EC number:1.14.14.9
Enzyme
Download| EC Tree |
| 1. Oxidoreductases |
| 1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen |
| 1.14.14 With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor |
| ID: | 1.14.14.9 |
|---|---|
| Description: | 4-hydroxyphenylacetate 3-monooxygenase. |
| Alternative Name: |
p-hydroxyphenylacetate 3-hydroxylase. 4-hydroxyphenylacetic acid-3-hydroxylase. 4 HPA 3-hydroxylase. |
| Cath: | 1.10.3140.10; 1.10.540.10; 1.20.140.10; 2.30.110.10; 2.40.110.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 1.14.14.9 |
| BRENDA Enzyme Link: | BRENDA 1.14.14.9 |
| KEGG Enzyme Link: | KEGG1.14.14.9 |
| BioCyc Enzyme Link: | BioCyc 1.14.14.9 |
| ExPASy Enzyme Link: | ExPASy1.14.14.9 |
| EC2PDB Enzyme Link: | EC2PDB 1.14.14.9 |
| ExplorEnz Enzyme Link: | ExplorEnz 1.14.14.9 |
| PRIAM enzyme-specific profiles Link: | PRIAM 1.14.14.9 |
| IntEnz Enzyme Link: | IntEnz 1.14.14.9 |
| MEDLINE Enzyme Link: | MEDLINE 1.14.14.9 |
EC number:1.14.14.9
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:30595 | 4-hydroxyphenylacetate + FADH2 + O2 = 3,4-dihydroxyphenylacetate + FAD + H(+) + H2O |
| RULE(radius=1) | [*:1]-[N;H0;+0:2]1-[*:3]:[*:4]-[NH;+0:5]-[c;H0;+0:6](:[*:7]):[c;H0;+0:8]-1:[nH;+0:9]:[*:10].[*:11]:[cH;+0:12]:[*:13].[O;H0;+0:14]=[O;H0;+0:15]>>[*:1]-[n;H0;+0:2]1:[*:3]:[*:4]:[n;H0;+0:5]:[c;H0;+0:6](:[*:7])-[c;H0;+0:8]:1:[n;H0;+0:9]:[*:10].[*:11]:[c;H0;+0:12](:[*:13])-[OH;+0:14].[OH2;+0:15] |
| Reaction |  |
| Core-to-Core |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Molecular characterization of 4-hydroxyphenylacetate 3-hydroxylase of Escherichia coli. A two-protein component enzyme. | Prieto MA, Garcia JL | 1994 Sep 9 | 8077235 |
| Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2. | Liu X, Dong Y, Li X, Ren Y, Li Y, Wang W, Wang L, Feng L | 2010 Feb | 19942660 |
| Crystal structure of the oxygenase component (HpaB) of the 4-hydroxyphenylacetate 3-monooxygenase from Thermus thermophilus HB8. | Kim SH, Hisano T, Takeda K, Iwasaki W, Ebihara A, Miki K | 2007 Nov 9 | 17804419 |
| Kinetic mechanisms of the oxygenase from a two-component enzyme, p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii. | Sucharitakul J, Chaiyen P, Entsch B, Ballou DP | 2006 Jun 23 | 16627482 |
| Cloning and expression of p-hydroxyphenylacetate 3-hydroxylase from Acinetobacter baumannii: evidence of the divergence of enzymes in the class of two-protein component aromatic hydroxylases. | Thotsaporn K, Sucharitakul J, Wongratana J, Suadee C, Chaiyen P | 2004 Oct 5 | 15451173 |
| Coordinated production and utilization of FADH2 by NAD(P)H-flavin oxidoreductase and 4-hydroxyphenylacetate 3-monooxygenase. | Louie TM, Xie XS, Xun L | 2003 Jun 24 | 12809507 |
| A novel two-protein component flavoprotein hydroxylase. | Chaiyen P, Suadee C, Wilairat P | 2001 Nov | 11683878 |
| Characterization of 4-hydroxyphenylacetate 3-hydroxylase (HpaB) of Escherichia coli as a reduced flavin adenine dinucleotide-utilizing monooxygenase. | Xun L, Sandvik ER | 2000 Feb | 10653707 |