Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor

L-isoleucine,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)

L-isoleucine + 2-oxoglutarate + O2 = (4S)-4-hydroxy-L-isoleucine + succinate + CO2 [RN:R10723]

R10723

L-isoleucine [CPD:C00407];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]

The enzyme, characterized from the bacterium Bacillus thuringiensis, can also catalyse the hydroxylation of L-leucine, L-norvaline, L-norleucine, and L-allo-isoleucine, as well as the sulfoxidation of L-methionine, L-ethionine, S-methyl-L-cysteine, S-ethyl-L-cysteine, and S-allyl-L-cysteine.

EC 1.14.11.45 created 2014

1  [PMID:19850012]

Kodera T, Smirnov SV, Samsonova NN, Kozlov YI, Koyama R, Hibi M, Ogawa J, Yokozeki K, Shimizu S

A novel l-isoleucine hydroxylating enzyme, l-isoleucine dioxygenase from Bacillus thuringiensis, produces (2S,3R,4S)-4-hydroxyisoleucine.

Biochem. Biophys. Res. Commun. 390 (2009) 506-10.

[ag:ADJ94127]

2  [PMID:21821743]

Hibi M, Kawashima T, Kodera T, Smirnov SV, Sokolov PM, Sugiyama M, Shimizu S, Yokozeki K, Ogawa J

Characterization of Bacillus thuringiensis L-isoleucine dioxygenase for production of useful amino acids.

Appl. Environ. Microbiol. 77 (2011) 6926-30.

[ag:ADJ94127]

3

Hibi, M., Kawashima, T., Yajima, H., Smirnov, S.V., Kodera, T., Sugiyama, M., Shimizu, S., Yokozeki, K., and Ogawa, J.

Enzymatic synthesis of chiral amino acid sulfoxides by Fe(II)/alpha ketoglutarate-dependent dioxygenase.

Tetrahedron Asym 24 (2013) 990-994.