1.1.1.87: homoisocitrate dehydrogenase

This is an abbreviated version, for detailed information about homoisocitrate dehydrogenase, go to the full flat file.

Reaction

(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate
+
NAD+
=
2-oxoadipate
+
CO2
+
NADH
+
H+

Synonyms

(-)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase (decarboxylating), 11-cis-RDH, 11-cis-retinol dehydrogenase, 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), atRDH, dehydrogenase, homoisocitrate, EC 1.1.1.155, HIc, HIc dehydrogenase, HICDH, homoisocitrate dehydrogenase, homoisocitric dehydrogenase, isocitrate-homoisocitrate dehydrogenase, protein PH1722, RDH10, retinol dehydrogenase 10, ScHICDH

ECTree

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

Engineering

Engineering on EC 1.1.1.87 - homoisocitrate dehydrogenase

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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
D169A
-
mutant enzyme completely loses enzymatic activity
D169N
-
mutant enzyme completely loses enzymatic activity
G43A/G47A/G49A
-
mutant enzyme completely loses enzymatic activity
K214A
-
mutant enzyme completely loses enzymatic activity
K214R
-
mutant enzyme completely loses enzymatic activity
S197A
-
mutation does not abolish activity
S197C
-
mutant enzyme completely loses enzymatic activity
S197G
-
mutation does not abolish activity
S197T
-
mutant enzyme completely loses enzymatic activity
S197V
-
mutant enzyme completely loses enzymatic activity
Y210A
-
mutant enzyme completely loses enzymatic activity
Y210F
-
mutant enzyme completely loses enzymatic activity
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
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
additional information