Expasy logo

ENZYME

ENZYME entry: EC 1.14.99.57

Accepted Name
heme oxygenase (mycobilin-producing)
Reaction catalysed
  • 3 AH2 + 2 H(+) + heme b + 3 O2 <=> 3 A + Fe(2+) + 3 H2O + mycobilin a
  • 3 AH2 + 2 H(+) + heme b + 3 O2 <=> 3 A + Fe(2+) + 3 H2O + mycobilin b
Comment(s)
  • 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 alpha-meso-carbon at the ring cleavage site as an aldehyde group.
  • EC 1.6.2.4 can act as electron donor in vitro.
Cross-references
BRENDA1.14.99.57
EC2PDB1.14.99.57
ExplorEnz1.14.99.57
PRIAM enzyme-specific profiles1.14.99.57
KEGG Ligand Database for Enzyme Nomenclature1.14.99.57
IUBMB Enzyme Nomenclature1.14.99.57
IntEnz1.14.99.57
MEDLINEFind literature relating to 1.14.99.57
MetaCyc1.14.99.57
Rhea expert-curated reactions1.14.99.57
UniProtKB/Swiss-Prot
P9WKH2, MHUD_MYCTOP9WKH3, MHUD_MYCTU

View entry in original ENZYME format
View entry in raw text format (no links)
All UniProtKB/Swiss-Prot entries referenced in this entry, with possibility to download in different formats, align etc.
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.99.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.14.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 1.-.-.-