KEGG   ENZYME: 1.14.14.18Help
Entry
EC 1.14.14.18               Enzyme                                 

Name
heme oxygenase (biliverdin-producing);
ORP33 proteins;
haem oxygenase (ambiguous);
heme oxygenase (decyclizing) (ambiguous);
heme oxidase (ambiguous);
haem oxidase (ambiguous);
heme oxygenase (ambiguous);
heme,hydrogen-donor:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen into the other donor
BRITE hierarchy
Sysname
protoheme,NADPH---hemoprotein reductase:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
Reaction(IUBMB)
protoheme + 3 [reduced NADPH---hemoprotein reductase] + 3 O2 = biliverdin + Fe2+ + CO + 3 [oxidized NADPH---hemoprotein reductase] + 3 H2O [RN:R00311]
Reaction(KEGG)
Substrate
protoheme [CPD:C00032];
[reduced NADPH---hemoprotein reductase] [CPD:C03024];
O2 [CPD:C00007]
Product
biliverdin [CPD:C00500];
Fe2+ [CPD:C14818];
CO [CPD:C00237];
[oxidized NADPH---hemoprotein reductase] [CPD:C03161];
H2O [CPD:C00001]
Comment
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 [4]. 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, NADPH---hemoprotein reductase. cf. EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin).
History
EC 1.14.14.18 created 1972 as EC 1.14.99.3, modified 2006, transferred 2015 to EC 1.14.14.18, modified 2016
Pathway
Porphyrin and chlorophyll metabolism
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K00510  
heme oxygenase 1
K21418  
heme oxygenase 2
Genes
HSA: 
3162(HMOX1) 3163(HMOX2)
PTR: 
453880(HMOX2) 470195(HMOX1)
PPS: 
100977821(HMOX1) 100995961(HMOX2)
GGO: 
101149599(HMOX2) 101152785(HMOX1)
PON: 
100173339(HMOX1) 100451286(HMOX2)
NLE: 
100587046(HMOX1) 100599593(HMOX2)
MCC: 
705461(HMOX2) 719266(HMOX1)
MCF: 
101926565(HMOX1) 102143766(HMOX2)
CSAB: 
103223230(HMOX1) 103227650(HMOX2)
RRO: 
104654687(HMOX2) 104682468(HMOX1)
RBB: 
108538293(HMOX2) 108540867(HMOX1)
CJC: 
SBQ: 
101039608(HMOX1) 101053852(HMOX2)
MMU: 
15368(Hmox1) 15369(Hmox2)
RNO: 
24451(Hmox1) 79239(Hmox2)
CGE: 
100756872(Hmox1) 100773727(Hmox2)
NGI: 
103742105(Hmox1) 103744546(Hmox2)
HGL: 
101708868(Hmox1) 101718879(Hmox2)
CCAN: 
109692950(Hmox1) 109694248(Hmox2)
OCU: 
100008919(HMOX1) 100009523(HMOX2)
TUP: 
102472031(HMOX2) 102485781(HMOX1)
CFA: 
442987(HMOX1) 479864(HMOX2)
AML: 
100472787(HMOX2) 100479189(HMOX1)
UMR: 
103668554(HMOX2) 103676557(HMOX1)
FCA: 
101092621(HMOX1) 101093823(HMOX2)
PTG: 
102948800(HMOX1) 102960470(HMOX2)
AJU: 
106978811(HMOX2) 106981079(HMOX1)
BTA: 
510243(HMOX2) 513221(HMOX1)
BOM: 
102274047(HMOX2) 102281265(HMOX1)
BIU: 
109559493(HMOX1) 109578491(HMOX2)
PHD: 
102322748(HMOX2) 102333615(HMOX1)
CHX: 
100860951(HMOX1) 102189453(HMOX2)
OAS: 
101102279(HMOX2) 101120910(HMOX1)
SSC: 
396622(HMOX2) 445512(HMOX1)
CFR: 
102503731(HMOX2) 102505023(HMOX1)
CDK: 
105097386(HMOX1) 105099820(HMOX2)
BACU: 
103012514(HMOX2) 103018426(HMOX1)
LVE: 
103077914(HMOX1) 103090745(HMOX2)
ECB: 
100066114(HMOX2) 100069058(HMOX1)
EPZ: 
103543240(HMOX1) 103553961(HMOX2)
EAI: 
106825719(HMOX1) 106826005(HMOX2)
MYB: 
102248030(HMOX1) 102253515(HMOX2)
MYD: 
102764042(HMOX2) 102767690(HMOX1)
HAI: 
109377639(HMOX1) 109392113(HMOX2)
RSS: 
109445766(HMOX1) 109460746(HMOX2)
PALE: 
102880347(HMOX1) 102882902(HMOX2)
LAV: 
100662132(HMOX2) 100673521(HMOX1)
MDO: 
SHR: 
100925365(HMOX1) 100928954(HMOX2)
OAA: 
100078850(HMOX2) 107547784(HMOX1)
GGA: 
396287(HMOX1) 416663(HMOX2)
MGP: 
100541778(HMOX2) 100551243(HMOX1)
CJO: 
107314345(HMOX1) 107320929(HMOX2)
APLA: 
101801310(HMOX2) 101805057(HMOX1)
ACYG: 
106035937(HMOX1)
TGU: 
100190323(HMOX2) 100226348(HMOX1)
GFR: 
102032618(HMOX2) 102043181(HMOX1)
FAB: 
101817237(HMOX2) 101817317(HMOX1)
PHI: 
102101610(HMOX1) 102104458(HMOX2)
PMAJ: 
107205203(HMOX1)
CCW: 
104684958(HMOX2) 104696269(HMOX1)
FPG: 
101915244(HMOX1) 101921302(HMOX2)
FCH: 
102047339(HMOX2) 102055466(HMOX1)
CLV: 
102084894(HMOX1) 106145636(HMOX2)
AAM: 
106482411(HMOX2) 106488415(HMOX1)
ASN: 
102368811(HMOX2) 102373399(HMOX1)
AMJ: 
102573866(HMOX1) 102575746(HMOX2)
PSS: 
102446230(HMOX2) 102462727(HMOX1)
CMY: 
102940527(HMOX1) 102942411(HMOX2)
CPIC: 
101931937(HMOX2) 101950994(HMOX1)
ACS: 
100555210(hmox1)
PVT: 
110075944(HMOX1) 110089101(HMOX2)
PBI: 
103054508(HMOX2) 103065892(HMOX1)
GJA: 
107109317(HMOX2) 107109423(HMOX1)
XLA: 
398965(hmox1.S) 444101(hmox2.L) 734976(hmox1.L)
XTR: 
100488303(hmox1) 780096(hmox2)
NPR: 
108793696(HMOX1) 108796525(HMOX2)
DRE: 
100002875(hmox2a) 100329531(hmox2b) 402970(hmox1b) 791518(hmox1a)
SRX: 
SANH: 
SGH: 
IPU: 
AMEX: 
TRU: 
101070079(hmox1) 101074254(hmox2)
TNG: 
LCO: 
NCC: 
MZE: 
OLA: 
XMA: 
CSEM: 
103393059(hmox2) 103393699(hmox1)
LCF: 
HCQ: 
BPEC: 
SASA: 
ELS: 
SFM: 
LCM: 
102354266(HMOX1) 102360501(HMOX2)
CMK: 
CIN: 
DME: 
DPO: 
DAN: 
DER: 
DPE: 
DSE: 
DSI: 
Dsimw501_GD18775(Dsim_GD18775)
DWI: 
DYA: 
DGR: 
DMO: 
DVI: 
MDE: 
AGA: 
AAG: 
CQU: 
AME: 
494506(Ho)
BIM: 
BTER: 
SOC: 
AEC: 
ACEP: 
CFO: 
NVI: 
BMOR: 
DPL: 
PXY: 
API: 
PHU: 
DPX: 
OBI: 
NVE: 
ADF: 
 » show all
Taxonomy
Reference
1  [PMID:18477]
  Authors
Maines MD, Ibrahim NG, Kappas A.
  Title
Solubilization and partial purification of heme oxygenase from rat liver.
  Journal
J. Biol. Chem. 252 (1977) 5900-3.
Reference
2  [PMID:6897023]
  Authors
Sunderman FW Jr, Downs JR, Reid MC, Bibeau LM.
  Title
Gas-chromatographic assay for heme oxygenase activity.
  Journal
Clin. Chem. 28 (1982) 2026-32.
Reference
3  [PMID:4370250]
  Authors
Yoshida T, Takahashi S, Kikuchi G.
  Title
Partial purification and reconstitution of the heme oxygenase system from pig spleen microsomes.
  Journal
J. Biochem. (Tokyo). 75 (1974) 1187-91.
Reference
4  [PMID:105935]
  Authors
Noguchi M, Yoshida T, Kikuchi G.
  Title
Specific requirement of NADPH-cytochrome c reductase for the microsomal heme oxygenase reaction yielding biliverdin IX alpha.
  Journal
FEBS. Lett. 98 (1979) 281-4.
Reference
5  [PMID:12500973]
  Authors
Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, Ortiz de Montellano PR, Poulos TL.
  Title
Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1.
  Journal
J. Biol. Chem. 278 (2003) 7834-43.
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9059-22-7

DBGET integrated database retrieval system