Sequence of LEU3_THET8
EC Number:1.1.1.85
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
3-isopropylmalate dehydrogenase
Q5SIY4
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)
345
36780
Reaction
(2R,3S)-3-isopropylmalate + NAD+ = (2S)-2-isopropyl-3-oxosuccinate + NADH + H+
General information:
Sequence
0 MKVAVLPGDG IGPEVTEAAL KVLRALDEAE GLGLAYEVFP FGGAAIDAFG EPFPEPTRKG
60 VEEAEAVLLG SVGGPKWDGL PRKIRPETGL LSLRKSQDLF ANLRPAKVFP GLERLSPLKE
120 EIARGVDVLI VRELTGGIYF GEPRGMSEAE AWNTERYSKP EVERVARVAF EAARKRRKHV
180 VSVDKANVLE VGEFWRKTVE EVGRGYPDVA LEHQYVDAMA MHLVRSPARF DVVVTGNIFG
240 DILSDLASVL PGSLGLLPSA SLGRGTPVFE PVHGSAPDIA GKGIANPTAA ILSAAMMLEH
300 AFGLVELARK VEDAVAKALL ETPPPDLGGS AGTEAFTATV LRHLA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
691228
Kagawa Y.,Nojima H.,Nukiwa N.,Ishizuka M.,Nakajima T.,Yasuhara T.,Tanaka T.,Oshima T.
High guanine plus cytosine content in the third letter of codons of an extreme thermophile. DNA sequence of the isopropylmalate dehydrogenase of Thermus thermophilus.
J. Biol. Chem.
259
2956-2960
1984
691229
Kirino H.,Aoki M.,Aoshima M.,Hayashi Y.,Ohba M.,Yamagishi A.,Wakagi T.,Oshima T.
Hydrophobic interaction at the subunit interface contributes to the thermostability of 3-isopropylmalate dehydrogenase from an extreme thermophile, Thermus thermophilus.
Eur. J. Biochem.
220
275-281
1994
691231
Miyazaki K.,Oshima T.
Tyr-139 in Thermus thermophilus 3-isopropylmalate dehydrogenase is involved in catalytic function.
FEBS Lett.
332
37-38
1993
691232
Hurley J.H.,Dean A.M.
Structure of 3-isopropylmalate dehydrogenase in complex with NAD+: ligand-induced loop closing and mechanism for cofactor specificity.
Structure
2
1007-1016
1994
691233
Nagata C.,Moriyama H.,Tanaka N.,Nakasako M.,Yamamoto M.,Ueki T.,Oshima T.
Cryocrystallography of 3-Isopropylmalate dehydrogenase from Thermus thermophilus and its chimeric enzyme.
Acta Crystallogr. D
52
623-630
1996
691234
Imada K.,Sato M.,Tanaka N.,Katsube Y.,Matsuura Y.,Oshima T.
Three-dimensional structure of a highly thermostable enzyme, 3-isopropylmalate dehydrogenase of Thermus thermophilus at 2.2-A resolution.
J. Mol. Biol.
222
725-738
1991
691235
Nurachman Z.,Akanuma S.,Sato T.,Oshima T.,Tanaka N.
Crystal structures of 3-isopropylmalate dehydrogenase with mutations at the C-terminus: crystallographic analyses of structure-stability relationships.
Protein Eng.
13
253-258
2000
691236
Qu C.,Akanuma S.,Tanaka N.,Moriyama H.,Oshima T.
Design, X-ray crystallography, molecular modelling and thermal stability studies of mutant enzymes at site 172 of 3-isopropylmalate dehydrogenase from Thermus thermophilus.
Acta Crystallogr. D
57
225-232
2001