Prenyltransferase: Difference between revisions

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| image = PDB 1sqc EBI.jpg
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| caption = Structure of a squalene cyclase.<ref name="pmid9295270">{{cite journal |vauthors=Wendt KU, Poralla K, Schulz GE |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |date=1997 |pmid=9295270 |doi= 10.1126/science.277.5333.1811|url=}}</ref>
| caption = Structure of a squalene cyclase.<ref name="pmid9295270">{{cite journal |vauthors=Wendt KU, Poralla K, Schulz GE |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |date=1997 |pmid=9295270 |doi= 10.1126/science.277.5333.1811}}</ref>
| Pfam= PF00432
| Pfam= PF00432
| Pfam_clan= CL0059
| Pfam_clan= CL0059
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'''Prenyltransferases''' are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.<ref name="pmid16900467">{{cite journal |vauthors=Takahashi S, Koyama T | title = Structure and function of cis-prenyl chain elongating enzymes | journal = The Chemical Record | volume = 6 | issue = 4 | pages = 194–205 | year = 2006 | pmid = 16900467 | doi = 10.1002/tcr.20083 | url = }}</ref>
'''Prenyltransferases''' are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.<ref name="pmid16900467">{{cite journal |vauthors=Takahashi S, Koyama T | title = Structure and function of cis-prenyl chain elongating enzymes | journal = The Chemical Record | volume = 6 | issue = 4 | pages = 194–205 | year = 2006 | pmid = 16900467 | doi = 10.1002/tcr.20083 }}</ref>


Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the [[stereochemistry]] of the resulting products. Examples of trans-prenyltranferases include [[dimethylallyltranstransferase]], and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to [[dolichol]]).
Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the [[stereochemistry]] of the resulting products. Examples of trans-prenyltranferases include [[dimethylallyltranstransferase]], and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to [[dolichol]]).


The beta subunit of the [[farnesyltransferase]]s is responsible for peptide binding. [[Squalene-hopene cyclase]] is a bacterial enzyme that catalyzes the [[cyclization reaction|cyclization]] of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism.<ref name="pmid9295270">{{cite journal |vauthors=Wendt KU, Poralla K, Schulz GE |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |date=1997 |pmid=9295270 |doi= 10.1126/science.277.5333.1811|url=}}</ref> Lanosterol synthase ({{EC number|5.4.99.7}}) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi.<ref name="PUB00005416">{{cite journal |vauthors=Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G |title=A specific amino acid repeat in squalene and oxidosqualene cyclases |journal=Trends Biochem. Sci. |volume=19 |issue=4 |pages=157–158 |year=1994 |pmid=8016864 |doi=10.1016/0968-0004(94)90276-3}}</ref> Cycloartenol synthase ({{EC number|5.4.99.8}}) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.
The beta subunit of the [[farnesyltransferase]]s is responsible for peptide binding. [[Squalene-hopene cyclase]] is a bacterial enzyme that catalyzes the [[cyclization reaction|cyclization]] of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism.<ref name="pmid9295270">{{cite journal |vauthors=Wendt KU, Poralla K, Schulz GE |title=Structure and function of a squalene cyclase |journal=Science |volume=277 |issue=5333 |pages=1811–1815 |date=1997 |pmid=9295270 |doi= 10.1126/science.277.5333.1811}}</ref> Lanosterol synthase ({{EC number|5.4.99.7}}) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi.<ref name="PUB00005416">{{cite journal |vauthors=Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G |title=A specific amino acid repeat in squalene and oxidosqualene cyclases |journal=Trends Biochem. Sci. |volume=19 |issue=4 |pages=157–158 |year=1994 |pmid=8016864 |doi=10.1016/0968-0004(94)90276-3}}</ref> Cycloartenol synthase ({{EC number|5.4.99.8}}) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.


==Human proteins containing this domain ==
==Human proteins containing this domain ==

Revision as of 17:14, 13 December 2020

Prenyltransferase and squalene oxidase repeat
Structure of a squalene cyclase.[1]
Identifiers
SymbolPrenyltrans
PfamPF00432
Pfam clanCL0059
InterProIPR001330
PROSITEPDOC00825
SCOP21sqc / SCOPe / SUPFAM
OPM superfamily37
OPM protein1w6k
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Prenyltransferases are a class of enzymes that transfer allylic prenyl groups to acceptor molecules. Prenyl transferases commonly refer to prenyl diphosphate synthases.[2]

Prenyltransferases are commonly divided into two classes, cis (or Z) and trans (or E), depending upon the stereochemistry of the resulting products. Examples of trans-prenyltranferases include dimethylallyltranstransferase, and geranylgeranyl pyrophosphate synthase. Cis-prenyltransferases include dehydrodolichol diphosphate synthase (involved in the production of a precursor to dolichol).

The beta subunit of the farnesyltransferases is responsible for peptide binding. Squalene-hopene cyclase is a bacterial enzyme that catalyzes the cyclization of squalene into hopene, a key step in hopanoid (triterpenoid) metabolism.[1] Lanosterol synthase (EC 5.4.99.7) (oxidosqualene-lanosterol cyclase) catalyzes the cyclization of (S)-2,3-epoxysqualene to lanosterol, the initial precursor of cholesterol, steroid hormones and vitamin D in vertebrates and of ergosterol in fungi.[3] Cycloartenol synthase (EC 5.4.99.8) (2,3-epoxysqualene-cycloartenol cyclase) is a plant enzyme that catalyzes the cyclization of (S)-2,3-epoxysqualene to cycloartenol.

Human proteins containing this domain

FNTB; LSS; PGGT1B; RABGGTB

References

  1. ^ a b Wendt KU, Poralla K, Schulz GE (1997). "Structure and function of a squalene cyclase". Science. 277 (5333): 1811–1815. doi:10.1126/science.277.5333.1811. PMID 9295270.
  2. ^ Takahashi S, Koyama T (2006). "Structure and function of cis-prenyl chain elongating enzymes". The Chemical Record. 6 (4): 194–205. doi:10.1002/tcr.20083. PMID 16900467.
  3. ^ Prestwich GD, Poralla K, Hewelt A, Abe I, Reipen I, Sprenger G (1994). "A specific amino acid repeat in squalene and oxidosqualene cyclases". Trends Biochem. Sci. 19 (4): 157–158. doi:10.1016/0968-0004(94)90276-3. PMID 8016864.

External links

This article incorporates text from the public domain Pfam and InterPro: IPR001330


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