- Function
- Tissue distribution
- Clinical significance
- References
- External links
- Further reading
| Name = 3-dehydrosphinganine reductase
| EC_number = 1.1.1.102
| CAS_number = 37250-36-5
| IUBMB_EC_number = 1/1/1/102
| GO_code = 0047560
| image =
| width =
| caption =
}}{{Infobox_gene}}3-dehydrosphinganine reductase ({{EC number|1.1.1.102}}) also known as 3-ketodihydrosphingosine reductase (KDSR) or follicular variant translocation protein 1 (FVT1) is an enzyme that in humans is encoded by the KDSR gene.[1][2][3][4][5]
Function
3-dehydrosphinganine reductase catalyzes the chemical reaction:
sphinganine + NADP+3-dehydrosphinganine + NADPH + H+
Thus, the two substrates of this enzyme are sphinganine and NADP+, whereas its 3 products are 3-dehydrosphinganine, NADPH, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. This enzyme participates in sphingolipid metabolism.
Tissue distribution
Follicular lymphoma variant translocation 1 is a secreted protein which is weakly expressed in hematopoietic tissue.
Clinical significance
FVT1 shows a high rate of transcription in some T cell malignancies and in phytohemagglutinin-stimulated lymphocytes. The proximity of FVT1 to BCL2 suggests that it may participate in the tumoral process.[5]
References
1. ^{{cite journal | vauthors = Rimokh R, Gadoux M, Berthéas MF, Berger F, Garoscio M, Deléage G, Germain D, Magaud JP | title = FVT-1, a novel human transcription unit affected by variant translocation t(2;18)(p11;q21) of follicular lymphoma | journal = Blood | volume = 81 | issue = 1 | pages = 136–42 | date = January 1993 | pmid = 8417785 | pmc = | doi = }}
2. ^{{cite journal | vauthors = Kihara A, Igarashi Y | title = FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane | journal = The Journal of Biological Chemistry | volume = 279 | issue = 47 | pages = 49243–50 | date = November 2004 | pmid = 15328338 | pmc = | doi = 10.1074/jbc.M405915200 }}
3. ^{{cite journal | vauthors = Krebs S, Medugorac I, Röther S, Strässer K, Förster M | title = A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 16 | pages = 6746–51 | date = April 2007 | pmid = 17420465 | pmc = 1868895 | doi = 10.1073/pnas.0607721104 | bibcode = 2007PNAS..104.6746K }}
4. ^{{cite journal | vauthors = Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U | title = The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative | journal = Chemico-Biological Interactions | volume = 178 | issue = 1–3 | pages = 94–8 | date = March 2009 | pmid = 19027726 | pmc = 2896744 | doi = 10.1016/j.cbi.2008.10.040 }}
5. ^1 {{cite web | title = Entrez Gene: FVT1 follicular lymphoma variant translocation 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2531| accessdate = }}
2. ^{{cite journal | vauthors = Kihara A, Igarashi Y | title = FVT-1 is a mammalian 3-ketodihydrosphingosine reductase with an active site that faces the cytosolic side of the endoplasmic reticulum membrane | journal = The Journal of Biological Chemistry | volume = 279 | issue = 47 | pages = 49243–50 | date = November 2004 | pmid = 15328338 | pmc = | doi = 10.1074/jbc.M405915200 }}
3. ^{{cite journal | vauthors = Krebs S, Medugorac I, Röther S, Strässer K, Förster M | title = A missense mutation in the 3-ketodihydrosphingosine reductase FVT1 as candidate causal mutation for bovine spinal muscular atrophy | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 16 | pages = 6746–51 | date = April 2007 | pmid = 17420465 | pmc = 1868895 | doi = 10.1073/pnas.0607721104 | bibcode = 2007PNAS..104.6746K }}
4. ^{{cite journal | vauthors = Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jörnvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U | title = The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative | journal = Chemico-Biological Interactions | volume = 178 | issue = 1–3 | pages = 94–8 | date = March 2009 | pmid = 19027726 | pmc = 2896744 | doi = 10.1016/j.cbi.2008.10.040 }}
5. ^1 {{cite web | title = Entrez Gene: FVT1 follicular lymphoma variant translocation 1| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2531| accessdate = }}
External links
- {{UCSC gene info|KDSR}}
Further reading
{{refbegin | 2}}- {{cite journal | vauthors = Quintero-Ramos A, Valdez-Vélázquez LL, Hernández G, Baltazar LM, Padilla-Gutiérrez JR, Valle Y, Rodarte K, Ortiz R, Ortiz-Aranda M, Olivares N, Rivas F | title = [Assessment of five thrombophilic genetic polymorphisms among couples with habitual abortion] | journal = Gaceta Médica de México | volume = 142 | issue = 2 | pages = 95–8 | year = 2006 | pmid = 16711541 | doi = }}
- {{cite journal | vauthors = Wang J, Blakey GL, Zhang L, Bane B, Torbenson M, Li S | title = Uterine tumor resembling ovarian sex cord tumor: report of a case with t(X;6)(p22.3;q23.1) and t(4;18)(q21.1;q21.3) | journal = Diagnostic Molecular Pathology | volume = 12 | issue = 3 | pages = 174–80 | date = September 2003 | pmid = 12960700 | doi = 10.1097/00019606-200309000-00009}}
- {{cite journal | vauthors = Nacheva E, Dyer MJ, Metivier C, Jadayel D, Stranks G, Morilla R, Heward JM, Holloway T, O'Connor S, Bevan PC | title = B-cell non-Hodgkin's lymphoma cell line (Karpas 1106) with complex translocation involving 18q21.3 but lacking BCL2 rearrangement and expression | journal = Blood | volume = 84 | issue = 10 | pages = 3422–8 | date = November 1994 | pmid = 7949096 | doi = }}
- {{cite journal | vauthors = Stoffel W, LeKim D, Sticht G | title = Biosynthesis of dihydrosphingosine in vitro | journal = Hoppe-Seyler's Zeitschrift für Physiologische Chemie | volume = 349 | issue = 5 | pages = 664–70 | date = May 1968 | pmid = 4386961 | doi = 10.1515/bchm2.1968.349.1.664 }}
- {{cite journal | vauthors = Stoffel W, LeKim D, Sticht G | title = Metabolism of sphingosine bases. 8. Distribution, isolation and properties of D-3-oxosphinganine reductase. Stereospecificity of the NADPH-dependent reaction of 3-oxodihydrospingosine (2-amino-1-hydroxyoctadecane-3-one) | journal = Hoppe-Seyler's Zeitschrift für Physiologische Chemie | volume = 349 | issue = 12 | pages = 1637–44 | date = December 1968 | pmid = 4387676 | doi = 10.1515/bchm2.1968.349.2.1637 }}
3 : EC 1.1.1|NADPH-dependent enzymes|Enzymes of unknown structure
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