CATH Classification

Domain Context

CATH Clusters

Superfamily Heme oxygenase-like
Functional Family Heme oxygenase 1

Enzyme Information

1.14.14.18
Heme oxygenase (biliverdin-producing).
based on mapping to UniProt P09601
Protoheme + 3 [reduced NADPH--hemoprotein reductase] + 3 O(2) = biliverdin + Fe(2+) + CO + 3 [oxidized NADPH--hemoprotein reductase] + 3 H(2)O.
-!- This mammalian enzyme participates in the degradation of heme. -!- The terminal oxygen atoms that are incorporated into the carbonyl groups of pyrrole rings A and B of biliverdin are derived from two separate oxygen molecules. -!- The third oxygen molecule provides the oxygen atom that converts the alpha-carbon to CO. -!- The enzyme requires NAD(P)H and EC 1.6.2.4. -!- Cf. EC 1.14.15.20. -!- Formerly EC 1.14.99.3.

UniProtKB Entries (1)

P09601
HMOX1_HUMAN
Homo sapiens
Heme oxygenase 1

PDB Structure

PDB 3TGM
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
A novel, "double-clamp" binding mode for human heme oxygenase-1 inhibition.
Rahman, M.N., Vlahakis, J.Z., Vukomanovic, D., Lee, W., Szarek, W.A., Nakatsu, K., Jia, Z.
Plos One