EzCatDB: S00026
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DB codeS00026
CATH domainDomain 11.10.600.10 : Farnesyl Diphosphate SynthaseCatalytic domain
E.C.4.2.3.9
CSA1di1
MACiEM0261

CATH domainRelated DB codes (homologues)
1.10.600.10 : Farnesyl Diphosphate SynthaseS00024,S00027

Enzyme Name
UniProtKBKEGG

Q03471
Protein nameAristolochene synthasearistolochene synthase
sesquiterpene cyclase
trans,trans-farnesyl diphosphate aristolochene-lyase
trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,aristolochene-forming)
SynonymsAS
EC 4.2.3.9
Sesquiterpene cyclase
PfamPF03936 (Terpene_synth_C)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00900Terpenoid biosynthesis

UniProtKB:Accession NumberQ03471
Entry nameARIS_PENRO
Activity2-trans,6-trans-farnesyl diphosphate = aristolochene + diphosphate.
Subunit
Subcellular locationCytoplasm.
CofactorMagnesium.,Manganese.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00305C00034C00448C02004C00013
CompoundMagnesiumManganesetrans,trans-farnesyl diphosphateAristolochenediphosphate
Typedivalent metal (Ca2+, Mg2+)heavy metallipid,phosphate group/phosphate ionlipidphosphate group/phosphate ion
ChEBI18420
18291
35154
17407
43445
29888
PubChem888
23930
445713
656496
21961011
1023
             
1dgpAUnboundUnboundAnalogue:FOHUnboundUnbound
1dgpBUnboundUnboundAnalogue:FOHUnboundUnbound
1di1AUnboundUnboundUnboundUnboundUnbound
1di1BUnboundUnboundUnboundUnboundUnbound

Active-site residues
resource
literature [5]
pdbCatalytic residues
         
1dgpATYR 92
1dgpBTYR 92
1di1ATYR 92
1di1BTYR 92

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[1]SCHEME I
[4]Fig.5, Fig.63
[5]Scheme 1p.7742

references
[1]
PubMed ID7986100
JournalArch Biochem Biophys
Year1994
Volume315
Pages527-32
AuthorsBack K, Yin S, Chappell J
TitleExpression of a plant sesquiterpene cyclase gene in Escherichia coli.
[2]
PubMed ID8563643
JournalProtein Sci
Year1995
Volume4
Pages2436-8
AuthorsLesburg CA, Lloyd MD, Cane DE, Christianson DW
TitleCrystallization and preliminary X-ray diffraction analysis of recombinant pentalenene synthase.
[3]
PubMed ID9324768
JournalScience
Year1997
Volume277
Pages1788-9
AuthorsSacchettini JC, Poulter CD
TitleCreating isoprenoid diversity.
[4]
CommentsX-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS)
Medline ID20400487
PubMed ID10825154
JournalJ Biol Chem
Year2000
Volume275
Pages25533-9
AuthorsCaruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW
TitleCrystal structure determination of aristolochene synthase from the blue cheese mold, Penicillium roqueforti.
Related PDB1dgp,1di1
Related UniProtKBQ03471
[5]
PubMed ID12820883
JournalBiochemistry
Year2003
Volume42
Pages7741-7
AuthorsDeligeorgopoulou A, Allemann RK
TitleEvidence for differential folding of farnesyl pyrophosphate in the active site of aristolochene synthase: a single-point mutation converts aristolochene synthase into an (E)-beta-farnesene synthase.


createdupdated
2004-05-242009-02-26


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Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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