2.3.3.14: homocitrate synthase
This is an abbreviated version!
For detailed information about homocitrate synthase, go to the full flat file.
Word Map on EC 2.3.3.14
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2.3.3.14
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gyrus
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resting-state
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frontal
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deficit
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sclerosis
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cingulate
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schizophrenia
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hair
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emotional
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prefrontal
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inferior
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anxiety
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bipolar
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neuropsychological
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auditory
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parietal
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insula
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neuroimaging
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occipital
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default
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precuneus
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high-content
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verbal
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cochlea
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putamen
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whole-brain
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tensor
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voxel-based
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precentral
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nervosa
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first-episode
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relapsing-remitting
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obsessive-compulsive
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salience
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hemichannels
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t1-weighted
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orbitofrontal
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dlpfc
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visuospatial
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unmedicated
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parahippocampal
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impulsivity
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event-related
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fluency
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fasciculus
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connectome
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tractography
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peripapillary
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euthymic
-
stroop
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biotechnology
-
synthesis
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medicine
- 2.3.3.14
- gyrus
-
resting-state
-
frontal
- deficit
- sclerosis
-
cingulate
-
schizophrenia
- hair
-
emotional
-
prefrontal
-
inferior
-
anxiety
-
bipolar
-
neuropsychological
-
auditory
-
parietal
-
insula
-
neuroimaging
-
occipital
-
default
-
precuneus
-
high-content
-
verbal
- cochlea
-
putamen
-
whole-brain
-
tensor
-
voxel-based
-
precentral
-
nervosa
-
first-episode
-
relapsing-remitting
-
obsessive-compulsive
-
salience
-
hemichannels
-
t1-weighted
-
orbitofrontal
-
dlpfc
-
visuospatial
-
unmedicated
-
parahippocampal
-
impulsivity
-
event-related
-
fluency
-
fasciculus
-
connectome
-
tractography
-
peripapillary
-
euthymic
-
stroop
- biotechnology
- synthesis
- medicine
Reaction
Synonyms
2-hydroxybutane-1,2,4-tricarboxylate 2-oxoglutarate-lyase (CoA-acetylating), acetyl-coenzyme A: 2-ketoglutarate C-transferase, acetyl-coenzyme A:2-ketoglutarate C-acetyl transferase, EC 4.1.3.21, HCS, HcsA, homocitrate synthase, homocitrate synthetase, homocitrate-condensing enzyme, homocondensing enzyme, LYS20, LYS21, Lys21p, LYS22, Lys22p, nifV, nifV2, saci_1304, SpHCS, synthase, homocitrate, TtHCS
ECTree
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Engineering
Engineering on EC 2.3.3.14 - homocitrate synthase
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E155A
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mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. Activity of E155A can be partially rescued by formate
E155Q
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mutant enzyme exhibits 1000fold lower activity than wild-type enzyme. The kcat for E155Q decreases at high pH, similar to the wild-type enzyme, but is pH independent at low pH
H309A
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inactive mutant enzyme. Slight increase in activity is observed for H309A in the presence of 300 mM imidazole, which is still 1000fold lower than that of wild type
Y320F
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mutant enzyme loses 25fold activity compared to that of the wild-type enzyme
E167A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
E167Q
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mutant, reveals the contribution of this residue to substrate binding and catalysis
E74A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
E74Q
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mutant, reveals the contribution of this residue to substrate binding and catalysis
H103A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
Q47A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
R163A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
R163K
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mutant, reveals the contribution of this residue to substrate binding and catalysis
R163Q
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mutant, reveals the contribution of this residue to substrate binding and catalysis
R43A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
R43K
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mutant, reveals the contribution of this residue to substrate binding and catalysis
R43Q
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mutant, reveals the contribution of this residue to substrate binding and catalysis
S165A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
T197A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
T197S
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mutant, reveals the contribution of this residue to substrate binding and catalysis
T197V
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mutant, reveals the contribution of this residue to substrate binding and catalysis
Y332A
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mutant, reveals the contribution of this residue to substrate binding and catalysis
Y332F
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mutant, reveals the contribution of this residue to substrate binding and catalysis
H72L
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replacement of His72 by leucine makes HCS resistant to lysine inhibition, demonstrating the regulatory role of this conserved residue
additional information
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activity and protein level of homocitrate synthase are dramatically reduced upon depletion of CuZn-superoxide dismutase. Overexpression of the lys4 gene increases homocitrate synthase activity and is sufficient to suppress the lysine requirement of CuZn-superoxide dismutase-deficient cells
additional information
the RAM domain is responsible for enzyme inhibition. A mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine
additional information
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the RAM domain is responsible for enzyme inhibition. A mutant enzyme lacking the RAM domain is insensitive to inhibition by lysine
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