Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

4.1.3.1: isocitrate lyase

This is an abbreviated version!
For detailed information about isocitrate lyase, go to the full flat file.

Word Map on EC 4.1.3.1

Reaction

isocitrate
=
succinate
 +
glyoxylate

Synonyms

AceA, acuD, citrate lyase, D-threo-isocitrate: glyoxylate lyase, EgGCE, FPICL1, ICL, ICL1, ICL2, isocitrase, isocitratase, isocitrate lyase, isocitrate lyase 1, isocitrate lyase 2, isocitric lyase, isocitritase, lyase, isocitrate, MtbIcl, PDP, petal death protein, SSO1333, threo-DS-Isocitrate glyoxylate-lyase

ECTree

     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.1 isocitrate lyase

Engineering

Engineering on EC 4.1.3.1 - isocitrate lyase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C165S
-
behaves as the wild-type
C165S/C247S
-
is inactivated by 5 mM GSSG and reactivated by treatment with either 20 mM reduced dithiothreitol or reduced glutaredoxin 1 as the wild-type protein. Complete shift in molecular mass corresponding to one glutathione adduct after 5 h of incubation, but prolonged incubation does not induce any additional glutathionylation
C165S/C247S/C301S
-
is inactivated by 5 mM GSSG and reactivated by treatment with either 20 mM reduced dithiothreitol or reduced glutaredoxin 1 as the wild-type protein. Complete shift in molecular mass corresponding to one glutathione adduct after 5 h of incubation, but prolonged incubation does not induce any additional glutathionylation
C178S
-
is totally inactive
C247S
-
behaves as the wild-type. Complete shift in molecular mass corresponding to one glutathione adduct after 5 h of incubation, but prolonged incubation does not induce any additional glutathionylation
C301S
-
behaves as the wild-type
Q207H
-
mutant with decreased activity between 10°C and 25°C
Q217K
-
mutant with decreased activity between 10°C and 25°C
A214S
increased thermostability and low specific activity at low temperature
A231E
more thermolabile than the wild type enzyme
A341N
decreased activity compared to the wild type enzyme
F333L
very low activity
Q47K
activity similar to the wild type enzyme
A214S
-
increased thermostability and low specific activity at low temperature
-
A231E
-
more thermolabile than the wild type enzyme
-
A341N
-
decreased activity compared to the wild type enzyme
-
F333L
-
very low activity
-
Q47K
-
activity similar to the wild type enzyme
-
C144A
mutant with no enzyme activity
D79A
mutant with 1000fold reduced turnover rate
A219C
-
similar catalytic properties as the wild-type enzyme
D475N
putative acetyl-CoA binding site of malate synthase, no malate synthase activity, but isocitrate lyase activity
R187K
putative acetyl-CoA binding site of malate synthase, no malate synthase activity, but isocitrate lyase activity
C191A
unable to form the closed conformation crystal form
C195A
reduced activity
C195S
reduced activity
E423D
the mutant shows about 75% of wild type enzyme activity
E423D/E424D
the mutant shows about 60% of wild type enzyme activity
E424D
the mutant shows about 70% of wild type enzyme activity
F345A
the mutation leads to complete loss of the enzyme activity, compromises the enzyme stability, and modulates the structural dynamics and flexibility of the protein
H180A
the mutation leads to the destabilization and formation of inactive monomeric enzyme
C191A
-
unable to form the closed conformation crystal form
-
C195A
-
reduced activity
-
C195S
-
reduced activity
-
E423D
-
the mutant shows about 75% of wild type enzyme activity
-
F345A
-
the mutation leads to complete loss of the enzyme activity, compromises the enzyme stability, and modulates the structural dynamics and flexibility of the protein
-
H180A
-
the mutation leads to the destabilization and formation of inactive monomeric enzyme
-
E219A
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity compared to the wild-type enzyme
N214D
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows 10fold reduced activity compared to the wild-type enzyme
Q211H
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity and elevated temperature optimum compared to the wild-type enzyme
Q221K
site-directed mutagenesis of the highly conserved residue in the ICL subfamily 3 catalytic pattern, the mutant enzyme shows reduced activity and elevated temperature optimum compared to the wild-type enzyme
T524V
the mutant shows increased Km and reduced kcat values compared to the wild type enzyme
T534A
the mutant shows reduced Km and kcat values compared to the wild type enzyme
additional information