EC Number   |
BRENDA No. |
Title |
Journal |
Volume |
Pages  |
Year |
Organism |
PubMed ID |
|---|
    1.14.11.17 | 657933 |
X-ray crystal structure of Escherichia coli taurine/alpha-ketoglutarate dioxygenase complexed to ferrous iron and substrates |
Biochemistry |
41 |
5185-5192 |
2002 |
Escherichia coli |
11955067 |
| 1.14.11.17 | 743152 |
Atom tunneling in the hydroxylation process of taurine/alpha-ketoglutarate dioxygenase identified by quantum mechanics/molecular mechanics simulations |
J. Phys. Chem. B |
121 |
5347-5354 |
2017 |
Escherichia coli |
28490178 |
| 1.14.11.17 | 657996 |
Substrate-induced conformational changes in Escherichia coli taurine/alpha-ketoglutarate dioxygenase and insight into the oligomeric structure |
Biochemistry |
42 |
5547-5554 |
2003 |
Escherichia coli |
12741810 |
| 1.14.11.17 | 685159 |
Probing the iron-substrate orientation for taurine/alpha-ketoglutarate dioxygenase using deuterium electron spin echo envelope modulation spectroscopy |
Biochemistry |
46 |
5951-5959 |
2007 |
Escherichia coli |
17469855 |
| 1.14.11.17 | 701264 |
Facile synthesis of 1,1-[2H2]-2-methylaminoethane-1-sulfonic acid as a substrate for taurine a ketoglutarate dioxygenase (TauD) |
Tetrahedron Lett. |
50 |
611-613 |
2009 |
Escherichia coli |
- |
| 1.14.11.17 | 687288 |
Spectroscopic and computational evaluation of the structure of the high-spin Fe(IV)-oxo intermediates in taurine: alpha-ketoglutarate dioxygenase from Escherichia coli and its His99Ala ligand variant |
J. Am. Chem. Soc. |
129 |
6168-6179 |
2007 |
Escherichia coli |
17451240 |
| 1.14.11.17 | 674930 |
Self-hydroxylation of taurine/alpha-ketoglutarate dioxygenase: evidence for more than one oxygen activation mechanism |
J. Biol. Inorg. Chem. |
11 |
63-72 |
2006 |
Escherichia coli |
16320009 |
| 1.14.11.17 | 671301 |
An assay for Fe(II)/2-oxoglutarate-dependent dioxygenases by enzyme-coupled detection of succinate formation |
Anal. Biochem. |
353 |
69-74 |
2006 |
Escherichia coli |
16643838 |
| 1.14.11.17 | 697475 |
Elucidating enzyme mechanism and intrinsic chemical properties of short-lived intermediates in the catalytic cycles of cysteine dioxygenase and taurine/alpha-ketoglutarate dioxygenase |
Coord. Chem. Rev. |
253 |
754-768 |
2009 |
Homo sapiens |
- |
| 1.14.11.17 | 765270 |
Strongly coupled redox-linked conformational switching at the active site of the non-heme iron-dependent dioxygenase, TauD |
J. Phys. Chem. B |
123 |
7785-7793 |
2019 |
Escherichia coli |
31433947 |
