EC 1.14.11.45 - L-isoleucine 4-hydroxylase

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IntEnz Enzyme Nomenclature
EC 1.14.11.45

Names

Accepted name:
L-isoleucine 4-hydroxylase
Other name:
ido (gene name)
Systematic name:
L-isoleucine,2-oxoglutarate:oxygen oxidoreductase (4-hydroxylating)

Reaction

Comments:

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
UniProtKB/Swiss-Prot:

References

  1. Kodera, T., Smirnov, S. V., Samsonova, N. N., Kozlov, Y. I., 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: 506-510 (2009). [PMID: 19850012]
  2. Hibi, M., Kawashima, T., Kodera, T., Smirnov, S. V., Sokolov, P. M., 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: 6926-6930 (2011). [PMID: 21821743]
  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)/α ketoglutarate-dependent dioxygenase.
    Tetrahedron Asym 24: 990-994 (2013).

[EC 1.14.11.45 created 2014]