Reference on EC 4.2.1.33 - 3-isopropylmalate dehydratase
Please use the Reference Search for a specific query.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Gross, S.R.
Isopropylmalate isomerase (Neurospora)
Methods Enzymol.
17A
786-790
1970
Neurospora sp., Salmonella sp.
-
Bigelis, R.; Umbarger, H.E.
Yeast alpha-isopropylmalate isomerase. Factors affecting enzyme stability and enzyme activity
J. Biol. Chem.
251
3545-3552
1976
Saccharomyces cerevisiae
Reichenbecher Jr, V.E.; Gross, S.R.
Structural features of normal and complemented forms of the Neurospora isopropylmalate isomerase
J. Bacteriol.
133
802-810
1978
Neurospora crassa
Gross, S.R.; Umbarger, H.E.
The biosynthesis of leucine: II. The enzymic isomerization of beta-carboxy-beta-hydroxyisocaproate and alpha-hydroxy-beta-carboxyisocaproate
Biochemistry
2
1046-1052
1963
Neurospora crassa, Salmonella enterica subsp. enterica serovar Typhimurium
Reichenbecher, V.E.; Fischer, M.; Gross, S.R.
Regulation of isopropylmalate synthesis in Neurospora crassa
J. Bacteriol.
133
794-801
1978
Neurospora crassa
Kohlhaw, G.B.
Isopropylmalate dehydratase from yeast
Methods Enzymol.
166
423-429
1988
Saccharomyces cerevisiae
Bode, R.; Birnbaum, D.
Some properties of the leucine-biosynthesizing enzymes from Candida maltosa
J. Basic Microbiol.
31
21-26
1991
Candida maltosa
-
Hayashi, M.; Mizoguchi, H.; Ohnishi, J.; Mitsuhashi, S.; Yonetani, Y.; Hashimoto, S.; Ikeda, M.
A leuC mutation leading to increased L-lysine production and rel-independent global expression changes in Corynebacterium glutamicum
Appl. Microbiol. Biotechnol.
72
783-789
2006
Corynebacterium glutamicum, Corynebacterium glutamicum B-6
Hamaji, T.; Ferris, P.J.; Coleman, A.W.; Waffenschmidt, S.; Takahashi, F.; Nishii, I.; Nozaki, H.
Identification of the minus-dominance gene ortholog in the mating-type locus of Gonium pectorale
Genetics
178
283-294
2008
Gonium pectorale
Karuppasamy, M.; Geerlof, A.; Schuldt, L.; Mueller-Dieckmann, C.; Weiss, M.S.
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the small subunit of isopropylmalate isomerase (Rv2987c) from Mycobacterium tuberculosis
Acta Crystallogr. Sect. F
65
136-139
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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
Arabidopsis thaliana (Q94AR8), Arabidopsis thaliana (Q94AR8 AND Q9ZW84), Arabidopsis thaliana (Q9LYT7), Arabidopsis thaliana (Q9ZW84), Arabidopsis thaliana (Q9ZW85), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q94AR8 AND Q9ZW84)
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
Arabidopsis thaliana
Manikandan, K.; Geerlof, A.; Zozulya, A.V.; Svergun, D.I.; Weiss, M.S.
Structural studies on the enzyme complex isopropylmalate isomerase (LeuCD) from Mycobacterium tuberculosis
Proteins
79
35-49
2011
Mycobacterium tuberculosis (P9WK95), Mycobacterium tuberculosis (P9WQF5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WK95), Mycobacterium tuberculosis H37Rv (P9WQF5)
Yasutake, Y.; Yao, M.; Sakai, N.; Kirita, T.; Tanaka, I.
Crystal structure of the Pyrococcus horikoshii isopropylmalate isomerase small subunit provides insight into the dual substrate specificity of the enzyme
J. Mol. Biol.
344
325-333
2004
Pyrococcus horikoshii (O59393), Pyrococcus horikoshii
Lee, E.H.; Lee, K.; Hwang, K.Y.
Structural characterization and comparison of the large subunits of IPM isomerase and homoaconitase from Methanococcus jannaschii
Acta Crystallogr. Sect. D
70
922-931
2014
Methanocaldococcus jannaschii (P81291), Methanocaldococcus jannaschii, Methanocaldococcus jannaschii DSM 2661 (P81291)
Lee, E.H.; Cho, Y.W.; Hwang, K.Y.
Crystal structure of LeuD from Methanococcus jannaschii
Biochem. Biophys. Res. Commun.
419
160-164
2012
Methanocaldococcus jannaschii (Q58673), Methanocaldococcus jannaschii
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
e91071
2014
Arabidopsis thaliana
html completed