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Sequence of LEUD2_ARATH

EC Number:4.2.1.33

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3-isopropylmalate dehydratase
Q9LYT7
Arabidopsis thaliana
253
27208
Reaction
(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate
Other sequences found for EC No. 4.2.1.33

EC Number:4.2.1.170

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
2-(omega-methylthio)alkylmalate dehydratase
Q9LYT7
Arabidopsis thaliana
253
27208
Reaction
a 2-[(omega-methylsulfanyl)alkyl]malate = a 2-[(omega-methylsulfanyl)alkyl]maleate + H2O
Other sequences found for EC No. 4.2.1.170

General information:

Sequence
  0 MATSQQFLNP TLFKSLASSN KNSCTLCPSP FLQLKSASTI FNYKPLTSSS ATIITRVAAS
 60 SSDSGESITR ETFHGLCFVL KDNIDTDQII PAEYGTLIPS IPEDREKLGS FALNGLPKFY
120 NERFVVPGEM KSKYSVIIGG DNFGCGSSRE HAPVCLGAAG AKAVVAESYA RIFFRNCVAT
180 GEIFPLESEV RICDECKTGD VVTIEHKEDG SSLLINHTTR KEYKLKPLGD AGPVIDAGGI
240 FAYARKAGMI PSA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
182542
Salanoubat M.,Lemcke K.,Rieger M.,Ansorge W.,Unseld M.,Fartmann B.,Valle G.,Bloecker H.,Perez-Alonso M.,Obermaier B.,Delseny M.,Boutry M.,Grivell L.A.,Mache R.,Puigdomenech P.,De Simone V.,Choisne N.,Artiguenave F.,Robert C.,Brottier P.,Wincker P.,Cattolico L.,Weissenbach J.,Saurin W.,Quetier F.,Schaefer M.,Mueller-Auer S.,Gabel C.,Fuchs M.,Benes V.,Wurmbach E.,Drzonek H.,Erfle H.,Jordan N.,Bangert S.,Wiedelmann R.,Kranz H.,Voss H.,Holland R.,Brandt P.,Nyakatura G.,Vezzi A.,D'Angelo M.,Pallavicini A.,Toppo S.,Simionati B.,Conrad A.,Hornischer K.,Kauer G.,Loehnert T.-H.,Nordsiek G.,Reichelt J.,Scharfe M.,Schoen O.,Bargues M.,Terol J.,Climent J.,Navarro P.,Collado C.,Perez-Perez A.,Ottenwaelder B.,Duchemin D.,Cooke R.,Laudie M.,Berger-Llauro C.,Purnelle B.,Masuy D.,de Haan M.,Maarse A.C.,Alcaraz J.-P.,Cottet A.,Casacuberta E.,Monfort A.,Argiriou A.,Flores M.,Liguori R.,Vitale D.,Mannhaupt G.,Haase D.,Schoof H.,Rudd S.,Zaccaria P.,Mewes H.-W.,Mayer K.F.X.,Kaul S.,Town C.D.,Koo H.L.,Tallon L.J.,Jenkins J.,Rooney T.,Rizzo M.,Walts A.,Utterback T.,Fujii C.Y.,Shea T.P.,Creasy T.H.,Haas B.,Maiti R.,Wu D.,Peterson J.,Van Aken S.,Pai G.,Militscher J.,Sellers P.,Gill J.E.,Feldblyum T.V.,Preuss D.,Lin X.,Nierman W.C.,Salzberg S.L.,White O.,Venter J.C.,Fraser C.M.,Kaneko T.,Nakamura Y.,Sato S.,Kato T.,Asamizu E.,Sasamoto S.,Kimura T.,Idesawa K.,Kawashima K.,Kishida Y.,Kiyokawa C.,Kohara M.,Matsumoto M.,Matsuno A.,Muraki A.,Nakayama S.,Nakazaki N.,Shinpo S.,Takeuchi C.,Wada T.,Watanabe A.,Yamada M.,Yasuda M.,Tabata S.
Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.
Nature
408
820-822
2000
182543
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
182544
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
182545
Knill T.,Reichelt M.,Paetz C.,Gershenzon J.,Binder S.
Arabidopsis thaliana encodes a bacterial-type heterodimeric isopropylmalate isomerase involved in both Leu biosynthesis and the Met chain elongation pathway of glucosinolate formation.
Plant Mol. Biol.
71
227-239
2009
182546
He Y.,Chen B.,Pang Q.,Strul J.M.,Chen S.
Functional specification of Arabidopsis isopropylmalate isomerases in glucosinolate and leucine biosynthesis.
Plant Cell Physiol.
51
1480-1487
2010
182547
Imhof J.,Huber F.,Reichelt M.,Gershenzon J.,Wiegreffe C.,Laechler K.,Binder S.
The small subunit 1 of the Arabidopsis isopropylmalate isomerase is required for normal growth and development and the early stages of glucosinolate formation.
PLoS ONE
9
0-0
2014
182548
Laechler K.,Clauss K.,Imhof J.,Crocoll C.,Schulz A.,Halkier B.A.,Binder S.
In Arabidopsis thaliana substrate recognition and tissue- as well as plastid type-specific expression define the roles of distinct small subunits of isopropylmalate isomerase.
Front. Plant Sci.
11
808-808
2020