EC 1.14.99.57 - Heme oxygenase (mycobilin-producing)

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IntEnz Enzyme Nomenclature
EC 1.14.99.57

Names

Accepted name:
heme oxygenase (mycobilin-producing)
Other name:
mhuD (gene name)
Systematic name:
protoheme,donor:oxygen oxidoreductase (mycobilin-producing)

Reactions

Comments:

The enzyme, characterized from the bacterium Mycobacterium tuberculosis, is involved in heme degradation and iron utilization. The enzyme binds two stacked protoheme molecules per monomer. Unlike the canonical heme oxygenases, the enzyme does not release carbon monoxide or formaldehyde. Instead, it forms unique products, named mycobilins, that retain the α-meso-carbon at the ring cleavage site as an aldehyde group. EC 1.6.2.4, NADPH-hemoprotein reductase, can act as electron donor in vitro.

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. Chim, N., Iniguez, A., Nguyen, T. Q., Goulding, C. W.
    Unusual diheme conformation of the heme-degrading protein from Mycobacterium tuberculosis.
    J. Mol. Biol. 395: 595-608 (2010). [PMID: 19917297]
  2. Nambu, S., Matsui, T., Goulding, C. W., Takahashi, S., Ikeda-Saito, M.
    A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO.
    J. Biol. Chem. 288: 10101-10109 (2013). [PMID: 23420845]
  3. Graves, A. B., Morse, R. P., Chao, A., Iniguez, A., Goulding, C. W., Liptak, M. D.
    Crystallographic and spectroscopic insights into heme degradation by Mycobacterium tuberculosis MhuD.
    Inorg Chem 53: 5931-5940 (2014). [PMID: 24901029]

[EC 1.14.99.57 created 2017]