CYP13 family

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Cytochrome P450, family 13, also known as CYP13, is a nematoda cytochrome P450 monooxygenase family. [1] The first gene identified in this family is the CYP13A1 from the Caenorhabditis elegans .

CYP13 can be divided into subfamily CYP13A and CYP13B, [1] and the CYP13B was named CYP16 family at the beginning of its discovery, which have been discontinued and been changed to the current name, because its genetic relationship with the subfamily CYP13A. [2]

Genes in C. elegans

GeneBiological FunctionsProtein Length [1] Ref
CYP13A1519
CYP13A2515
CYP13A3520
CYP13A4520
CYP13A5 Dauer formation 520
CYP13A6518
CYP13A7Dauer formation, Detoxication518
CYP13A8Acidic Stress509 [3]
CYP13A9 pseudogene
CYP13A10519
CYP13A11517
CYP13A12 Lipid metabolism 518 [4]
CYP13B1510
CYP13B2511

Related Research Articles

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Cytochrome P450 2A6 is a member of the cytochrome P450 mixed-function oxidase system, which is involved in the metabolism of xenobiotics in the body. CYP2A6 is the primary enzyme responsible for the oxidation of nicotine and cotinine. It is also involved in the metabolism of several pharmaceuticals, carcinogens, and a number of coumarin-type alkaloids. CYP2A6 is the only enzyme in the human body that appreciably catalyzes the 7-hydroxylation of coumarin, such that the formation of the product of this reaction, 7-hydroxycoumarin, is used as a probe for CYP2A6 activity.

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<span class="mw-page-title-main">CYP2J2</span> Gene of the species Homo sapiens

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<span class="mw-page-title-main">CYP4F2</span> Protein-coding gene in the species Homo sapiens

Leukotriene-B(4) omega-hydroxylase 1 is an enzyme protein involved in the metabolism of various endogenous substrates and xenobiotics. The most notable substrate of the enzyme is leukotriene B4, a potent mediator of inflammation. The CYP4F2 gene encodes the enzyme in humans.

<span class="mw-page-title-main">CYP2A13</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 2A13 is a protein that in humans is encoded by the CYP2A13 gene.

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Cytochrome P450 4F8 is a protein that in humans is encoded by the CYP4F8 gene.

<span class="mw-page-title-main">CYP4F12</span> Protein-coding gene in the species Homo sapiens

Cytochrome P450 4F12 is a protein that in humans is encoded by the CYP4F12 gene.

<span class="mw-page-title-main">CYP20A1</span>

CYP20A1 is a protein which in humans is encoded by the CYP20A1 gene.

<span class="mw-page-title-main">CYP4F11</span> Protein-coding gene in the species Homo sapiens

CYP4F11 is a protein that in humans is encoded by the CYP4F11 gene. This gene encodes a member of 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. This gene is part of a cluster of cytochrome P450 genes on chromosome 19. Another member of this family, CYP4F2, is approximately 16 kb away. Alternatively spliced transcript variants encoding the same protein have been found for this gene.

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The DAF-12 gene encodes the nuclear receptor of dafachronic acid in the worm Caenorhabditis elegans, with the NRNC Symbol NR1J1 as the homolog of nuclear hormone receptor HR96 in Drosophila melanogaster. DAF-12 has been implicated by Cynthia Kenyon and colleagues in the formation of Dauer larva.

The Daf-9 gene encodes a cytochrome p450 enzyme catalysis the generation of dafachronic acid in the worm Caenorhabditis elegans, with the CYP Symbol CYP22A1. After generation, dafachronic acid will binding it's nuclear receptor Daf-12 and has been implicated by Cynthia Kenyon and colleagues related to the formation of Dauer larva.

The Dod-13 gene in the worm Caenorhabditis elegans encoding a cytochrome p450 enzyme, which have steroid hydroxylase activity, with the CYP Symbol CYP35B1. Dod-13 is downstream gene of Daf-16 influenced the lifespan of C. elegans.

Cytochrome P450, family 16, also known as CYP16, is an animal cytochrome P450 monooxygenase family. This family was the last vertebrate CYP family recognized, and is absent from the mammal and zebrafish genome, but found in other fish and many invertebrates including some very old branches, such as Trichoplax and Oscarella carmela. Synteny mapping of CYP16 family members showing linkages to CYP26 family members, means the tetrapod's CYP26 may evolved from CYP16 of fish.

Cytochrome P450, family 9, also known as CYP9, is a cytochrome P450 family found in Insect genome, CYP9 and insect CYP6 family belong to the same clan as mammalian CYP3 and CYP5 families. The first gene identified in this family is the CYP9A1 from the Heliothis virescens, which is involved in thiodicarb insecticide resistance. Subfamily CYP9A in Lepidopteran play important roles in insecticide resistance, can metabolize esfenvalerate efficiently.

Cytochrome P450, family 6, also known as CYP6, is a cytochrome P450 family found in Insect genome. CYP6 and CYP9, another insect CYP family, belong to the same clan as mammalian CYP3 and CYP5 families.

Cytochrome P450, family 14, also known as CYP14, is a nematoda cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP14A1 from the Caenorhabditis elegans. The function of most genes in this family is unknown.

Cytochrome P450, family 23, also known as CYP23, is a nematoda cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP23A1 from the Caenorhabditis elegans, is a homolog of the human gene CYP7B1.

Cytochrome P450, family 25, also known as CYP25, is a nematoda cytochrome P450 monooxygenase family. The first gene identified in this family is the CYP25A1 from the Caenorhabditis elegans.

References

  1. 1 2 3 Larigot, L; Mansuy, D; Borowski, I; Coumoul, X; Dairou, J (22 February 2022). "Cytochromes P450 of Caenorhabditis elegans: Implication in Biological Functions and Metabolism of Xenobiotics". Biomolecules. 12 (3): 342. doi: 10.3390/biom12030342 . PMC   8945457 . PMID   35327534.
  2. Nelson, DR (November 1998). "Metazoan cytochrome P450 evolution". Comparative Biochemistry and Physiology. Part C, Pharmacology, Toxicology & Endocrinology. 121 (1–3): 15–22. doi:10.1016/s0742-8413(98)10027-0. PMID   9972448.
  3. Cong, Yanyi; Yang, Hanwen; Zhang, Pengchi; Xie, Yusu; Cao, Xuwen; Zhang, Liusuo (10 September 2020). "Transcriptome Analysis of the Nematode Caenorhabditis elegans in Acidic Stress Environments". Frontiers in Physiology. 11: 1107. doi: 10.3389/fphys.2020.01107 . PMC   7511720 . PMID   33013473.
  4. Keller, J; Ellieva, A; Ma, DK; Ju, J; Nehk, E; Konkel, A; Falck, JR; Schunck, WH; Menzel, R (15 November 2014). "CYP-13A12 of the nematode Caenorhabditis elegans is a PUFA-epoxygenase involved in behavioural response to reoxygenation" (PDF). The Biochemical Journal. 464 (1): 61–71. doi:10.1042/BJ20140848. PMID   25138176.