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1.1.1.85: 3-isopropylmalate dehydrogenase

This is an abbreviated version!
For detailed information about 3-isopropylmalate dehydrogenase, go to the full flat file.

Word Map on EC 1.1.1.85

Reaction

(2R,3S)-3-isopropylmalate
+
NAD+
=
(2S)-2-isopropyl-3-oxosuccinate
+
NADH
+
H+

Synonyms

2-hydroxy-4-methyl-3-carboxyvalerate:NAD+ oxidoreductase, 2R,3S-isopropylmalate:NAD+ oxidoreductase (decaboxylating), 3-IPM dehydrogenase, 3-IPM-DH, 3-isopropylmalate dehydrogenase, 3-isopropylmalateDH, APS IPMDH, beta-IPM dehydrogenase, beta-IPMDH, beta-isopropylmalate dehydrogenase, beta-isopropylmalic enzyme, Bs3-isopropylmalateDH, dehydrogenase, 3-isopropylmalate, IMDH, IPMDH, IPMDH1, IPMDH2, IPMDH3, isopropylmalate dehydrogenase, leuB, NAD-dependent isopropylmalate dehydrogenase, Saci_0600, SbIPMDH, SoIPMDH, threo-Ds-3-isopropylmalate dehydrogenase, Tt-beta-3-isopropylmalateDH, two-domain 3-isopropylmalate dehydrogenase, Ydr417cp

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.1 With NAD+ or NADP+ as acceptor
                1.1.1.85 3-isopropylmalate dehydrogenase

Cloned

Cloned on EC 1.1.1.85 - 3-isopropylmalate dehydrogenase

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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned into the pIVEX2.4d vector and expressed in Escherichia coli
-
construction of a chimeric gene by fusing the Bacillus subtilis and Thermus thermophilus genes coding for 3-isopropylmalate dehydrogenase, expression in Escherichia coli
effectively expressed both Escherichia coli and Bacillus subtilis
-
expressed as His-tagged and non-His-tagged fusion proteins in Escherichia coli
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3)Codon-Plus-RIL cells
expressed in Escherichia coli HB101 cells
expressed in the Escherichia coli BL21 (DE3)
expression in Escherichia coli
expression in Escherichia coli and Bacillus subtilis using pLS353 as a vector and PstI as an enzyme, enzyme activities in both Escherichia coli and Bacillus subtilis transformants are 4-8fold higher than those in the present strains
-
expression in Escherichia coli C6000 using pBR322 as a vector plasmid
-
expression in Escherichia coli or yeast
-
expression in Escherichia coli using pBR322 as a vector
expression of wild-type and mutant enzymes in Escherichia coli
-
gene LEU2, DNA and amino acid sequence determination and analysis, sequence comparison, subcloning in Escherichia coli, and complementation of an enzyme-deficient Saccharomyces cerevisiae strain HS1-2
gene leuB, DNA and amino acid sequence determination and analysis, phylogenetic analysis, expression of wild-type and mutants in Escherichia coli strain MA153
gene leuB, expression of wild-type and mutant enzymes in Escherichia coli strain MA153
gene leuB, expression of wild-type and mutants in Escherichia coli strain MA153
genes IMD1, IMD2, and IMD3, DNA and amino acid sequence determination and analysis, expression analysis, complementation of the deficient Saccharomyces cerevisiae strain BY4741
-
phylogenetic analysis, comparison to isocitrate dehydrogenase, EC 1.1.1.41, overview
recombinant enzyme expression in Escherichia coli
-
the sequence motif is introduced into a mesophilic Escherichia coli isopropylmalate dehydrogenase, one by one. The introduction of the whole motif leads the mesophilic enzyme to be more unstable whereas substitution of only one amino acid residue in the motif thermostabilizes the enzyme
-
two ancestral sequences of 3-isopropylmalate dehydrogenase (ancIPMDH-IQ and ancIPMDH-ML) are designed by an ancestral sequence reconstruction technique based on a phylogenetic analysis of extant homologous amino acid sequences. Genes encoding the designed sequences are artificially synthesized and expressed in Escherichia coli
-
wild type and mutant leuB genes are overexpressed in Escherichia coli