Abietadiene synthase: Difference between revisions

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| Name = aristolochene synthase
| EC_number = 4.2.3.9
| CAS_number =  
| IUBMB_EC_number = 4/2/3/9
| GO_code = 0045483
| image =  
| width =  
| caption =  
}}
In [[enzymology]], an '''aristolochene synthase''' ({{EC number|4.2.3.9}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
 
:2-trans,6-trans-farnesyl diphosphate <math>\rightleftharpoons</math> aristolochene + diphosphate
 
Hence, this enzyme has one [[substrate (biochemistry)|substrate]], [[2-trans,6-trans-farnesyl diphosphate]], and two [[product (chemistry)|products]], [[aristolochene]] and [[diphosphate]].
 
This enzyme belongs to the family of [[lyase]]s, specifically those carbon-oxygen lyases acting on phosphates. The systematic name of this enzyme class is '''2-trans,6-trans-farnesyl-diphosphate diphosphate-lyase (cyclizing, aristolochene-forming)'''. Other names in common use include '''sesquiterpene cyclase''', '''trans,trans-farnesyl diphosphate aristolochene-lyase''', '''trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,''', and '''aristolochene-forming)'''. This enzyme participates in [[terpenoid biosynthesis]].
 
This protein may use the [[morpheein]] model of [[allosteric regulation]]. <ref name=pmid22182754>{{cite journal | author = T. Selwood and E. K. Jaffe. | title = Dynamic dissociating homo-oligomers and the control of protein function. | journal = Arch. Biochem. Biophys. | volume = 519| issue =  2| pages =  131–43| year = 2011 | pmid = 22182754 | url = http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=22182754 | doi=10.1016/j.abb.2011.11.020 | pmc=3298769}}</ref>
 
==Structural studies==
 
As of late 2007, two [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|2E4O}} and {{PDB link|2OA6}}. They are both notable for the very high helix content of the structure.
 
==References==
{{reflist|1}}
* {{cite journal | author = Cane DE, Prabhakaran PC, Oliver JS and McIlwaine DB | date = 1990 | title = Aristolochene biosynthesis. Stereochemistry of the deprotonation steps in the enzymatic cyclization of farnesyl pyrophosphate | journal = J. Am. Chem. Soc. | volume = 112 | issue = 8 | pages = 3209&ndash;3210 | doi = 10.1021/ja00164a051 }}
* {{cite journal | author = Noguchi H and Rawlings BJ | date = 1989 | title = Aristolochene biosynthesis and enzymatic cyclization of farnesyl pyrophosphate | journal = J. Am. Chem. Soc| volume = 111 | issue = 24 | pages = 8914&ndash;8916 | doi = 10.1021/ja00206a022 }}
* {{cite journal | author = Hohn TM, Plattner RD | date = 1989 | title = Purification and characterization of the sesquiterpene cyclase aristolochene synthase from Penicillium roqueforti | journal = Arch. Biochem. Biophys. | volume = 272 | pages = 137&ndash;43  | pmid = 2544140 | doi = 10.1016/0003-9861(89)90204-X | issue = 1 }}
* {{cite journal | author = Proctor RH, Hohn TM | date = 1993 | title = Aristolochene synthase. Isolation, characterization, and bacterial expression of a sesquiterpenoid biosynthetic gene (Ari1) from Penicillium roqueforti | journal = J. Biol. Chem.  | volume = 268 | pages = 4543&ndash;8  | pmid = 8440737 | issue = 6 }}
* {{cite journal | author = Calvert MJ, Ashton PR, Allemann RK | date = 2002 | title = Germacrene A is a product of the aristolochene synthase-mediated conversion of farnesylpyrophosphate to aristolochene | journal = J. Am. Chem. Soc.  | volume = 124 | pages = 11636&ndash;41  | pmid = 12296728 | doi = 10.1021/ja020762p | issue = 39 }}
 
{{4.2-enzyme-stub}}
 
[[Category:EC 4.2.3]]
[[Category:Enzymes of known structure]]

Latest revision as of 21:42, 9 November 2014

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