Sequence of PCS1_ARATH
EC Number:2.3.2.15
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
glutathione + [Glu(-Cys)]n-Gly = Gly + [Glu(-Cys)]n+1-Gly
Other sequences found for EC No. 2.3.2.15
General information:
Sequence
0 MAMASLYRRS LPSPPAIDFS SAEGKLIFNE ALQKGTMEGF FRLISYFQTQ SEPAYCGLAS
60 LSVVLNALSI DPGRKWKGPW RWFDESMLDC CEPLEVVKEK GISFGKVVCL AHCSGAKVEA
120 FRTSQSTIDD FRKFVVKCTS SENCHMISTY HRGVFKQTGT GHFSPIGGYN AERDMALILD
180 VARFKYPPHW VPLKLLWEAM DSIDQSTGKR RGFMLISRPH REPGLLYTLS CKDESWIEIA
240 KYLKEDVPRL VSSQHVDSVE KIISVVFKSL PSNFNQFIRW VAEIRITEDS NQNLSAEEKS
300 RLKLKQLVLK EVHETELFKH INKFLSTVGY EDSLTYAAAK ACCQGAEILS GSPSKEFCCR
360 ETCVKCIKGP DDSEGTVVTG VVVRDGNEQK VDLLVPSTQT ECECGPEATY PAGNDVFTAL
420 LLALPPQTWS GIKDQALMHE MKQLISMASL PTLLQEEVLH LRRQLQLLKR CQENKEEDDL
480 AAPAY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
202805
Ha S.-B.,Smith A.P.,Howden R.,Dietrich W.M.,Bugg S.,O'Connell M.J.,Goldsbrough P.B.,Cobbett C.S.
Phytochelatin synthase genes from Arabidopsis and the yeast Schizosaccharomyces pombe.
Plant Cell
11
1153-1164
1999
202806
Clemens S.,Kim E.J.,Neumann D.,Schroeder J.I.
Tolerance to toxic metals by a gene family of phytochelatin synthases from plants and yeast.
EMBO J.
18
3325-3333
1999
202807
Vatamaniuk O.K.,Mari S.,Lu Y.-P.,Rea P.A.
AtPCS1, a phytochelatin synthase from Arabidopsis: isolation and in vitro reconstitution.
Proc. Natl. Acad. Sci. U.S.A.
96
7110-7115
1999
202809
Sauge-Merle S.,Cuine S.,Carrier P.,Lecomte-Pradines C.,Luu D.-T.,Peltier G.
Enhanced toxic metal accumulation in engineered bacterial cells expressing Arabidopsis thaliana phytochelatin synthase.
Appl. Environ. Microbiol.
69
490-494
2003
202810
Kotani H.,Nakamura Y.,Sato S.,Kaneko T.,Asamizu E.,Miyajima N.,Tabata S.
Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence features of the regions of 1,044,062 bp covered by thirteen physically assigned P1 clones.
DNA Res.
4
291-300
1997
202811
Cheng C.Y.,Krishnakumar V.,Chan A.P.,Thibaud-Nissen F.,Schobel S.,Town C.D.
Araport11: a complete reannotation of the Arabidopsis thaliana reference genome.
Plant J.
89
789-804
2017
202812
Yamada K.,Lim J.,Dale J.M.,Chen H.,Shinn P.,Palm C.J.,Southwick A.M.,Wu H.C.,Kim C.J.,Nguyen M.,Pham P.K.,Cheuk R.F.,Karlin-Newmann G.,Liu S.X.,Lam B.,Sakano H.,Wu T.,Yu G.,Miranda M.,Quach H.L.,Tripp M.,Chang C.H.,Lee J.M.,Toriumi M.J.,Chan M.M.,Tang C.C.,Onodera C.S.,Deng J.M.,Akiyama K.,Ansari Y.,Arakawa T.,Banh J.,Banno F.,Bowser L.,Brooks S.Y.,Carninci P.,Chao Q.,Choy N.,Enju A.,Goldsmith A.D.,Gurjal M.,Hansen N.F.,Hayashizaki Y.,Johnson-Hopson C.,Hsuan V.W.,Iida K.,Karnes M.,Khan S.,Koesema E.,Ishida J.,Jiang P.X.,Jones T.,Kawai J.,Kamiya A.,Meyers C.,Nakajima M.,Narusaka M.,Seki M.,Sakurai T.,Satou M.,Tamse R.,Vaysberg M.,Wallender E.K.,Wong C.,Yamamura Y.,Yuan S.,Shinozaki K.,Davis R.W.,Theologis A.,Ecker J.R.
Empirical analysis of transcriptional activity in the Arabidopsis genome.
Science
302
842-846
2003
202813
Grill E.,Winnacker E.-L.,Zenk M.H.
Phytochelatins, a class of heavy-metal-binding peptides from plants, are functionally analogous to metallothioneins.
Proc. Natl. Acad. Sci. U.S.A.
84
439-443
1987
202814
Grill E.,Loffler S.,Winnacker E.-L.,Zenk M.H.
Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase).
Proc. Natl. Acad. Sci. U.S.A.
86
6838-6842
1989
202815
Lee S.,Korban S.S.
Transcriptional regulation of Arabidopsis thaliana phytochelatin synthase (AtPCS1) by cadmium during early stages of plant development.
Planta
215
689-693
2002
202816
Ruotolo R.,Peracchi A.,Bolchi A.,Infusini G.,Amoresano A.,Ottonello S.
Domain organization of phytochelatin synthase: functional properties of truncated enzyme species identified by limited proteolysis.
J. Biol. Chem.
279
14686-14693
2004
202817
Vatamaniuk O.K.,Mari S.,Lang A.,Chalasani S.,Demkiv L.O.,Rea P.A.
Phytochelatin synthase, a dipeptidyltransferase that undergoes multisite acylation with gamma-glutamylcysteine during catalysis: stoichiometric and site-directed mutagenic analysis of arabidopsis thaliana PCS1-catalyzed phytochelatin synthesis.
J. Biol. Chem.
279
22449-22460
2004
202818
Romanyuk N.D.,Rigden D.J.,Vatamaniuk O.K.,Lang A.,Cahoon R.E.,Jez J.M.,Rea P.A.
Mutagenic definition of a papain-like catalytic triad, sufficiency of the N-terminal domain for single-site core catalytic enzyme acylation, and C-terminal domain for augmentative metal activation of a eukaryotic phytochelatin synthase.
Plant Physiol.
141
858-869
2006
202819
Loscos J.,Naya L.,Ramos J.,Clemente M.R.,Matamoros M.A.,Becana M.
A reassessment of substrate specificity and activation of phytochelatin synthases from model plants by physiologically relevant metals.
Plant Physiol.
140
1213-1221
2006
202820
Maor R.,Jones A.,Nuehse T.S.,Studholme D.J.,Peck S.C.,Shirasu K.
Multidimensional protein identification technology (MudPIT) analysis of ubiquitinated proteins in plants.
Mol. Cell. Proteomics
6
601-610
2007
202821
Blum R.,Beck A.,Korte A.,Stengel A.,Letzel T.,Lendzian K.,Grill E.
Function of phytochelatin synthase in catabolism of glutathione-conjugates.
Plant J.
49
740-749
2007
