Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.14.14.18 - heme oxygenase (biliverdin-producing) and Organism(s) Danio rerio and UniProt Accession E7F079

for references in articles please use BRENDA:EC1.14.14.18
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
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, NADPH---hemoprotein reductase. cf. EC 1.14.15.20, heme oxygenase (biliverdin-producing, ferredoxin).
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Danio rerio
UNIPROT: E7F079
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The taxonomic range for the selected organisms is: Danio rerio
The enzyme appears in selected viruses and cellular organisms
Synonyms
heme oxygenase-1, heme oxygenase, hmox1, heme oxygenase 1, haem oxygenase, hsp32, heme oxygenase-2, hmox2, heme oxygenase 2, hmox1a, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
haem oxygenase
-
-
-
-
ORP33 proteins
-
-
-
-
oxygenase, heme (decyclizing)
-
-
-
-
proteins, specific or class, ORP33 (oxygen-regulated protein 33,000-mol.-wt.)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protoheme,NADPH-hemoprotein reductase:oxygen oxidoreductase (alpha-methene-oxidizing, hydroxylating)
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).
CAS REGISTRY NUMBER
COMMENTARY hide
9059-22-7
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform Hmox2b
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
E7F079_DANRE
318
1
35299
TrEMBL
other Location (Reliability: 1)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of Hmox1a, Hmox1b and biliverdin reductase b is significantly induced in zebrafish eleutheroembryos in response to pro-oxidants cadmium, hemin and tert-butylhydroquinone
expression of isoforms Hmox1a, Hmox2a and Hmox2b is significantly induced in male liver tissues in response to 96 hour cadmium exposure (20 microM). Hmox2a and Hmox2b are significantly induced in male brain samples
expression of Hmox1a, Hmox1b and biliverdin reductase b is significantly induced in zebrafish eleutheroembryos in response to pro-oxidants cadmium, hemin and tert-butylhydroquinone
expression of isoform Hmox2a is significantly reduced in male gill samples in response to the 96 hour cadmium exposure
expression of isoforms Hmox1a, Hmox2a and Hmox2b is significantly induced in male liver tissues in response to 96 hour cadmium exposure (20 microM). Hmox2a and Hmox2b are significantly induced in male brain samples
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Holowiecki, A.; OShields, B.; Jenny, M.J.
Characterization of heme oxygenase and biliverdin reductase gene expression in zebrafish (Danio rerio) Basal expression and response to pro-oxidant exposures
Toxicol. Appl. Pharmacol.
311
74-87
2016
Danio rerio (A0A1D8GR35), Danio rerio (A7MD59), Danio rerio (B0UXS0), Danio rerio (E7F079), Danio rerio
Manually annotated by BRENDA team