cytochrome P450 family 1 subfamily B member 1
Last updated 4 Apr 2022
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The CYP1B1 gene provides instructions for producing an enzyme that is a member of the cytochrome P450 family of enzymes. These enzymes are involved in many processes in the body, such as assisting with reactions that break down drugs and produce certain fats (lipids). The CYP1B1 enzyme participates in biochemical reactions in which an oxygen atom is added to other molecules.
Normal function
The CYP1B1 gene provides instructions for producing an enzyme that is a member of the cytochrome P450 family of enzymes. These enzymes are involved in many processes in the body, such as assisting with reactions that break down drugs and produce certain fats (lipids). The CYP1B1 enzyme participates in biochemical reactions in which an oxygen atom is added to other molecules.
The CYP1B1 enzyme is active in many tissues, including structures of the eye. The function of the CYP1B1 enzyme in the development of the eye is unclear, but it may play a role in forming structures at the front of the eye and may also be involved in a process that regulates the secretion of fluid inside the eye.
Conditions referring to this gene or chromosome
Other names
aryl hydrocarbon hydroxylase
CP1B
CP1B1_HUMAN
cytochrome P450, family 1, subfamily B, polypeptide 1
cytochrome P450, subfamily I (dioxin-inducible), polypeptide 1 (glaucoma 3, primary infantile)
flavoprotein-linked monooxygenase
GLC3A
microsomal monooxygenase
xenobiotic monooxygenase
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I... Why this happens Black cohosh and vitamin C are processed by the body through different pathways. Vitamin C is a water-soluble vitamin that does not significantly interfere with the liver enzymes (such as the Cytochrome P450 system) that process black cohosh. Additionally, they do not have overlapping effects that would cause a dangerous.

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Further reading and references
- cytochrome P450 family 1 subfamily B member 1; MedlinePlus, National Library of Medicine.
- Achary MS, Reddy AB, Chakrabarti S, Panicker SG, Mandal AK, Ahmed N, Balasubramanian D, Hasnain SE, Nagarajaram HA. Disease-causing mutations in proteins: structural analysis of the CYP1B1 mutations causing primary congenital glaucoma in humans. Biophys J. 2006 Dec 15;91(12):4329-39. doi: 10.1529/biophysj.106.085498. Epub 2006 Sep 8.
- Chavarria-Soley G, Sticht H, Aklillu E, Ingelman-Sundberg M, Pasutto F, Reis A, Rautenstrauss B. Mutations in CYP1B1 cause primary congenital glaucoma by reduction of either activity or abundance of the enzyme. Hum Mutat. 2008 Sep;29(9):1147-53. doi: 10.1002/humu.20786.
- Chen Y, Jiang D, Yu L, Katz B, Zhang K, Wan B, Sun X. CYP1B1 and MYOC mutations in 116 Chinese patients with primary congenital glaucoma. Arch Ophthalmol. 2008 Oct;126(10):1443-7. doi: 10.1001/archopht.126.10.1443.
- Melki R, Colomb E, Lefort N, Brezin AP, Garchon HJ. CYP1B1 mutations in French patients with early-onset primary open-angle glaucoma. J Med Genet. 2004 Sep;41(9):647-51. doi: 10.1136/jmg.2004.020024.
- Selvan H, Gupta S, Wiggs JL, Gupta V. Juvenile-onset open-angle glaucoma - A clinical and genetic update. Surv Ophthalmol. 2022 Jul-Aug;67(4):1099-1117. doi: 10.1016/j.survophthal.2021.09.001. Epub 2021 Sep 16.
- Vasiliou V, Gonzalez FJ. Role of CYP1B1 in glaucoma. Annu Rev Pharmacol Toxicol. 2008;48:333-58. doi: 10.1146/annurev.pharmtox.48.061807.154729.
- Vincent A, Billingsley G, Priston M, Glaser T, Oliver E, Walter M, Ritch R, Levin A, Heon E. Further support of the role of CYP1B1 in patients with Peters anomaly. Mol Vis. 2006 May 16;12:506-10.
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