1.1.1.87: homoisocitrate dehydrogenase
This is an abbreviated version!
For detailed information about homoisocitrate dehydrogenase, go to the full flat file.
Word Map on EC 1.1.1.87
-
1.1.1.87
-
alpha-aminoadipate
-
3-isopropylmalate
-
homocitrate
-
homoaconitase
-
beta-decarboxylating
-
alpha-ketoadipate
-
medicine
-
synthesis
- 1.1.1.87
- alpha-aminoadipate
- 3-isopropylmalate
- homocitrate
- homoaconitase
-
beta-decarboxylating
- alpha-ketoadipate
- medicine
- synthesis
Reaction
Synonyms
(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating), 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), beta-decarboxylating dehydrogenase, dehydrogenase, homoisocitrate, EC 1.1.1.155, HIc, HIc dehydrogenase, HICDH, homoisocitrate dehydrogenase, homoisocitric dehydrogenase, isocitrate-homoisocitrate dehydrogenase, LYS12, protein PH1722, ScHICDH, TK0280
ECTree
Advanced search results
Engineering
Engineering on EC 1.1.1.87 - homoisocitrate dehydrogenase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
A80del
-
site-directed mutagenesis, the mutant shows altered substrate specificity preferring isocitrate to homoisocitrate, it is unable to oxidize 3-isopropylmalate, the specificity is similar to the enzyme from Thermus thermophilus
R87T
-
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
R87V
-
site-directed mutagenesis, the mutant oxidizes homoisocitrate, but not isocitrate and 3-isopropylmalate
D271N
site-directed mutagenesis, mutation of a metal ion ligand and binding determinant for Mg2+, to N. The mutant enzyme shows a decrease of 520fold in V and V/Km_Mg2+, suggesting that the same step(s) limit the reaction at limiting and saturating MgHIc concentrations
K206M
Y150F
I82N
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
L81P
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
L83R
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
S80A
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
T71V
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate, as well as increased catalytic efficiency with 3-isopropylmalate compared to the wild type enzyme
I82N
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
-
L81P
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
-
L83R
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate compared to the wild type enzyme and has no activity with 3-isopropylmalate
-
S80A
-
the mutant shows decreased catalytic efficiency with homoisocitrate, isocitrate and 3-isopropylmalate compared to the wild type enzyme
-
T71V
-
the mutant shows decreased catalytic efficiency with homoisocitrate and isocitrate, as well as increased catalytic efficiency with 3-isopropylmalate compared to the wild type enzyme
-
R85V
-
complete loss of activity with isocitrate, significant activity with 3-isopropylmalate, no effect on activity with homoisocitrate
V135M
-
site-directed mutagenesis, tetramer-to-dimer structural transition enhances the activity with isocitrate 1.6fold
R85V
Thermus thermophilus HB27 / ATCC BAA-163 / DSM 7039
-
complete loss of activity with isocitrate, significant activity with 3-isopropylmalate, no effect on activity with homoisocitrate
-
additional information
K206M
-
site-directed mutagenesis, the active site mutant shows about 2400fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly
Y150F
-
site-directed mutagenesis, the active site mutant shows about 680fold reduced activity compared to the wild-type enzyme, the Km for HIc does not change significantly
-
modulation of the broad substrate specificity of the trifunctional enzyme through site-directed mutagenesis, overview
additional information
-
trex mutant allele, T to C exchange at nucleotide 251. Midgestation lethal mutant which displays craniofacial, limb, and organ abnormalities due to insufficient retinoic acid signaling