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Information on EC 1.3.1.24 - biliverdin reductase and Organism(s) Rattus norvegicus and UniProt Accession P46844

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EC Tree
     1 Oxidoreductases
         1.3 Acting on the CH-CH group of donors
             1.3.1 With NAD+ or NADP+ as acceptor
                1.3.1.24 biliverdin reductase
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This record set is specific for:
Rattus norvegicus
UNIPROT: P46844 not found.
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Word Map
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
Synonyms
bvr, biliverdin reductase, bvr-a, blvra, biliverdin reductase a, biliverdin reductase-a, bvr-b, rv2074, biliverdin-ixalpha reductase, biliverdin ixalpha reductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biliverdin IXalpha reductase
-
biliverdin reductase
-
Biliverdin reductase-A
-
biliverdin IXalpha reductase
-
-
biliverdin reductase
-
-
BV reductase
-
-
BVRB
-
isoform, predominant during fetal development
reductase, biliverdin
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
bilirubin + NAD(P)+ = biliverdin + NAD(P)H + H+
show the reaction diagram
catalysis via hydride transfer from NADH
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
SYSTEMATIC NAME
IUBMB Comments
bilirubin:NAD(P)+ oxidoreductase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9074-10-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
biliverdin IXalpha + NAD(P)H + H+
bilirubin IXalpha + NAD(P)+
show the reaction diagram
substrate of BVRA but not of BVRB isoform
-
-
ir
insulin receptor substrate 1 + NAD(P)H
?
show the reaction diagram
phosphorylates serine residues in insulin receptor substrate 1
-
-
?
bilirubin + NAD+
biliverdin + NADH + H+
show the reaction diagram
bilirubin + NADP+
biliverdin + NADPH + H+
show the reaction diagram
-
-
-
-
r
biliverdin + NAD(P)H
bilirubin + NAD(P)+
show the reaction diagram
biliverdin + NAD(P)H + H+
bilirubin + NAD(P)+
show the reaction diagram
-
-
-
-
?
biliverdin + NADH + H+
bilirubin + NAD+
show the reaction diagram
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
show the reaction diagram
-
-
-
r
insulin receptor substrate 1 + NAD(P)H
?
show the reaction diagram
phosphorylates serine residues in insulin receptor substrate 1
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
bilirubin + NAD+
biliverdin + NADH + H+
show the reaction diagram
-
-
-
-
r
bilirubin + NADP+
biliverdin + NADPH + H+
show the reaction diagram
-
-
-
-
r
biliverdin + NADH + H+
bilirubin + NAD+
show the reaction diagram
-
-
-
r
biliverdin + NADPH + H+
bilirubin + NADP+
show the reaction diagram
-
-
-
r
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
additional information
-
the enzyme shows dual cofactor- and pH-dependency in activity
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
bilirubin
Biliverdin
HgCl2
-
irreversible inhibition
iodoacetamide
Iron-hematoporphyrin
-
competitive, acts as biliverdin-bilirubin analog
Metalloporphyrin complexes
-
-
-
N-ethylmaleimide
NAD+
-
product inhibition
NADP+
-
product inhibition
p-chloromercuribenzoate
SH-reactive agent
-
34000 Da form extremely sensitive to, larger 68000 Da form lacks sensitivity to
-
SH-reagents
-
zinc-protoporphyrin
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cGMP
-
BVR localizes into the nucleus upon activation by cGMP
cytokine
-
induces BVR transcription
-
hyperthermia
-
induces BVR transcription
-
oxidant
-
activates
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.003 - 0.1633
Biliverdin
0.023
biliverdin IXalpha
-
-
0.27 - 0.567
NADH
0.0023 - 0.0133
NADPH
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.7 - 69.3
Biliverdin
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
20 - 15100
Biliverdin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0098
bilirubin
-
at pH 7
0.0019
NAD+
-
at pH 7
0.0454 - 0.583
NADP+
-
at pH 8.7
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.7
optimal pH value for NADH as cofactor
8.7
optimal pH value for NADPH as cofactor
7
-
biliverdin + NADH
8.5
-
biliverdin + NADPH
additional information
-
the enzyme shows dual cofactor- and pH-dependency in activity
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 42
-
exposure of male rats to 42°C for 20 min does not decrease brain biliverdin activity, the 1.5 kb biliverdin reductase mRNA displayes thermal tolerance too
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
pulmonary arterial smooth muscle cell
Manually annotated by BRENDA team
-
inflamed lesions, increased in rats with clinical autoimmune encephalomyelitis, also present in both white and gray matter
Manually annotated by BRENDA team
-
sparingly expressed
Manually annotated by BRENDA team
-
sparingly expressed
Manually annotated by BRENDA team
additional information
-
the BVR activity progressively increases after birth and reaches adult levels by postpartum day 28
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
metabolism
key enzymes of the hemoglobin degradation cascade. Biliverdin reductase is probably also involved in protecting choroid plexus epithelial cells and the blood-cerebrospinal fluid barrier from the negative effects of subarachnoid hemorrhage
physiological function
a biliverdin reductase-A (BLVRA)-dependent mechanism regulates inflammatory responses and splenocyte death after germinal matrix hemorrhage (GMH)
malfunction
-
using BVR siRNA, blocking generation of bilirubin, reverses the effect of hypoxia on enhancing cell survival and apoptotic protein (Bcl-2, procasepase-9, procasepase-3) expression, preventing nuclear shrinkage, DNA fragmentation and mitochondrial depolarization in starved pulmonary arterial smooth muscle cell, which are recovered by exogenous bilirubin. The inhibitory effect of bilirubin on pulmonary arterial smooth muscle cell apoptosis under hypoxic condition is blocked by the inhibitor of ERK1/2 pathway
metabolism
-
the heme oxygenase/biliverdin reductase axis is the main metabolic pathway for heme degradation. Activation suirng stress results in increased heme degradation and acceleration of biliverdin transformation to bilirubin
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
BIEA_RAT
295
0
33566
Swiss-Prot
other Location (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
33500
BVRA, SDS-PAGE
21000
BVRB, SDS-PAGE
30100
-
SDS-PAGE
30400 - 31400
-
various forms, two dimensional PAGE
33000
-
SDS-PAGE
34000
34000 - 36000
-
liver
46000
-
form 2 in liver, SDS-PAGE
54000
-
liver (form 2), HPLC
56000
-
minor form 2, SDS-PAGE
60000
-
expression of rat biliverdin reductase as a gluthatione-S-transferase protein, SDS-PAGE
68000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 33500, BVRA, SDS-PAGE
dimer
-
2 * 34000, liver (form I), minor dimeric form, SDS-PAGE
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
apo enzyme and in complex with NADH
apo-, NADP+-bound and biliverdin-NADP+ complex forms of the enzyme, hanging drop vapor diffusion method, using 15% (w/v) PEG 4,000, 50mM Tris-HCl (pH 7.25), 0.2M sodium acetate and 0.2mM Cymal-2
BVR-NADH complex, NH2-terminal domain in dinucleotide binding
-
crystals of the biliverdin reductase obtained by sitting-drop vapour-diffusion method, enzyme diffraction data collected to 1.6 A, crystals belong to the orthorhombic space group P212121 with unit-cell parameters a=58.89, b=70.41, c=87.76 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Y97F
50% of activity compared to wild type
C280A
-
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 280 principally functions in substrate binding
C291A
-
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 291 is predominantly involved in cofactor binding.
C73A
-
the modification of the amino-proximal cysteine, which is flanked by a tyrosine residue, completely inactivates the enzyme with NADH at pH 6.75 and NADPH at pH 8.7
R171A
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171E
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
R171K
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y97F
the mutant shows strongly reduced catalytic efficiency compared to the wild type enzyme
Y98F
the mutant shows about wild type catalytic efficiency
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
-
0.1 M potassium phosphate buffer, most stable
437789
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
-
10 min, no loss of activity
55
-
10 min, complete loss of activity
60
-
1 h, 15-30% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
loss of activity in solutions with protein concentration below 0.030-0.035 mg/ml
-
NADPH stabilizes
-
repeated freeze-thawing: little loss of activity , no significant loss of activity, partially purified enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, several months -25°C, 1 month: no loss of activity, 2 months: 50% loss of activity
-
0-4°C, 5 days
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
protein extracts of transgenic Arabidopsis thaliana plants are prepared
nickel affinity gel chromatography and Sephacryl S-200 gel filtration
purification of biliverdin reductase expressed in Escherichia coli and from rat tissue
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
using the vector pBIB-KAN a plant transformation vector, containing the CAB3 promoter, a chloroplast targeting sequence and the BVR gene, is constructed, using pMON672 leads to a similar construct containing the MERI5 promoter
biliverdin reductase cDNA cloned into pUC18, used for expression and purification
-
expressed in Escherichia coli BL21(DE3) cells
expression in SH-SY5Y cells
-
kidney form of the enzyme cloned into the expression vector pGEX-KG
-
recombinant biliverdin reductase expressed in Escherichia coli
-
the expression of rat kidney biliverdin reductase is targeted by translational fusion of the chloroplast transit peptide sequence of the soybean small subunit of ribulose bisphosphate carboxylase gene to the enzyme cDNA, with this method transgenic Arabidopsis plants are cloned which express constitutive biliverdin reductase and display aberrant photomorphogenesis throughout their life-cycle
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increased levels of heme oxygenase-1 and biliverdin reductase protein in the choroid plexus over the entire period following subarachnoid hemorrhage induction
about 56% of the BVR expression in total lung tissue is increased by hypoxia
-
in fetal liver and maternal liver and placenta ursodeoxycholic acid up-regulates biliverdin-IX reductase
-
induction of BVR and HO-2 is mediated by the cAMP-PKA pathway and isoproterenol, overview
-
up-regulated in levels of protein and mRNA by hypoxia in pulmonary arterial smooth muscle cell
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
-
BVR may represent a novel strategy for the treatment of multiple sclerosis and other oxidative stress-mediated diseases, treatment with BVR ameliorates both clinical and pathological signs of autoimmune encephalomyelitis more efficiently than treatments with traditional antioxidant enzymes
additional information
-
regulates oxidative response and HO-1 expression
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noguchi, M.; Yoshida, T.; Kikuchi, G.
Purification and properties of biliverdin reductases from pig spleen and rat liver
J. Biochem.
86
833-848
1979
Rattus norvegicus, Sus scrofa
Manually annotated by BRENDA team
Kutty, R.K.; Maines, M.D.
Purification and characterization of biliverdin reductase from rat liver
J. Biol. Chem.
256
3956-3962
1981
Rattus norvegicus
Manually annotated by BRENDA team
Frydman, J.; Tomaro, M.L.; Rosenfeld, J.; Frydman, R.B.
Identification of the amino acid residues essential for the activity and the interconversion of the molecular forms of biliverdin reductase
Biochim. Biophys. Acta
1040
119-129
1990
Rattus norvegicus
Manually annotated by BRENDA team
Huang, T.J.; Trakshel, G.M.; Maines, M.D.
Detection of 10 variants of biliverdin reductase in rat liver by two-dimensional gel electrophoresis
J. Biol. Chem.
264
7844-7849
1989
Rattus norvegicus
Manually annotated by BRENDA team
Huang, T.J.; Trakshel, G.M.; Maines, M.D.
Multiple forms of biliverdin reductase: modification of the pattern of expression in rat liver by bromobenzene
Arch. Biochem. Biophys.
270
513-520
1989
Rattus norvegicus
Manually annotated by BRENDA team
Cascone, O.; Frydman, R.B.; Ferrara, P.; Tomaro, M.L.; Rosenfeld, J.
Molecular differences between rat-liver and rat-kidney biliverdin reductase. Implications for their in vivo regulation
Eur. J. Biochem.
179
123-130
1989
Rattus norvegicus
Manually annotated by BRENDA team
Rigney, E.M.; Phillips, O.; Mantle, T.J.
Some physical and immunological properties of ox kidney biliverdin reductase
Biochem. J.
255
431-435
1988
Bos taurus, Mus musculus, Rattus norvegicus
Manually annotated by BRENDA team
Bell, J.E.; Maines, M.D.
Kinetic properties and regulation of biliverdin reductase
Arch. Biochem. Biophys.
263
1-9
1988
Rattus norvegicus
Manually annotated by BRENDA team
Frydman, R.B.; Tomaro, M.L.; Rosenfeld, J.; Awruch, J.; Sambrotta, L.; Valasinas, A.; Frydman, B.
Biliverdin reductase: substrate specificity and kinetics
Biochim. Biophys. Acta
916
500-511
1987
Rattus norvegicus
Manually annotated by BRENDA team
Tomaro, M.L.; Frydman, R.B.; Awruch, J.; Valasinas, A.; Frydman, B.; Pandey, R.K.; Smith, K.M.
The specificity of biliverdin reductase. A study with different biliverdin types
Biochim. Biophys. Acta
791
350-356
1984
Rattus norvegicus
Manually annotated by BRENDA team
Awruch, J.; Tomaro, M.L.; Frydman, R.B.; Frydman, B.
The specificity of biliverdin reductase. The reduction of biliverdin XIII isomers
Biochim. Biophys. Acta
787
146-151
1984
Rattus norvegicus
Manually annotated by BRENDA team
Frydman, R.B.; Tomaro, M.L.; Awruch, J.; Frydman, B.
Molecular forms of biliverdin reductase from rat liver with different reduction rates for biliverdin-IX
Biochem. Biophys. Res. Commun.
105
752-758
1982
Rattus norvegicus
Manually annotated by BRENDA team
Lagarias, D.M.; Crepeau, M.W.; Maines, M.D.; Lagarias, J.C.
Regulation of photomorphogenesis by expression of mammalian biliverdin reductase in transgenic Arabidopsis plants
Plant Cell
9
675-688
1997
Rattus norvegicus
Manually annotated by BRENDA team
Sun, D.; Sato, M.; Yoshida, T.; Shimizu, H.; Miyatake, H.; Adachi, S.; Shiro, Y.; Kikuchi, A.
Crystallization and preliminary X-ray diffraction analysis of a rat biliverdin reductase
Acta Crystallogr. Sect. D
56
1180-1182
2000
Rattus norvegicus
Manually annotated by BRENDA team
Kikuchi, A.; Park, S.Y.; Miyatake, H.; Sun, D.; Sato, M.; Yoshida, T.; Shiro, Y.
Crystal structure of rat biliverdin reductase
Nat. Struct. Biol.
8
221-225
2001
Rattus norvegicus
Manually annotated by BRENDA team
Ewing, J.F.; Maines, M.D.
Immunohistochemical localization of biliverdin reductase in rat brain: age related expression of protein and transcript
Brain Res.
672
29-41
1995
Rattus norvegicus
Manually annotated by BRENDA team
Ennis, O.M.; Mantle, T.
Expression of rat biliverdin reductase as a glutathione-S-transferase fusion protein
Biochem. Soc. Trans.
23
443S
1995
Rattus norvegicus
Manually annotated by BRENDA team
Maines, M.D.; Trakshel, G.M.
Purification and characterization of human biliverdin reductase
Arch. Biochem. Biophys.
300
320-326
1993
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ewing, J.F.; Weber, C.M.; Maines, M.D.
Biliverdin reductase is heat resistant and coexpressed with constitutive and heat shock forms of heme oxygenase in brain
J. Neurochem.
61
1015-1023
1993
Rattus norvegicus
Manually annotated by BRENDA team
McCoubrey, W.K., Jr.; Maines, M.D.
Site-directed mutagenesis of cysteine residues in biliverdin reductase. Roles in substrate and cofactor binding
Eur. J. Biochem.
222
597-603
1994
Rattus norvegicus
Manually annotated by BRENDA team
Wang, J.; de Montellano, P.R.
The binding sites on human heme oxygenase-1 for cytochrome p450 reductase and biliverdin reductase
J. Biol. Chem.
278
20069-20076
2003
Rattus norvegicus
Manually annotated by BRENDA team
Whitby, F.G.; Phillips, J.D.; Hill, C.P.; McCoubrey, W.; Maines, M.D.
Crystal structure of a biliverdin IXalpha reductase enzyme-cofactor complex
J. Mol. Biol.
319
1199-1210
2002
Rattus norvegicus (P46844)
Manually annotated by BRENDA team
Franklin, K.A.; Linley, P.J.; Montgomery, B.L.; Lagarias, J.C.; Thomas, B.; Jackson, S.D.; Terry, M.J.
Misregulation of tetrapyrrole biosynthesis in transgenic tobacco seedlings expressing mammalian biliverdin reductase
Plant J.
35
717-728
2003
Rattus norvegicus
Manually annotated by BRENDA team
Liu, Y.; Liu, J.; Tetzlaff, W.; Paty, D.W.; Cynader, M.S.
Biliverdin reductase, a major physiologic cytoprotectant, suppresses experimental autoimmune encephalomyelitis
Free Radic. Biol. Med.
40
960-967
2006
Rattus norvegicus
Manually annotated by BRENDA team
Maines, M.D.
New insights into biliverdin reductase functions: linking heme metabolism to cell signaling
Physiology
20
382-389
2005
Arabidopsis sp., Canis lupus familiaris, Cavia porcellus, Gallus gallus, Cyanidium caldarium, Homo sapiens, Mus musculus, Pan troglodytes, Rattus norvegicus, Sus scrofa, Takifugu rubripes, Xenopus sp.
Manually annotated by BRENDA team
Florczyk, U.M.; Jozkowicz, A.; Dulak, J.
Biliverdin reductase: new features of an old enzyme and its potential therapeutic significance
Pharmacol. Rep.
60
38-48
2008
Rattus norvegicus, Rattus norvegicus (P46844), Homo sapiens (P30043), Homo sapiens (P53004)
Manually annotated by BRENDA team
Warnasooriya, S.N.; Montgomery, B.L.
Detection of spatial-specific phytochrome responses using targeted expression of biliverdin reductase in Arabidopsis
Plant Physiol.
149
424-433
2009
Rattus norvegicus (P46844)
Manually annotated by BRENDA team
Perez, M.J.; Castano, B.; Jimenez, S.; Serrano, M.A.; Gonzalez-Buitrago, J.M.; Marin, J.J.
Role of vitamin C transporters and biliverdin reductase in the dual pro-oxidant and anti-oxidant effect of biliary compounds on the placental-fetal unit in cholestasis during pregnancy
Toxicol. Appl. Pharmacol.
232
327-336
2008
Rattus norvegicus, Homo sapiens (P53004), Homo sapiens
Manually annotated by BRENDA team
Mancuso, C.; Barone, E.
The heme oxygenase/biliverdin reductase pathway in drug research and development
Curr. Drug Metab.
10
579-594
2009
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Ding, B.; Gibbs, P.E.; Brookes, P.S.; Maines, M.D.
The coordinated increased expression of biliverdin reductase and heme oxygenase-2 promotes cardiomyocyte survival: a reductase-based peptide counters beta-adrenergic receptor ligand-mediated cardiac dysfunction
FASEB J.
25
301-313
2010
Homo sapiens, Rattus norvegicus
Manually annotated by BRENDA team
Song, S.; Wang, S.; Ma, J.; Yao, L.; Xing, H.; Zhang, L.; Liao, L.; Zhu, D.
Biliverdin reductase/bilirubin mediates the anti-apoptotic effect of hypoxia in pulmonary arterial smooth muscle cells through ERK1/2 pathway
Exp. Cell Res.
319
1973-1987
2013
Rattus norvegicus
Manually annotated by BRENDA team
Takao, H.; Hirabayashi, K.; Nishigaya, Y.; Kouriki, H.; Nakaniwa, T.; Hagiwara, Y.; Harada, J.; Sato, H.; Yamazaki, T.; Sakakibara, Y.; Suiko, M.; Asada, Y.; Takahashi, Y.; Yamamoto, K.; Fukuyama, K.; Sugishima, M.; Wada, K.
A substrate-bound structure of cyanobacterial biliverdin reductase identifies stacked substrates as critical for activity
Nat. Commun.
8
14397
2017
Rattus norvegicus (P06762), Homo sapiens (P53004), Synechocystis sp. PCC 6803 (P72782)
Manually annotated by BRENDA team
Solar, P.; Brazda, V.; Levin, S.; Zamani, A.; Jancalek, R.; Dubovy, P.; Joukal, M.
Subarachnoid hemorrhage increases level of heme oxygenase-1 and biliverdin reductase in the choroid plexus
Front. Cell. Neurosci.
14
593305
2020
Rattus norvegicus (P46844)
Manually annotated by BRENDA team
Zhang, Y.; Ding, Y.; Lu, T.; Zhang, Y.; Xu, N.; McBride, D.W.; Tang, J.; Zhang, J.H.
Biliverdin reductase-A attenuated GMH-induced inflammatory response in the spleen by inhibiting toll-like receptor-4 through eNOS/NO pathway
J. Neuroinflammation
15
118
2018
Rattus norvegicus (P46844)
Manually annotated by BRENDA team