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CYP1B1 - Wikipedia

From Wikipedia, the free encyclopedia

CYP1B1

Available structures

PDB

Ortholog search: PDBe RCSB

List of PDB id codes
3PM0

Identifiers

Aliases

CYP1B1, CP1B, CYPIB1, GLC3A, P4501B1, cytochrome P450 family 1 subfamily B member 1, ASGD6

External IDs

OMIM: 601771; MGI: 88590; HomoloGene: 68035; GeneCards: CYP1B1; OMA:CYP1B1 - orthologs

Gene location (Human)

Chr.	Chromosome 2 (human)^[1]

Band	2p22.2	Start	38,066,973 bp^[1]
Band	2p22.2	End	38,109,902 bp^[1]

Gene location (Mouse)

Chr.	Chromosome 17 (mouse)^[2]

Band	17\|17 E3	Start	80,008,966 bp^[2]
Band	17\|17 E3	End	80,022,490 bp^[2]

RNA expression pattern

Bgee

Human

Mouse (ortholog)

Top expressed in

pericardium

cartilage tissue

synovial joint

trigeminal ganglion

spinal ganglia

synovial membrane

tendon of biceps brachii

superficial temporal artery

hair follicle

urethra

Top expressed in

stroma of bone marrow

vestibular membrane of cochlear duct

renal corpuscle

cumulus cell

ciliary body

lactiferous gland

mesenteric lymph nodes

vas deferens

ankle joint

tunica media of zone of aorta

More reference expression data

BioGPS


More reference expression data

Gene ontology
Molecular function	iron ion binding oxygen binding metal ion binding heme binding oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen oxidoreductase activity aromatase activity oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen monooxygenase activity
Cellular component	organelle membrane endoplasmic reticulum membrane intracellular membrane-bounded organelle membrane endoplasmic reticulum mitochondrion
Biological process	toxin metabolic process steroid metabolic process retina vasculature development in camera-type eye cellular response to organic cyclic compound epoxygenase P450 pathway endothelial cell-cell adhesion omega-hydroxylase P450 pathway angiogenesis cellular aromatic compound metabolic process sterol metabolic process response to toxic substance visual perception blood vessel morphogenesis trabecular meshwork development negative regulation of NF-kappaB transcription factor activity regulation of reactive oxygen species metabolic process retinal metabolic process endothelial cell migration nitric oxide biosynthetic process retinol metabolic process cell adhesion negative regulation of cell population proliferation positive regulation of apoptotic process positive regulation of receptor signaling pathway via JAK-STAT negative regulation of cell adhesion mediated by integrin xenobiotic metabolic process cellular response to hydrogen peroxide membrane lipid catabolic process retinal blood vessel morphogenesis positive regulation of angiogenesis positive regulation of vascular endothelial growth factor production intrinsic apoptotic signaling pathway in response to oxidative stress arachidonic acid metabolic process negative regulation of cell migration estrogen metabolic process collagen fibril organization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


1545


13078

Ensembl


ENSG00000138061


ENSMUSG00000024087

UniProt


Q16678


Q64429

RefSeq (mRNA)


NM_000104


NM_009994 NM_001364889

RefSeq (protein)


NP_000095


NP_034124 NP_001351818

Location (UCSC)

Chr 2: 38.07 – 38.11 Mb

Chr 17: 80.01 – 80.02 Mb

PubMed search

^[3]

^[4]

Wikidata

View/Edit Human

View/Edit Mouse

Cytochrome P450 1B1 is an enzyme that in humans is encoded by the CYP1B1 gene.^[5]

Function

CYP1B1 belongs to the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids, and other lipids. The enzyme encoded by this gene localizes to the endoplasmic reticulum (ER) and metabolizes procarcinogens such as polycyclic aromatic hydrocarbons and 17beta-estradiol.

Despite over 20 years of research on CYP1A1 and CYP1A2, CYP1B1 was not identified and sequenced until 1994. Nucleic and amino acid analysis showed approximately 40% identity with CYP1A1. Despite this similarity, these two enzymes have very different catalytic efficiencies and metabolites when incubated with common substrates, such as retinoic acid and arachidonic acid. Recently CYP1B1 has been shown to be physiologically important in fetal development, since mutations in CYP1B1 are linked with a form of primary congenital glaucoma.

CYP1A1 and CYP1B1 are regulated by the aryl hydrocarbon receptor, a ligand activated transcription factor. They are part of the Phase I reactions of drug metabolism.

Clinical significance

Mutations in this gene have been associated with primary congenital glaucoma; therefore it is thought that the enzyme also metabolizes a signaling molecule involved in eye development, possibly a steroid.^[5]

P450 is highly expressed in tumours and implicated in drug resistance, and is a research target to combat cancer. Developed inhibitors include flavonoids, trans-stilbenes, quinazolines, and derivatives of bentranil, a herbicide.^[6]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000138061 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000024087 – 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.
^ ^a ^b This article incorporates public domain material from "Entrez Gene: cytochrome P450". Reference Sequence collection. National Center for Biotechnology Information.
^ Yi, Lan; Huang, Xinyue; Yang, Meixian; Cai, Jiajing; Jia, Jianhua; Peng, Zhiping; Zhao, Zhenghuan; Yang, Fengyuan; Qiu, Dachuan (January 2023). "A new class of CYP1B1 inhibitors derived from bentranil". Bioorganic & Medicinal Chemistry Letters. 80: 129112. doi:10.1016/j.bmcl.2022.129112.

External links

cytochrome+P-450+CYP1B1 at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
CYP1B1+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
GeneReview/NCBI/NIH/UW entry on Primary Congenital Glaucoma
Human CYP1B1 genome location and CYP1B1 gene details page in the UCSC Genome Browser.

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

v t e Cytochromes, oxygenases: cytochrome P450 (Most belong to EC 1.14)
CYP1	A1 A2 A5 B1
CYP2	A6 A7 A13 B6 C8 C9 C18 C19 D6 E1 F1 J2 R1 S1 U1 W1
CYP3 (CYP3A)	A4 A5 A7 A37 A43
CYP4	A11 A22 B1 F2 F3 F8 F11 F12 F22 V2 X1 Z1
CYP5-20	CYP5 (A1) CYP6 (G1, M2) CYP7 (A1, B1) CYP8 (A1, B1) CYP9 CYP10 CYP11 (A1, A2, B1, B2, B3, C1) CYP12 CYP13 CYP14 CYP15 CYP16 CYP17 (A1) CYP18 CYP19 (A1) CYP20 (A1)
CYP21-49	CYP21 (A2) CYP22 (A1) CYP23 CYP24 (A1) CYP25 CYP26 (A1, B1, C1) CYP27 (A1, B1, C1) CYP28 (A1) CYP29 CYP35 (B1) CYP39 (A1) CYP46 (A1)
CYP51-69	CYP51 (A1, F1) CYP52 CYP53 A1 CYP55 A1 CYP56 A1 CYP61
CYP71-99	CYP71 (C1, C2, C3, C4, Z6, AJ4, AV1, BA1) CYP72A1 CYP73A1 CYP74 (D1) CYP75 (A1, B1) CYP76 (B6, M7) CYP79 (A1, A2, B1, B2, B3, D1, D2, D3, D4) CYP80 (A1, B1, G2) CYP81 (E1, E3, E7, E9) CYP88D6 CYP90C1 CYP93E1 CYP97C1 CYP99A3
CYP101-281	CYP101A1 CYP102A1 CYP105 A1 D7 CYP106A2 CYP107 A1 G1 CYP109 B1 E1 CYP111 CYP113A1 CYP119A1 CYP123 CYP125A1 CYP139 CYP147 CYP152 A1 B1 CYP154C3 CYP158A CYP161C CYP170 A1 B1 CYP176A1 CYP183A CYP197 CYP199A2 CYP255A
CYP301-499	CYP303A1 CYP305 M2 Halloween genes ( CYP302A1, CYP306A1, CYP307A1, CYP307A2, CYP314A1, CYP315A1) CYP318A1
CYP501-699	CYP503 CYP504B1
CYP701-999	CYP704B22 CYP710 CYP720A1

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme 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)

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Function

Clinical significance

References

Further reading

External links