Sequence of ARIS_ASPTE
EC Number:4.2.3.9
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
(2E,6E)-farnesyl diphosphate = aristolochene + diphosphate
Other sequences found for EC No. 4.2.3.9
General information:
Sequence
0 MKKPNGTNGA SSSLEPPPST FQPLCHPLVE EVSKEVDGYF LQHWNFPNEK ARKKFVAAGF
60 SRVTCLYFPK ALDDRIHFAC RLLTVLFLID DLLEYMSFEE GSAYNEKLIP ISRGDVLPDR
120 SIPVEYIIYD LWESMRAHDR EMADEILEPV FLFMRAQTDR TRARPMGLGG YLEYRERDVG
180 KELLAALMRF SMGLKLSPSE LQRVREIDAN CSKHLSVVND IYSYEKELYT SKTAHSEGGI
240 LCTSVQILAQ EADVTAEAAK RVLFVMCREW ELRHQLLVAR LSAEGLETPG LAAYVEGLEY
300 QMSGNELWSQ TTLRYSVVVD
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
1158153
Cane D.E.,Kang I.
Aristolochene synthase: purification, molecular cloning, high-level expression in Escherichia coli, and characterization of the Aspergillus terreus cyclase.
Arch. Biochem. Biophys.
376
354-364
2000
1158154
Felicetti B.,Cane D.E.
Aristolochene synthase: mechanistic analysis of active site residues by site-directed mutagenesis.
J. Am. Chem. Soc.
126
7212-7221
2004
1158155
Shishova E.Y.,Di Costanzo L.,Cane D.E.,Christianson D.W.
X-ray crystal structure of aristolochene synthase from Aspergillus terreus and evolution of templates for the cyclization of farnesyl diphosphate.
Biochemistry
46
1941-1951
2007
1158156
Shishova E.Y.,Yu F.,Miller D.J.,Faraldos J.A.,Zhao Y.,Coates R.M.,Allemann R.K.,Cane D.E.,Christianson D.W.
X-ray crystallographic studies of substrate binding to aristolochene synthase suggest a metal ion binding sequence for catalysis.
J. Biol. Chem.
283
15431-15439
2008
