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
ec00860  Porphyrin and chlorophyll metabolism
ec01100  Metabolic pathways
ec01110  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: 100395145(HMOX2) 100405992 100414343(HMOX1)
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)
ORO: 101364369(HMOX1) 101367073(HMOX2)
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)
OOR: 101279301(HMOX2) 101282134(HMOX1)
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: 100019502(HMOX2) 100024355(HMOX1) 100030714
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: 106033412(HMOX2) 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) 107211143(HMOX2)
CCW: 104684958(HMOX2) 104696269(HMOX1)
FPG: 101915244(HMOX1) 101921302(HMOX2)
FCH: 102047339(HMOX2) 102055466(HMOX1)
CLV: 102084894(HMOX1) 106145636(HMOX2)
EGZ: 104121977(HMOX2) 104134285(HMOX1)
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)
IPU: 100528875(hmox) 108272923 108272926 108276515(hmox2) 108278324(hmox1)
AMEX: 103022889 103032679(hmox2) 103044464(hmox1)
TRU: 101070079(hmox1) 101074254(hmox2)
NFU: 107376240(hmox1) 107376482(hmox2) 107382233
CSEM: 103393059(hmox2) 103393699(hmox1)
BPEC: 110167460(hmox2) 110172090(hmox1) 110172617
ELS: 105006006 105012149(hmox) 105013172(hmox1)
SFM: 108928847(hmox2) 108939753
LCM: 102354266(HMOX1) 102360501(HMOX2)
CMK: 103178752(hmox2) 103189669
CIN: 100185311
DME: Dmel_CG14716(Ho)
DSI: Dsimw501_GD18775(Dsim_GD18775)
MDE: 101894027
AAG: 5570153
AME: 494506(Ho)
BIM: 100743864
BTER: 100651999
SOC: 105203060
AEC: 105154734
ACEP: 105626739
CFO: 105251022
LHU: 105671105
PGC: 109860607
NVI: 100115195(Ho)
BMOR: 732895
PMAC: 106711006
PRAP: 110995109
API: 100162545
DNX: 107163196
ZNE: 110831500
OBI: 106879648
ADF: 107331736
 » 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 252:5900-3 (1977)
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 28:2026-32 (1982)
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) 75:1187-91 (1974)
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 98:281-4 (1979)
DOI:10.1016/0014-5793(79)80200-8
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 278:7834-43 (2003)
DOI:10.1074/jbc.M211450200
Other DBs
ExplorEnz - The Enzyme Database: 1.14.14.18
IUBMB Enzyme Nomenclature: 1.14.14.18
ExPASy - ENZYME nomenclature database: 1.14.14.18
BRENDA, the Enzyme Database: 1.14.14.18
CAS: 9059-22-7

DBGET integrated database retrieval system