Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

1.13.11.52: indoleamine 2,3-dioxygenase

This is an abbreviated version!
For detailed information about indoleamine 2,3-dioxygenase, go to the full flat file.

Word Map on EC 1.13.11.52

Reaction

D-tryptophan
+
O2
=
N-formyl-D-kynurenine

Synonyms

31854, BRAFLDRAFT_126354, CG5163, EC 1.13.1.12, hIDO, hIDO1, hTDO, IDO, IDO-1, IDO-2, IDO-I, IDO-II, IDO-III, IDO-IV, IDO1, IDO2, INDO, INDOL1, indolamine 2,3-dioxygenase, indole 2,3-dioxygenase, indoleamine 2, 3-dioxygenase, indoleamine 2,3 dioxygenase, indoleamine 2,3-dioxygenase, indoleamine 2,3-dioxygenase 1, indoleamine 2,3-dioxygenase 2, indoleamine 2,3-dioxygenase-1, indoleamine 2,3-dioxygenase-2, indoleamine 2,3-dioxygenase-like protein, indoleamine-2,3-dioxygenase, Indoleamine-pyrrole 2,3-dioxygenase, L-tryptophan 2,3-dioxygenase, L-tryptophan pyrrolase, mIDO, oxygenase, tryptophan 2,3-di-, proto-IDO, proto-indoleamine 2,3-dioxygenase, superoxygenase, TDO, TDO2, TioF, TO, TRPO, Tryptamin 2,3-dioxygenase, tryptamine 2,3-dioxygenase, tryptophan 2,3-dioxygenase, tryptophan dioxygenase, tryptophan oxygenase, tryptophan peroxidase, tryptophan pyrrolase, tryptophan-2,3-dioxygenase, tryptophanase, v1g244579, Vermilion protein

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.52 indoleamine 2,3-dioxygenase

Engineering

Engineering on EC 1.13.11.52 - indoleamine 2,3-dioxygenase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A264G
site-directed mutagenesis, mutation of a loop residues that connects the hIDO domains
A4T
variant observed in Homo sapiens
C129A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D274A
-
mutant without enzyme activity, may be distal ligand or essential in maintaining the conformation of the heme pocket
F185A
mutation eliminates activity of the enzyme
F226A
-
drastically reduced the dioxygenase activity
F227A
-
drastically reduced the dioxygenase activity
G261A
site-directed mutagenesis, mutation of a loop residues that connects the hIDO domains
G261V
site-directed mutagenesis, mutation of a loop residues that connects the hIDO domains
H16A
-
does not act as proximal ligand
H303A
H346A
-
mutant without enzyme activity, His346 is essential for heme binding
H76A
-
active site, tryptophan binding
K352A
-
mutant with diminished heme binding ability
medicine
-
IDO expression as a T-cell inhibitory effector pathway in professional antigen-presenting cells
P182A
mutation eliminates activity of the enzyme
P182A/F185A
mutation eliminates activity of the enzyme
P314A
mutation increases IC50 for kushenol E
R213E
site-directed mutagenesis, mutation of an active site residue
R231A
R231L
site-directed mutagenesis, altered structure compared to wild-type, inactive mutant
R77H
variant observed in Homo sapiens
R77K
variant not observed in Homo sapiens, used as control
S167A
site-directed mutagenesis, the mutant shows 3.6fold reduced activity compared to the wild-type enzyme, the mutant shows altered sensitivity to inhibitors compared to the wild-type enzyme
S167H
S167L
site-directed mutagenesis, mutation of an active site residue
S263A
T342A
-
site-directed mutagenesis, the mutation only slightly perturbs the global structural properties of the enzyme, but it totally abolishes the substrate stereoselectivity, substrate-free spectrum
T379A
V109A
-
mutant maintained heme binding ability
Y42F
-
active site, tryptophan binding
H238A
-
mutant retains little or no heme, strong reduction of activity
H75A
-
mutant retains little or no heme, strong reduction of activity
H55S
active site, tryptophan binding
T254A
-
ternary complex molecular simulations. The mutation causes the opening of the loop 250-260 to loop 117-130, leading to a more dynamic and open distal pocket, accounting for the much lower substrate affinity (i.e. higher Km). On the other hand, the simulation data of the ferryl/L-indole 2,3-epoxide intermediate indicate that the T254A mutation also results in the opening of the loop 250-260 to loop 117-130. It leads to local reorganization of the H-bonding interactions surrounding the NH3+ group of the substrate, resulting in an open conformation, in which the H-bond between the NH3+ and the epoxide is temporarily lost
H339A
-
used as negative control
additional information