Biliverdin reductase A

BLVRA
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2H63
Identifiers
Aliases	BLVRA, BLVR, BVR, BVRA, biliverdin reductase A
External IDs	OMIM: 109750 MGI: 88170 HomoloGene: 572 GeneCards: BLVRA
Gene location (Human)
Chr.	Chromosome 7 (human)[1]
End	43,807,342 bp[1]
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)[2]
End	127,097,084 bp[2]
Gene ontology
Molecular function	• GO:0001948 protein binding; • metal ion binding; • zinc ion binding; • oxidoreductase activity; • biliverdin reductase activity;
Cellular component	• extracellular exosome; • cytoplasm; • cytosol;
Biological process	• heme catabolic process; • oxidation-reduction process;
	Sources:Amigo / QuickGO
Orthologs
	644
	109778
	ENSG00000106605
	ENSMUSG00000001999
	P53004
	Q9CY64
	NM_000712; NM_001253823
	NM_026678
	NP_000703; NP_001240752
	NP_080954
	Wikidata
View/Edit Human	View/Edit Mouse

biliverdin reductase A
	Biliverdin reductase A dimer, Human
Identifiers
EC number	1.3.1.24
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search
PMC	articles
PubMed	articles
NCBI	proteins

Biliverdin reductase A is a protein that in humans is encoded by the BLVRA gene.[5]

Function

The protein encoded by this gene belongs to the biliverdin reductase family, members of which catalyze the conversion of biliverdin to bilirubin in the presence of NADPH or NADH.[5]

Mutations in this gene are associated with hyperbiliverdinemia.[5]

GRCh38: Ensembl release 89: ENSG00000106605 - Ensembl, May 2017
GRCm38: Ensembl release 89: ENSMUSG00000001999 - Ensembl, May 2017
"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
"Entrez Gene: Biliverdin reductase A".

Human BLVRA genome location and BLVRA gene details page in the UCSC Genome Browser.
PDBe-KB provides an overview of all the structure information available in the PDB for Human Biliverdin reductase A

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.

Oxidoreductases: CH–CH oxidoreductases (EC 1.3)
1.3.1: NAD/NADP acceptor	Enoyl-acyl carrier protein reductase/Enoyl ACP reductase 7-Dehydrocholesterol reductase Biliverdin reductase 2,4 Dienoyl-CoA reductase Dihydroxymethyloxo-tetrahydroquinoline dehydrogenase
1.3.3: Oxygen acceptor	Dihydroorotate dehydrogenase Coproporphyrinogen III oxidase Protoporphyrinogen oxidase Bilirubin oxidase Acyl-CoA oxidase Dihydrouracil oxidase Tetrahydroberberine oxidase Secologanin synthase Tryptophan alpha,beta-oxidase Pyrroloquinoline-quinone synthase L-galactonolactone oxidase
1.3.5: Quinone	Succinate dehydrogenase SDHA SDHB SDHC SDHD
1.3.99: Other acceptors	Fumarate reductase Butyryl-CoA dehydrogenase Acyl CoA dehydrogenase ACADSB ACADS 5α-reductase SRD5A1 SRD5A2 SRD5A3 Glutaryl-CoA dehydrogenase Isovaleryl coenzyme A dehydrogenase 3-oxo-5beta-steroid 4-dehydrogenase

Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)