDB | |
| Related UniProtKB | |
| [14] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANTS |
| Medline ID | 94146010 |
| PubMed ID | 8312276 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 1555-64 |
| Authors | Lah MS, Palfey BA, Schreuder HA, Ludwig ML |
| Title |
Crystal structures of mutant Pseudomonas aeruginosa p-hydroxybenzoate hydroxylases: the Tyr201Phe, |
| Related PDB | 1pxa 1pxb 1pxc |
| Related UniProtKB | P20586 |
| [13] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 7520279 |
| Journal | Biochemistry |
| Year | 1994 |
| Volume | 33 |
| Pages | 10161-70 |
| Authors | Schreuder HA, Mattevi A, Obmolova G, Kalk KH, Hol WG, van der Bolt FJ, van Berkel WJ |
| Title |
Crystal structures of wild-type p-hydroxybenzoate hydroxylase complexed with 4-aminobenzoate,2,4-dihydroxybenzoate, |
| Related PDB | 1pbb 1pbc 1pbd 1pbf |
| Related UniProtKB | |
| [15] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 7756982 |
| Journal | Protein Sci |
| Year | 1994 |
| Volume | 3 |
| Pages | 2245-53 |
| Authors | van Berkel WJ, Eppink MH, Schreuder HA |
| Title | Crystal structure of p-hydroxybenzoate hydroxylase reconstituted with the modified FAD present in alcohol oxidase from methylotrophic yeasts: evidence for an arabinoflavin. |
| Related PDB | 1pdh |
| Related UniProtKB | |
| [16] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) |
| Medline ID | 95025875 |
| PubMed ID | 7939628 |
| Journal | Science |
| Year | 1994 |
| Volume | 266 |
| Pages | 110-4 |
| Authors | Gatti DL, Palfey BA, Lah MS, Entsch B, Massey V, Ballou DP, Ludwig ML |
| Title | The mobile flavin of 4-OH benzoate hydroxylase. |
| Related PDB | 1dob 1doc 1dod 1doe |
| Related UniProtKB | P20586 |
| [17] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-44 |
| Medline ID | 95354684 |
| PubMed ID | 7628466 |
| Journal | Eur J Biochem |
| Year | 1995 |
| Volume | 231 |
| Pages | 157-65 |
| Authors | Eppink MH, Schreuder HA, Van Berkel WJ |
| Title | Structure and function of mutant Arg44Lys of 4-hydroxybenzoate hydroxylase implications for NADPH binding. |
| Related PDB | 1bkw |
| Related UniProtKB | P00438 |
| [18] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
| Medline ID | 96140232 |
| PubMed ID | 8555229 |
| Journal | Biochemistry |
| Year | 1996 |
| Volume | 35 |
| Pages | 567-78 |
| Authors | Gatti DL, Entsch B, Ballou DP, Ludwig ML |
| Title | pH-dependent structural changes in the active site of p-hydroxybenzoate hydroxylase point to the importance of proton and water movements during catalysis. |
| Related PDB | 1ius 1iut 1iuu 1iuv 1iuw 1iux |
| Related UniProtKB | P20586 |
| [19] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9369493 |
| Journal | Biochemistry |
| Year | 1997 |
| Volume | 36 |
| Pages | 14192-201 |
| Authors | van der Bolt FJ, van den Heuvel RH, Vervoort J, van Berkel WJ |
| Title | 19F NMR study on the regiospecificity of hydroxylation of tetrafluoro-4-hydroxybenzoate by wild-type and Y385F p-hydroxybenzoate hydroxylase: evidence for a consecutive oxygenolytic dehalogenation mechanism. |
| Related PDB | |
| Related UniProtKB | |
| [20] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9385648 |
| Journal | Protein Sci |
| Year | 1997 |
| Volume | 6 |
| Pages | 2454-8 |
| Authors | Eppink MH, Schreuder HA, Van Berkel WJ |
| Title | Identification of a novel conserved sequence motif in flavoprotein hydroxylases with a putative dual function in FAD/NAD(P)H binding. |
| Related PDB | |
| Related UniProtKB | |
| [21] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9546198 |
| Journal | Biophys Chem |
| Year | 1998 |
| Volume | 70 |
| Pages | 217-22 |
| Authors | Mattevi A |
| Title | The PHBH fold: not only flavoenzymes. |
| Related PDB | |
| Related UniProtKB | |
| [22] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF MUTANT LYS-42 AND SER-42 |
| Medline ID | 98237589 |
| PubMed ID | 9578477 |
| Journal | Eur J Biochem |
| Year | 1998 |
| Volume | 253 |
| Pages | 194-201 |
| Authors | Eppink MH, Schreuder HA, van Berkel WJ |
| Title | Lys42 and Ser42 variants of p-hydroxybenzoate hydroxylase from Pseudomonas fluorescens reveal that Arg42 is essential for NADPH binding. |
| Related PDB | 1bf3 |
| Related UniProtKB | P00438 |
| [23] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 9694855 |
| Journal | J Biol Chem |
| Year | 1998 |
| Volume | 273 |
| Pages | 21031-9 |
| Authors | Eppink MH, Schreuder HA, van Berkel WJ |
| Title |
Interdomain binding of NADPH in p-hydroxybenzoate hydroxylase as suggested by kinetic, |
| Related PDB | 1bgj 1bgn |
| Related UniProtKB | |
| [24] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10320359 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 6292-9 |
| Authors | Moran GR, Entsch B, Palfey BA, Ballou DP |
| Title | Mechanistic insights into p-hydroxybenzoate hydroxylase from studies of the mutant Ser212Ala. |
| Related PDB | |
| Related UniProtKB | |
| [25] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10600126 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 16636-47 |
| Authors | Ortiz-Maldonado M, Gatti D, Ballou DP, Massey V |
| Title | Structure-function correlations of the reaction of reduced nicotinamide analogues with p-hydroxybenzoate hydroxylase substituted with a series of 8-substituted flavins. |
| Related PDB | 1d7l |
| Related UniProtKB | |
| [26] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9930974 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 1153-8 |
| Authors | Palfey BA, Moran GR, Entsch B, Ballou DP, Massey V |
| Title | Substrate recognition by "password" in p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [27] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10606503 |
| Journal | Biochemistry |
| Year | 1999 |
| Volume | 38 |
| Pages | 16727-32 |
| Authors | Zheng Y, Dong J, Palfey BA, Carey PR |
| Title | Using Raman spectroscopy to monitor the solvent-exposed and "buried" forms of flavin in p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [28] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF VARIANTS |
| Medline ID | 99148809 |
| PubMed ID | 10025942 |
| Journal | FEBS Lett |
| Year | 1999 |
| Volume | 443 |
| Pages | 251-5 |
| Authors | Eppink MH, Bunthol C, Schreuder HA, van Berkel WJ |
| Title |
Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. |
| Related PDB | 1cc4 1cc6 |
| Related UniProtKB | P00438 |
| [29] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 10493859 |
| Journal | J Mol Biol |
| Year | 1999 |
| Volume | 292 |
| Pages | 87-96 |
| Authors | Eppink MH, Overkamp KM, Schreuder HA, Van Berkel WJ |
| Title | Switch of coenzyme specificity of p-hydroxybenzoate hydroxylase. |
| Related PDB | 1cj2 1cj3 1cj4 |
| Related UniProtKB | |
| [30] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10736773 |
| Journal | J Mol Graph Model |
| Year | 1999 |
| Volume | 17 |
| Pages | 163-75, 214 |
| Authors | Ridder L, Mulholland AJ, Rietjens IM, Vervoort J |
| Title | Combined quantum mechanical and molecular mechanical reaction pathway calculation for aromatic hydroxylation by p-hydroxybenzoate-3-hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [31] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10922496 |
| Journal | FEBS Lett |
| Year | 2000 |
| Volume | 478 |
| Pages | 197-201 |
| Authors | Ridder L, Palfey BA, Vervoort J, Rietjens IM |
| Title | Modelling flavin and substrate substituent effects on the activation barrier and rate of oxygen transfer by p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [32] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11300768 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 3891-9 |
| Authors | Frederick KK, Ballou DP, Palfey BA |
| Title | Protein dynamics control proton transfers to the substrate on the His72Asn mutant of p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [33] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11170433 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 1091-101 |
| Authors | Ortiz-Maldonado M, Ballou DP, Massey V |
| Title | A rate-limiting conformational change of the flavin in p-hydroxybenzoate hydroxylase is necessary for ligand exchange and catalysis: studies with 8-mercapto- and 8-hydroxy-flavins. |
| Related PDB | |
| Related UniProtKB | |
| [34] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11248022 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 2001 |
| Volume | 98 |
| Pages | 3006-11 |
| Authors | Altose MD, Zheng Y, Dong J, Palfey BA, Carey PR |
| Title | Comparing protein-ligand interactions in solution and single crystals by Raman spectroscopy. |
| Related PDB | |
| Related UniProtKB | |
| [35] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11805318 |
| Journal | Proc Natl Acad Sci U S A |
| Year | 2002 |
| Volume | 99 |
| Pages | 608-13 |
| Authors | Wang J, Ortiz-Maldonado M, Entsch B, Massey V, Ballou D, Gatti DL |
| Title | Protein and ligand dynamics in 4-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [36] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14503873 |
| Journal | Biochemistry |
| Year | 2003 |
| Volume | 42 |
| Pages | 11234-42 |
| Authors | Ortiz-Maldonado M, Entsch B, Ballou DP |
| Title | Conformational changes combined with charge-transfer interactions are essential for reduction in catalysis by p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [37] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12684497 |
| Journal | J Biol Chem |
| Year | 2003 |
| Volume | 278 |
| Pages | 22210-6 |
| Authors | Palfey BA, Murthy YV, Massey V |
| Title | Altered balance of half-reactions in p-hydroxybenzoate hydroxylase caused by substituting the 2'-carbon of FAD with fluorine. |
| Related PDB | |
| Related UniProtKB | |
| [38] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14769033 |
| Journal | Biochemistry |
| Year | 2004 |
| Volume | 43 |
| Pages | 1569-79 |
| Authors | Ortiz-Maldonado M, Cole LJ, Dumas SM, Entsch B, Ballou DP |
| Title | Increased positive electrostatic potential in p-hydroxybenzoate hydroxylase accelerates hydroxylation but slows turnover. |
| Related PDB | |
| Related UniProtKB | |
| [39] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 14709077 |
| Journal | J Am Chem Soc |
| Year | 2004 |
| Volume | 126 |
| Pages | 127-42 |
| Authors | Bach RD, Dmitrenko O |
| Title |
Model studies on p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| [40] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 15581585 |
| Journal | Arch Biochem Biophys |
| Year | 2005 |
| Volume | 433 |
| Pages | 297-311 |
| Authors | Entsch B, Cole LJ, Ballou DP |
| Title | Protein dynamics and electrostatics in the function of p-hydroxybenzoate hydroxylase. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
According to the literature [10], (A) Hydride transfer from NADPH to FAD, (B) Oxygenation of hydroxybenzoate by O2 at FADH2 (Oxidative half-reaction): (B1) Oxygenation to form a flavin 4a-hydroperoxide intermediate. (B2) Additive double-bond deformation; Addition of hydroxyl group to substrate, (B3) Eliminative double-bond formation; Elimination of H2O from flavin 4a-hydroxide intermediate, |
| Created | Updated |
|---|---|
| 2004-03-24 | 2009-02-26 |