DB code: S00026
CATH domain | 1.10.600.10 : Farnesyl Diphosphate Synthase | Catalytic domain |
---|---|---|
E.C. | 4.2.3.9 | |
CSA | 1di1 | |
M-CSA | 1di1 | |
MACiE | M0261 |
CATH domain | Related DB codes (homologues) |
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1.10.600.10 : Farnesyl Diphosphate Synthase | S00024 S00027 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | Pfam |
---|---|---|---|
Q03471 |
Aristolochene synthase
|
AS
EC 4.2.3.9 Sesquiterpene cyclase |
PF03936
(Terpene_synth_C)
[Graphical View] |
KEGG enzyme name |
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aristolochene synthase
sesquiterpene cyclase trans,trans-farnesyl diphosphate aristolochene-lyase trans,trans-farnesyl-diphosphate diphosphate-lyase (cyclizing,aristolochene-forming) |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
Q03471 | ARIS_PENRO | 2-trans,6-trans-farnesyl diphosphate = aristolochene + diphosphate. | Cytoplasm. | Magnesium. Manganese. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00900 | Terpenoid biosynthesis |
Compound table | |||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
Cofactors | Substrates | Products | Intermediates | ||||||||
KEGG-id | C00305 | C00034 | C00448 | C02004 | C00013 | ||||||
E.C. | |||||||||||
Compound | Magnesium | Manganese | trans,trans-farnesyl diphosphate | Aristolochene | diphosphate | ||||||
Type | divalent metal (Ca2+, Mg2+) | heavy metal | lipid,phosphate group/phosphate ion | lipid | phosphate group/phosphate ion | ||||||
ChEBI |
18420 18420 |
18291 35154 18291 35154 |
17407 17407 |
43445 43445 |
29888 29888 |
||||||
PubChem |
888 888 |
23930 23930 |
445713 445713 |
656496 656496 |
1023 21961011 1023 21961011 |
||||||
1dgpA | Unbound | Unbound | Analogue:FOH | Unbound | Unbound | ||||||
1dgpB | Unbound | Unbound | Analogue:FOH | Unbound | Unbound | ||||||
1di1A | Unbound | Unbound | Unbound | Unbound | Unbound | ||||||
1di1B | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
literature [5] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1dgpA | TYR 92 | |||||||||
1dgpB | TYR 92 | |||||||||
1di1A | TYR 92 | |||||||||
1di1B | TYR 92 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[1]
|
SCHEME I | |
[4]
|
Fig.5, Fig.6 | 3 |
[5]
|
Scheme 1 | p.7742 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 7986100 |
Journal | Arch Biochem Biophys |
Year | 1994 |
Volume | 315 |
Pages | 527-32 |
Authors | Back K, Yin S, Chappell J |
Title | Expression of a plant sesquiterpene cyclase gene in Escherichia coli. |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 8563643 |
Journal | Protein Sci |
Year | 1995 |
Volume | 4 |
Pages | 2436-8 |
Authors | Lesburg CA, Lloyd MD, Cane DE, Christianson DW |
Title | Crystallization and preliminary X-ray diffraction analysis of recombinant pentalenene synthase. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9324768 |
Journal | Science |
Year | 1997 |
Volume | 277 |
Pages | 1788-9 |
Authors | Sacchettini JC, Poulter CD |
Title | Creating isoprenoid diversity. |
Related PDB | |
Related UniProtKB | |
[4] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
Medline ID | 20400487 |
PubMed ID | 10825154 |
Journal | J Biol Chem |
Year | 2000 |
Volume | 275 |
Pages | 25533-9 |
Authors | Caruthers JM, Kang I, Rynkiewicz MJ, Cane DE, Christianson DW |
Title |
Crystal structure determination of aristolochene synthase from the blue cheese mold, |
Related PDB | 1dgp 1di1 |
Related UniProtKB | Q03471 |
[5] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12820883 |
Journal | Biochemistry |
Year | 2003 |
Volume | 42 |
Pages | 7741-7 |
Authors | Deligeorgopoulou A, Allemann RK |
Title | Evidence 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. |
Related PDB | |
Related UniProtKB |
Comments |
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Created | Updated |
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2004-05-24 | 2009-02-26 |