Sequence of FNTA_RAT
EC Number:2.5.1.59
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
geranylgeranyl diphosphate + protein-cysteine = S-geranylgeranyl-protein + diphosphate
Other sequences found for EC No. 2.5.1.59
General information:
Sequence
0 MAATEGVGES APGGEPGQPE QPPPPPPPPP AQQPQEEEMA AEAGEAAASP MDDGFLSLDS
60 PTYVLYRDRA EWADIDPVPQ NDGPSPVVQI IYSEKFRDVY DYFRAVLQRD ERSERAFKLT
120 RDAIELNAAN YTVWHFRRVL LRSLQKDLQE EMNYIIAIIE EQPKNYQVWH HRRVLVEWLK
180 DPSQELEFIA DILNQDAKNY HAWQHRQWVI QEFRLWDNEL QYVDQLLKED VRNNSVWNQR
240 HFVISNTTGY SDRAVLEREV QYTLEMIKLV PHNESAWNYL KGILQDRGLS RYPNLLNQLL
300 DLQPSHSSPY LIAFLVDIYE DMLENQCDNK EDILNKALEL CEILAKEKDT IRKEYWRYIG
360 RSLQSKHSRE SDIPASV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
672455
Chen W.-J.,Andres D.A.,Goldstein J.L.,Brown M.S.
Cloning and expression of a cDNA encoding the alpha subunit of rat p21ras protein farnesyltransferase.
Proc. Natl. Acad. Sci. U.S.A.
88
11368-11372
1991
672456
Park H.-W.,Boduluri S.R.,Mooomaw J.F.,Casey P.J.,Beese L.S.
Crystal structure of protein farnesyltransferase at 2.25-A resolution.
Science
275
1800-1804
1997
672458
Dunten P.,Kammlott U.,Crowther R.,Weber D.,Palermo R.,Birktoft J.
Protein farnesyltransferase: structure and implications for substrate binding.
Biochemistry
37
7907-7912
1998
672459
Long S.B.,Casey P.J.,Beese L.S.
Cocrystal structure of protein farnesyltransferase complexed with a farnesyl diphosphate substrate.
Biochemistry
37
9612-9618
1998
672460
Strickland C.L.,Windsor W.T.,Syto R.,Wang L.,Bond R.,Wu Z.,Schwartz J.,Le H.V.,Beese L.S.,Weber P.C.
Crystal structure of farnesyl protein transferase complexed with a CaaX peptide and farnesyl diphosphate analogue.
Biochemistry
37
16601-16611
1998
672461
Strickland C.L.,Weber P.C.,Windsor W.T.,Wu Z.,Le H.V.,Albanese M.M.,Alvarez C.S.,Cesarz D.,del Rosario J.,Deskus J.,Mallams A.K.,Njoroge F.G.,Piwinski J.J.,Remiszewski S.,Rossman R.R.,Taveras A.G.,Vibulbhan B.,Doll R.J.,Girijavallabhan V.M.,Ganguly A.K.
Tricyclic farnesyl protein transferase inhibitors: crystallographic and calorimetric studies of structure-activity relationships.
J. Med. Chem.
42
2125-2135
1999
672462
Long S.B.,Casey P.J.,Beese L.S.
The basis for K-Ras4B binding specificity to protein farnesyltransferase revealed by 2 A resolution ternary complex structures.
Structure
8
209-222
2000
672463
Long S.B.,Hancock P.J.,Kral A.M.,Hellinga H.W.,Beese L.S.
The crystal structure of human protein farnesyltransferase reveals the basis for inhibition by CaaX tetrapeptides and their mimetics.
Proc. Natl. Acad. Sci. U.S.A.
98
12948-12953
2001
672464
Long S.B.,Casey P.J.,Beese L.S.
Reaction path of protein farnesyltransferase at atomic resolution.
Nature
419
645-650
2002
672465
Turek-Etienne T.C.,Strickland C.L.,Distefano M.D.
Biochemical and structural studies with prenyl diphosphate analogues provide insights into isoprenoid recognition by protein farnesyl transferase.
Biochemistry
42
3716-3724
2003
672466
Gwaltney S.L.,O'Connor S.J.,Nelson L.T.,Sullivan G.M.,Imade H.,Wang W.,Hasvold L.,Li Q.,Cohen J.,Gu W.Z.,Tahir S.K.,Bauch J.,Marsh K.,Ng S.C.,Frost D.J.,Zhang H.,Muchmore S.,Jakob C.G.,Stoll V.,Hutchins C.,Rosenberg S.H.,Sham H.L.
Aryl tetrahydropyridine inhibitors of farnesyltransferase: glycine, phenylalanine and histidine derivatives.
Bioorg. Med. Chem. Lett.
13
1359-1362
2003
672467
Taylor J.S.,Reid T.S.,Terry K.L.,Casey P.J.,Beese L.S.
Structure of mammalian protein geranylgeranyltransferase type-I.
EMBO J.
22
5963-5974
2003
672468
Reid T.S.,Beese L.S.
Crystal structures of the anticancer clinical candidates R115777 (Tipifarnib) and BMS-214662 complexed with protein farnesyltransferase suggest a mechanism of FTI selectivity.
Biochemistry
43
6877-6884
2004
672469
Reid T.S.,Terry K.L.,Casey P.J.,Beese L.S.
Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity.
J. Mol. Biol.
343
417-433
2004
672470
DeGraw A.J.,Hast M.A.,Xu J.,Mullen D.,Beese L.S.,Barany G.,Distefano M.D.
Caged protein prenyltransferase substrates: tools for understanding protein prenylation.
Chem. Biol. Drug Des.
72
171-181
2008
672471
Nguyen U.T.,Guo Z.,Delon C.,Wu Y.,Deraeve C.,Franzel B.,Bon R.S.,Blankenfeldt W.,Goody R.S.,Waldmann H.,Wolters D.,Alexandrov K.
Analysis of the eukaryotic prenylome by isoprenoid affinity tagging.
Nat. Chem. Biol.
5
227-235
2009
672472
Stigter E.A.,Guo Z.,Bon R.S.,Wu Y.W.,Choidas A.,Wolf A.,Menninger S.,Waldmann H.,Blankenfeldt W.,Goody R.S.
Development of selective, potent RabGGTase inhibitors.
J. Med. Chem.
55
8330-8340
2012
