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ATP + DL-threo-3-methyl aspartate
ADP + 3-methyl-4-phosphoaspartate
-
aspartokinase III
-
-
?
ATP + L-asparagine
?
-
aspartokinase III
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
ATP + L-aspartate
ADP + phospho-L-aspartate
ATP + L-aspartate beta-hydroxamate
?
-
aspartokinase III
-
-
?
ATP + L-aspartate beta-methyl ester
?
-
aspartokinase III
-
-
?
ATP + L-aspartic acid 1-benzyl ester
?
-
aspartokinase III
-
-
?
ATP + L-aspartic acid 4-benzyl ester
?
-
aspartokinase III
-
-
?
ATP + L-aspartic acid amide
ADP + 4-phospho-L-aspartic acid amide
-
aspartokinase III
-
-
?
ATP + N-acetyl-L-aspartate
ADP + N-acetyl-4-phospho-L-aspartate
-
aspartokinase III
-
-
?
ATP + N-chloroacetyl-L-aspartate
ADP + N-chloroacetyl-4-phospho-L-aspartate
-
aspartokinase III
-
-
?
ATP + N-formyl-L-aspartate
ADP + N-formyl-4-phospho-L-aspartate
-
aspartokinase III
-
-
?
GTP + L-aspartate
GDP + 4-phospho-L-aspartate
-
-
-
r
additional information
?
-
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
first and third step of the synthesis of methionine, catalyzed by a bifunctional enzyme
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step of a branched biosynthetic pathway for L-lysine, L-threonine, L-isoleucine and L-methionine, regulated by the end products through feedback inhibition, the 3 aspartate kinases I, II and II are regulated by different end products
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
physiological role of aspartokinase II is to supply precursors for the amino acid pool
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first specific step in the biosynthesis of L-lysine, L-threonine and L-methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
transfer of the gamma-phosphate group of ATP to aspartate, substrate binding site structures, overview
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
ir
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
disruption analyes of Deinococcus radiodurans AK indicates that the AK is not used for lysine biosynthesis, but for threonine and methionine biosyntheses
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
disruption analyes of Deinococcus radiodurans AK indicates that the AK is not used for lysine biosynthesis, but for threonine and methionine biosyntheses
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
maximum velocity of the reverse reaction is only one-twelfth that of the forward reaction, but has the advantage of using commercial substrates
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step in the branched biosynthetic pathway for the synthesis of L-lysine, L-methionine, L-threonine, L-isoleucine and diaminopimelic acid
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
part of the aspartate pathway of amino acid biosynthesis
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
aspartate kinase activity
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step in the branched biosynthetic pathway for the synthesis of L-lysine, L-methionine, L-threonine, L-isoleucine and diaminopimelic acid
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first and key enzyme of the aspartate pathway leading to the biosynthesis of essential amino acids L-lysine and L-threonine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
branched pathway for biosynthesis of isoleucine, threonine, homoserine, methionine and lysine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
L-aspartate binds to this recombinant enzyme in two different orientations
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first enzyme of aspartic acid metabolic pathway, leads to synthesis of lysine, threonine, methionine and isoleucine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step in the branched pathway leading to synthesis of threonine and methionine from aspartate
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step of the branched biosynthetic pathway for lysine, threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
-
-
r
ATP + L-aspartate
ADP + 4-phospho-L-aspartate
-
first step common to the biosynthesis of L-lysine, L-threonine, isoleucine and methionine
-
r
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
-
-
-
?
ATP + L-aspartate
ADP + phospho-L-aspartate
-
maximum activity is achieved with 12.5 mM MgSO4 and 20 mM ATP
-
-
?
additional information
?
-
no isoenzymes
-
-
?
additional information
?
-
-
no isoenzymes
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
aspartokinase III, D-isomers of the derivatives of aspartic acid, including D-aspartate alpha-benzyl ester and D-aspartate beta-hydroxamate are not substrates regardless of whether the alpha- or the beta-carboxyl group is derivatized, L-cysteine sulfinate and 2-methyl-DL-aspartate are no substrates
-
-
?
additional information
?
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3
-
-
-
additional information
?
-
-
activity is regulated by light
-
-
?
additional information
?
-
-
no other natural aminoacids or D-aspartate are substrates of this reaction
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
aspartate analogues succinate, maleate, L-glutamate and DL-2-amino-3-phosphonopropionate have no influence on the reaction
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
absolute requirement for ATP, no other nucleoside phosphates serve as phosphate donor, analogs of aspartate such as L-glutamate, DL-alpha-methyl aspartate, N-acetyl aspartate and D-aspartate are inactive as acceptors
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
-
D-aspartate, L-glutamate and beta-alanine are inactive as substitutes for L-aspartate in the forward reaction, in the reverse reaction ADP cannot be replaced by AMP, UDP, GDP or IDP
-
-
?
additional information
?
-
-
strict requirement for ATP as a phosphorylating agent, CTP and GTP are not active
-
-
?
additional information
?
-
-
strict requirement for ATP as a phosphorylating agent, CTP and GTP are not active
-
-
?
additional information
?
-
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3. It shows substantial activities of both aspartate kinase (AK) and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3. It shows substantial activities of both aspartate kinase (AK) and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3. It shows substantial activities of both aspartate kinase (AK) and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3. It shows substantial activities of both aspartate kinase (AK) and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
the bifunctional enzyme also exhibits L-homoserine dehydrogenase activity, EC 1.1.1.3. It shows substantial activities of both aspartate kinase (AK) and homoserine dehydrogenase (HseDH)
-
-
-
additional information
?
-
-
no reaction observed with ITP, CTP or UTP
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxy-L-norvaline
works as L-threonine analog
ADP
-
competitive inhibition
aspartate-beta-semialdehyde
D-aspartate beta-hydroxamate
-
-
D-aspartic acid 1-benzyl ester
-
-
Diethyl aminomalonate
-
-
DL-2,6-Diaminoheptanoate
-
-
DL-3-amino-4-hydroxybutyrate methyl ester
-
-
DL-3-hydroxy-L-norvaline
L-lysine-analog
DL-meso-diaminopimelic acid
iodosalicylate
-
20% inhibition
L-2-aminobutyrate
-
competitive inhibitor
L-alanine
-
no significant effect on AK activity at 5 and 20 mM
L-glutamate gamma-methyl ester
-
-
L-leucine
-
allosteric effector
L-Threonine methyl ester
-
in combination with either L-lysine or L-methionine
methionine
-
concerted feedback inhibition with L-threonine
N-epsilon-formyl-L-lysine
-
-
p-chloromercuribenzoate
-
-
S-(2-aminoethyl)-L-cysteine
L-threonine-analog; works as L-lysine analog
S-2-aminoethyl-L-cysteine
-
less effective on the first isoenzyme than L-lysine alone
aspartate-beta-semialdehyde
-
-
aspartate-beta-semialdehyde
-
-
DL-meso-diaminopimelic acid
-
aspartokinase I, noncompetitive inhibition
DL-meso-diaminopimelic acid
-
ATCC6051, aspartokinase I
DL-meso-diaminopimelic acid
-
-
DL-meso-diaminopimelic acid
-
-
EGTA
-
isoenzyme II
L-homoserine
-
-
L-homoserine
inhibits the activity of aspartokinase encoded by metL
L-isoleucine
-
repression of aspartokinase gene transcription
L-isoleucine
-
no significant effect on AK activity at 5 and 20 mM
L-lysine
-
-
L-lysine
-
repression of aspartokinase gene transcription
L-lysine
-
no significant effect on AK activity at 5 and 20 mM
L-lysine
AK1 is inhibited in a synergistic manner by lysine and S-adenosyl-L-methionine, in the absence of S-adenosyl-L-methionine AK1 displays low apparent affinity for lysine compared to AK2 and AK3; AK1 is inhibited in a synergistic manner by lysine and SAM; AK2 is inhibited by lysine, SAM by itself has no effect on the enzyme activity; AK3 is inhibited only by lysine, SAM by itself has no effect on the enzyme activity
L-lysine
-
no inhibition is observed; the truncated protein is no longer inhibited by lysine, even at 10 mM, wild type protein is inhibited by lysine
L-lysine
-
concerted feedback inhibition with L-threonine
L-lysine
threonine and lysine exhibit concerted feedback inhibition of asparatate kinase. Large conformational changes in the catalytic domain are associated with the lysine binding at the regulatory domains, L-lysine binding site structure, overview
L-lysine
-
concerted feedback inhibition with L-threonine
L-lysine
AK is inhibited moderately by Lys, the enzyme is inhibited dramatically by simultaneous addition of Lys and Thr, dimerization of the regulatory subunit induced by Thr binding is a key step in the inhibitory mechanism of AK; feedback inhibition, inhibits moderately, simultaneous addition of lysine and threonine inhibits dramatically
L-lysine
-
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit
L-lysine
feedback inhibition
L-lysine
-
feedback inhibition
L-lysine
each dimer contains two lysine binding sites, in which one site is exclusively found in the dimer with A and B chains located at the interface between alpha and beta subunits
L-lysine
-
85.43% residual activity at 10 mM
L-lysine
-
85.43% residual activity at 10 mM. The inhibition rate for the single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met)
L-lysine
-
40.72% residual activity at 10 mM
L-lysine
-
binding of L-lysine to the regulatory ACT1 domain in R-state AKIII instigates a series of changes that release a 'latch', the beta15-alphaK loop, from the catalytic domain, which in turn undergoes large rotational rearrangements, promoting tetramer formation and completion of the transition to the T-state. L-lysine-induced allosteric transition in AKIII involves both destabilizing the R-state and stabilizing the T-state tetramer. Rearrangement of the catalytic domain blocks the ATP-binding site, which is therefore the structural basis for allosteric inhibition of AKIII by L-lysine
L-lysine
-
inhibited 50% by 0.7 mM, almost completely by 5.0 mM
L-lysine
-
inhibits the activity of ThrA2 by 87% at 1 mM and by 96% at 10 mM, no concerted inhibition by L-lysine plus L-threonine
L-lysine
-
concerted feedback inhibition with L-threonine
L-lysine
-
L-lysine inhibits Ask_LysC only in a mixture with L-threonine
L-lysine
-
partially inhibits the first isoenzyme
L-lysine
-
concerted feedback inhibition with L-threonine; L-threonine methyl ester and L-threonine amide are able to substitute for L-threonine in feedback inhibition, but the requirement for L-lysine is strict
L-lysine
feedback resistance of Ask, more than 20% relative activity of Ask in the assay mixture even with extremely high concentrations of 100 mM L-lysine and L-threonine each, L-Lysine alone has no effect on activity; more than 20% relative activity of rAsk is detected in the assay mixture even with extremely high concentrations of L-lysine and L-threonine (100 mM each), L-lysine alone has no effect on activity
L-lysine
enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-lysine, the enzyme displays partial inhibition by L-threonine (50% residual activity at saturation with L-threonine) with a K0.5 value of 0.7 mM
L-lysine
-
no inhibition is observed
L-lysine
-
2 mM, significant inhibition
L-lysine
Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity; Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity, to measure inhibition of AK activity by lysine, reaction rates using 50 mM Asp substrate are measured in the presence of 5 microM to 10 mM L-lysine
L-lysine
-
concerted feedback inhibition with L-threonine
L-methionine
feedback inhibition
L-methionine
-
feedback inhibition
L-methionine
-
72.66% residual activity at 5 mM
L-methionine
-
73.72% residual activity at 10 mM. The inhibition rate for a single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met)
L-methionine
-
inhibits the first isoenzyme at 5 mM
L-threonine
-
-
L-threonine
-
repression of aspartokinase gene transcription
L-threonine
-
inhibition at 0.5-1.0 mM in complemented S2207A cells is variable, it does not exceed 67%
L-threonine
-
in the presence of 1 mM aspartate and 2 mM ATP
L-threonine
-
aspartokinase II, competitive inhibition
L-threonine
-
almost insensitive to threonine
L-threonine
threonine and lysine exhibit concerted feedback inhibition of asparatate kinase
L-threonine
Thr alone has no effect on the inhibitory profile, the enzyme is inhibited dramatically by simultaneous addition of Lys and Thr; threonine alone has no effect, simultaneous addition of lysine and threonine inhibits dramatically
L-threonine
-
enzyme is inhibited by lysine and threonine in a concerted manner: comparison of the crystal structures between inhibitory and active forms reveal that binding inhibitors causes a conformational change to a closed inhibitory form, and the interaction between the catalytic domain in the alpha subunit and beta subunit
L-threonine
feedback inhibition
L-threonine
-
feedback inhibition
L-threonine
-
89.76% residual activity at 10 mM
L-threonine
-
89.37% residual activity at 5 mM. The inhibition rate for a single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met)
L-threonine
-
61.33% residual activity at 10 mM
L-threonine
-
feedback inhibition
L-threonine
-
represses, reduces growth rate, no concerted inhibition by L-lysine plus L-threonine
L-threonine
mechanism for allosteric regulation in which the domain movements induced by L-threonine binding causes displacement of the substrates from the enzyme, resulting in a relaxed, inactive conformation
L-threonine
-
above 10 mM
L-threonine
-
allosteric inhibition, causes a decrease in the apparent molecular mass of the enzyme, no inhibition is detected in the threonine insensitive mutant up to 50 mM threonine
L-threonine
75% inhibition at 10 mM, 22°C culture temperature, 22°C assay temperature, 71% inhibition at 10 mM, 37°C culture temperature, 22°C assay temperature, 87% inhibition at 10 mM, 22°C culture temperature, 37°C assay temperature, 86% inhibition at 10 mM, 37°C culture temperature, 37°C assay temperature, 93% inhibition of glutathione-S-transferase fusion protein at 10 mM, 22°C assay temperature, 73% inhibition of glutathione-S-transferase fusion protein at 10 mM, 37°C assay temperature; reduced sensitivity to threonine inhibition, 0% inhibition at 10 mM, 22°C culture temperature, 22°C assay temperature, 15% inhibition at 10 mM, 37°C culture temperature, 22°C assay temperature, 4% inhibition at 10 mM, 22°C culture temperature, 37°C assay temperature, 14% inhibition at 10 mM, 37°C culture temperature, 37°C assay temperature; resistance to feedback inhibition, 16% inhibition at 10 mM, 22°C culture temperature, 22°C assay temperature, 15% inhibition at 10 mM, 37°C culture temperature, 22°C assay temperature, 9% inhibition at 10 mM, 22°C culture temperature, 37°C assay temperature, 6% inhibition at 10 mM, 37°C culture temperature, 37°C assay temperature, 31% inhibition of GST-fusion protein at 10 mM, 22°C assay temperature, 16% inhibition of glutathione-S-transferase fusion protein at 10 mM, 37°C assay temperature
L-threonine
-
some inhibition of the first isoenzyme, together with L-lysine total inhibition
L-threonine
-
isoenzyme II
L-threonine
feedback resistance of Ask, more than 20% relative activity of Ask in the assay mixture even with extremely high concentrations of 100 mM L-lysine and L-threonine each, L-threonine alone has no effect on activity; more than 20% activity in the rAsk is detected even with extremely high concentrations of L-lysine and L-threonine (100 mM each), L-threonine alone has no effect on activity
L-threonine
enzyme is inhibited synergistically by L-threonine and L-lysine with the binding of threonine first. In the absence of L-threonine, the enzyme is inhibited by Lys in a cooperative manner, but the inhibition requires very high concentrations of L-lysine
L-threonine
inhibits AK activity in a cooperative manner by 90% at 0.35 mM. The distinctive sequence of the regulatory domain in Thermotoga maritima AK-HseDH is likely responsible for the unique sensitivity to L-threonine. The quaternary structure of this enzyme is not affected by L-threonine
L-threonine
feedback inhibition by the end product
L-threonine
-
concerted inhibition together with L-lysine
L-threonine
-
no inhibitory effect at 2 mM
N-ethylmaleimide
-
17% inhibition
S-adenosyl-L-methionine
AK1 is inhibited in a synergistic manner by lysine and S-adenosyl-L-methionine, in the presence of S-adenosyl-L-methionine, the apparent affinity of AK1 for lysine increases considerably for lysine inhibition similar to those of AK2 and AK3
S-adenosyl-L-methionine
-
potentiates inhibition by lysine
S-adenosyl-L-methionine
-
inhibits the reaction by 12%
S-adenosyl-L-methionine
-
only able to inhibit AK activity of the the first isoenzyme synergistically, when present with either L-lysine or L-threonine
threonine
-
-
additional information
-
mutant RL4 is lysine-resistant
-
additional information
-
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM SAM; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3; the other amino acids tested (Met, Gln, Asn, Glu, Arg) have no effect on the enzyme activities at 2.5 mM either in the presence or the absence of the inhibitor Lys or Lys plus SAM
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM SAM; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3; the other amino acids tested (Met, Gln, Asn, Glu, Arg) have no effect on the enzyme activities at 2.5 mM either in the presence or the absence of the inhibitor Lys or Lys plus SAM
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM SAM; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3; the other amino acids tested (Met, Gln, Asn, Glu, Arg) have no effect on the enzyme activities at 2.5 mM either in the presence or the absence of the inhibitor Lys or Lys plus SAM
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM SAM; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2; no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3; the other amino acids tested (Met, Gln, Asn, Glu, Arg) have no effect on the enzyme activities at 2.5 mM either in the presence or the absence of the inhibitor Lys or Lys plus SAM
-
additional information
-
threonine has no effect
-
additional information
completely resistant to inhibition by mixtures of L-lysine and threonine
-
additional information
-
completely resistant to inhibition by mixtures of L-lysine and threonine
-
additional information
-
dimerization of the regulatory subunit by Thr binding is the critical step of inhibition
-
additional information
dimerization of the regulatory subunit by Thr binding is the critical step of inhibition
-
additional information
aspartate kinase is an allosteric enzyme, and its activity is inhibited by allosteric inhibitors, such as Lys, Met, and Thr
-
additional information
-
aspartate kinase is an allosteric enzyme, and its activity is inhibited by allosteric inhibitors, such as Lys, Met, and Thr
-
additional information
-
L-methionine does not affect the enzyme by itself but at low concentrations increases the inhibition by L-lysine
-
additional information
L-lysine has no effect on activity at concentrations up to 10 mM, not inhibited by L-isoleucine and L-methionine
-
additional information
-
L-lysine has no effect on activity at concentrations up to 10 mM, not inhibited by L-isoleucine and L-methionine
-
additional information
insensitive to S-(2-aminoethyl)-L-cysteine at concentrations up to 12 mM
-
additional information
-
KCl, calcium, EGTA, calmodulin, compound 48/80 and L-valine have no effect on AK activity of the first isoenzyme
-
additional information
-
Ask of Streptomyces albulus CR1 is found to be the feedback resistant enzyme, but Ask of Streptomyces albulus CR1 is also subject to feedback inhibition by a mixture of L-lysine plus L-threonine of more than 1 mM each. L-lysine or L-threonine alone has no effect on activity.
-
additional information
Ask of Streptomyces albulus CR1 is found to be the feedback resistant enzyme, but Ask of Streptomyces albulus CR1 is also subject to feedback inhibition by a mixture of L-lysine plus L-threonine of more than 1 mM each. L-lysine or L-threonine alone has no effect on activity.
-
additional information
-
the enzyme is insensitive to lysine, threonine, methionine, and isoleucine. Furthermore, the addition of lysine + threonine or lysine + threonine + methionine + isoleucine does not affect its activity. The enzyme is not inhibited by 4-hydroxy-3-nitrosobenzamide (0.1 mM), and 3-amino-4-hydroxybenzoic acid (1 mM)
-
additional information
-
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine
-
additional information
L-homoserine oxidation of the Thermotoga maritima enzyme is almost impervious to inhibition by L-threonine
-
additional information
-
no inhibition with L-homoserine, L-methionine and L-isoleucine
-
additional information
-
addition of lysine and threonine together at 2 mM each results in a stronger inhibition than lysine alone
-
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147
DL-threo-3-methyl aspartate
-
pH 8.0, 25°C, aspartokinase III
16
L-asparagine
-
pH 8.0, 25°C, aspartokinase III
2.5
L-aspartate beta-benzyl ester
-
pH 8.0, 25°C, aspartokinase III
13
L-aspartate beta-hydroxamate
-
pH 8.0, 25°C, aspartokinase III
4.9
L-aspartate beta-methyl ester
-
pH 8.0, 25°C, aspartokinase III
1.8 - 50.1
L-aspartic acid
5.3
L-aspartic acid 1-benzyl ester
-
pH 8.0, 25°C, aspartokinase III
184
L-aspartic acid amide
-
pH 8.0, 25°C, aspartokinase III
48
N-acetyl-L-aspartate
-
pH 8.0, 25°C, aspartokinase III
68
N-Chloroacetyl-L-aspartate
-
pH 8.0, 25°C, aspartokinase III
41
N-formyl-L-aspartate
-
pH 8.0, 25°C, aspartokinase III
additional information
additional information
-
1.095
aspartate
AK3, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
1.94
aspartate
AK2, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
2.037
aspartate
30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
0.18
ATP
-
aspartokinase I
0.27
ATP
-
pH 7.5, 60°C, mutant G177A
0.29
ATP
-
pH 7.5, 60°C, mutant G149A
0.41
ATP
-
pH 7.5, 60°C, mutant G149A
0.42
ATP
-
50 mM aspartate, presence of alanine
0.43
ATP
-
pH 7.5, 60°C, mutant D174A
0.44
ATP
-
pH 7.5, 60°C, mutant S153A
0.45
ATP
-
pH 7.5, 60°C, mutant A157L
0.46
ATP
-
pH 7.5, 60°C, mutant G150A
0.48
ATP
-
50 mM aspartate, presence of alanine
0.5
ATP
-
pH 7.5, 60°C, wild-type and mutant G152A
0.52
ATP
-
pH 7.5, 60°C, mutant S12A, G135A
0.56
ATP
-
pH 7.5, 60°C, mutant T238A
0.56
ATP
AK3, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
0.57
ATP
-
pH 7.5, 60°C, mutant F136A
0.6
ATP
-
pH 7.5, 60°C, mutant I171A
0.63
ATP
-
pH 7.5, 60°C, mutant D154N
0.72
ATP
-
pH 7.5, 60°C, mutant A23L
0.8
ATP
-
wild type, in the presence of 10 mM aspartate
0.86
ATP
-
pH 7.5, 60°C, mutant Y8A
0.89
ATP
-
pH 7.5, 60°C, mutant V39A
0.97
ATP
-
pH 7.5, 60°C, mutant L148A
0.98
ATP
-
pH 7.5, 60°C, mutant A189L
0.98
ATP
AK2, 30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
1
ATP
-
pH 7.5, isoenzyme I
1.02
ATP
-
pH 7.5, 60°C, mutant A42S
1.05
ATP
-
pH 7.5, 60°C, mutant D154A
1.2
ATP
-
glutathione-S-transferase fusion protein, in the presence of 10 mM aspartate
1.2
ATP
-
threonine insensitive mutant, in the presence of 10 mM aspartate
1.28
ATP
-
pH 7.5, 60°C, mutant G73A
1.39
ATP
-
pH 7.5, 60°C, mutant S41A
1.62
ATP
-
pH 8.0, 30°C, mutant E257K/T359I
1.67
ATP
-
pH 7.5, isoenzyme II
1.7
ATP
30°C, 50 mM HEPES, pH 8.0, 150 mM KCl, 20 mM MgCl2 with a coupled assay using aspartate semialdehyde dehydrogenase from Arabidopsis thaliana
1.82
ATP
-
pH 8.0, 30°C, mutant T359I
1.89
ATP
-
pH 8.0, 30°C, mutant E257K
1.9
ATP
-
pH 7.5, 60°C, mutant P183A
1.9
ATP
-
aspartokinase II, 27°C
2.1
ATP
-
pH 7.5, 60°C, mutant T47A
2.2
ATP
-
50 mM aspartate, absence of alanine
2.45
ATP
-
pH 7.5, 60°C, mutant D182A
2.56
ATP
-
pH 8.0, 30°C, wild-type
3
ATP
wild-type, recombinant enzyme purified to homogeneity
3.54
ATP
at pH 7.0 and 55°C
3.54
ATP
recombinant enzyme, pH 7.5, 55°C
3.57
ATP
-
pH 7.5, 60°C, mutant G10A
3.7
ATP
mutant M68V, recombinant enzyme purified to homogeneity
4.8
ATP
-
aspartokinase III, 27°C
5.16
ATP
-
mutant enzyme M372I/T379W, at pH 7.4 and 28°C
5.4
ATP
-
mutant hom3-S45
6.5
ATP
-
50 mM aspartate, absence of alanine
7.93
ATP
-
wild type enzyme, at pH 7.4 and 28°C
10.4
ATP
-
mutant hom3-S49
12.9
ATP
pH 8.0, 30°C, 0.5 M effector threonine
0.19
L-aspartate
-
pH 7.5, 60°C, mutant A157L
0.27
L-aspartate
-
pH 7.5, 60°C, mutant E202A
0.32
L-aspartate
-
pH 7.5, 60°C, mutant Y8A, S12A
0.33
L-aspartate
-
pH 7.5, 60°C, mutant V39A
0.34
L-aspartate
-
pH 7.5, 60°C, mutant G177A
0.36
L-aspartate
-
pH 7.5, 60°C, mutant G149A, G177A
0.37
L-aspartate
-
pH 7.5, 60°C, mutant I171A
0.39
L-aspartate
-
pH 7.5, 60°C, mutant T238A
0.41
L-aspartate
-
pH 7.5, 60°C, mutant S41A
0.42
L-aspartate
-
pH 7.5, 60°C, mutant G152A, P183A
0.45
L-aspartate
-
pH 7.5, 60°C, mutant A189L
0.47
L-aspartate
-
pH 7.5, 60°C, mutant S153A
0.51
L-aspartate
-
recombinant hybrid bifunctional holoenzyme AKIII-HDHI+ containing the interface region, asparate kinase activity
0.53
L-aspartate
-
pH 7.5, 60°C, mutant D174A
0.6
L-aspartate
-
pH 8.0, 25°C, aspartokinase III
0.6
L-aspartate
-
pH 7.5, 60°C, mutant A42S
0.61
L-aspartate
-
pH 7.5, 60°C, mutant G73A
0.63
L-aspartate
-
recombinant wild-type bifunctional holoenzyme, asparate kinase activity
0.65
L-aspartate
-
pH 7.5, 60°C, mutant A23L
1
L-aspartate
-
pH 7.0, 25°C
1.04
L-aspartate
-
pH 8.0, 25°C
1.1
L-aspartate
-
threonine insensitive mutant, in the presence of 10 mM ATP
1.1
L-aspartate
-
wildtype, in the presence of 10 mM ATP
1.2
L-aspartate
-
pH 7.5, 60°C, mutant P183A
1.2
L-aspartate
-
glutathione-S-transferase fusion protein, in the presence of 10 mM ATP
1.23
L-aspartate
-
pH 7.5, 60°C, mutant R150A, D154A
1.31
L-aspartate
-
pH 7.5, 60°C, D182A
1.34
L-aspartate
-
pH 7.5, 60°C, mutant G10A, G135A
1.5
L-aspartate
-
pH 8.0, 25°C
1.5
L-aspartate
-
aspartokinase I
1.5
L-aspartate
-
20 mM ATP, presence of alanine
1.63
L-aspartate
-
mutant K18R
1.8
L-aspartate
mutant M68V
1.9
L-aspartate
-
at pH 8.0 and 30°C
2
L-aspartate
-
pH 7.5, isoenzyme I and II
2.1
L-aspartate
-
pH 7.5, 60°C, mutant L148A
2.1
L-aspartate
-
aspartokinase II, 27°C
2.3
L-aspartate
-
20 mM ATP, presence of alanine
2.31
L-aspartate
-
pH 8.0, 30°C, mutant T359I
2.33
L-aspartate
-
mutant E279A
2.35
L-aspartate
-
pH 7.5, 30°C
2.37
L-aspartate
-
mutant enzyme Y198N/D201M, at pH 7.5 and 25°C
2.6
L-aspartate
-
pH 8.0, 55°C, in presence of inhibitor
2.6
L-aspartate
-
20 mM ATP, absence of alanine
2.73
L-aspartate
-
pH 8.0, 30°C, wild-type
3
L-aspartate
-
aspartokinase I
3.06
L-aspartate
-
pH 8.0, 30°C, mutant E257K
3.1
L-aspartate
-
pH 8.0, 30°C, mutant E257K/T359I
3.19
L-aspartate
-
mutant T295V
3.21
L-aspartate
-
mutant K18A
3.25
L-aspartate
-
mutant R419A
3.58
L-aspartate
-
wild type enzyme, at pH 7.5 and 25°C
3.66
L-aspartate
-
mutant enzyme A380I, at pH 8.0 and 28°C
3.67
L-aspartate
-
mutant enzyme T379L, at pH 8.0 and 26°C
4.17
L-aspartate
-
wild type enzyme, at pH 8.0 and 26°C
4.17
L-aspartate
-
wild type enzyme, at pH 8.0 and 28°C
4.25
L-aspartate
-
mutant K18Q
4.59
L-aspartate
-
wild type
4.66
L-aspartate
at pH 7.0 and 55°C
4.66
L-aspartate
recombinant enzyme, pH 7.5, 55°C
4.7
L-aspartate
-
aspartokinase III, 27°C
5
L-aspartate
-
pH 8.0, 55°C
5.29
L-aspartate
-
pH 7.5, 60°C, mutant F136A
5.5
L-aspartate
-
pH 8.1, 29°C
5.77
L-aspartate
-
mutant enzyme M372I/T379W, at pH 7.4 and 28°C
6.15
L-aspartate
-
20 mM ATP, absence of alanine
6.18
L-aspartate
-
wild type enzyme, at pH 7.4 and 28°C
6.81
L-aspartate
-
mutant H292A
6.99
L-aspartate
-
mutant S23A
7.08
L-aspartate
-
mutant T22A
8.66
L-aspartate
-
mutant H497A
9.77
L-aspartate
-
mutant E254A
10
L-aspartate
-
wild type
11.3
L-aspartate
-
mutant hom3-S45
11.6
L-aspartate
pH 8.0, 30°C
11.9
L-aspartate
-
mutant H292Q
12.4
L-aspartate
-
mutant hom3-S49
16.7
L-aspartate
-
pH 7.8, 27°C
17
L-aspartate
-
aspartokinase II
19.5
L-aspartate
-
pH 7.5, 60°C, mutant T47A
21
L-aspartate
-
pH 7.0, 30°C
21.6
L-aspartate
-
pH 8.0, 30°C
26.4
L-aspartate
pH 8.0, 30°C, 0.5 M effector threonine
29.7
L-aspartate
-
pH 8.0, 30°C
50.1
L-aspartate
wild-type
1.8
L-aspartic acid
mutant M68V, recombinant enzyme purified to homogeneity
50.1
L-aspartic acid
wild-type, recombinant enzyme purified to homogeneity
additional information
additional information
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at 37°C, but not at 25°C, the apparent Km for L-aspartate is highly dependent on enzyme concentration, increasing from 0.4 mM to about 50 mM. As the enzyme concentration decreases from 13.4 to 0.17 units per ml, the presence of dioxane increases apparent Km for L-aspartate
-
additional information
additional information
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Km for MgCl2 3.3 mM
-
additional information
additional information
steady-state kinetics analysis of wild-type and mutant enzymes, overview
-
additional information
additional information
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steady-state kinetics analysis of wild-type and mutant enzymes, overview
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113000
-
gel filtration, native PAGE, isoenzyme AK Late
115000
-
aspartokinase II, equilibrium sedimentation
116000
-
equilibrium ultracentrifugation
122000
-
2 * 122000, ultracentrifugation in TES or HEPES buffer
122400
-
alpha2, beta2, calculated from nucleotide sequence
124400
-
alpha2, beta2, calculated from nucleotide sequence
125000
-
aspartokinase II
127000
-
aspartokinase III, sedimentation equilibrium
133000
-
sedimentation velocity centrifugation
140000
gel filtration, homodimer
150000
-
sucrose density gradient centrifugation, peak 2
154000
dynamic light-scattering, crystallization
166000
-
in presence of KCl and L-lysine at 11°C, sedimentation equilibrium
167000
-
first AK isoenzyme, gel filtration
169000
-
aspartokinase II, equilibrium sedimentation
17700
aspartate kinase beta, calculated from amino acid sequence
180000 - 200000
-
aspartokinase devoid of homoserine dehydrogenase activity in presence of threonine, gel filtration
181000
-
in presence of KCl and L-lysine at 25°C, sedimentation equilibrium
18145
-
1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
18500
-
beta subunit, calculated from nucleotide sequence
200000
-
isoenzyme II, gel filtration
20200
AKbeta analytical ultracentrifugation, absence of threonine
21700
aspartate kinase beta, gel filtration
230000
-
sucrose density gradient centrifugation, peak 3
240000
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calculated from Stokes' radius
246000
-
gel filtration, Superose 6
253000
-
gel filtration, non-denaturing electrophoresis, 4-20% polyacrylamide gradient gels
258000
-
gel filtration, Superose 12
297000
-
glutathione-S-transferase fusion protein, in the presence of threonine, blue native gel electrophoresis
298000
-
wild type, in the presence of threonine, gel filtration
320000
gel filtration, in presence of 5.0 mM L-threonine
330000
-
isoenzyme I, gel filtration
33300
AKbeta gel-filtration chromatography, addition of threonine induces dimerization
334000
-
native complex, Svedberg equation
33800
AKbeta in presence with 5 mM L-threonine, gel filtration
358000
-
light scattering studies
36000
AKbeta analytical ultracentrifugation, presence of threonine
360000
-
equilibrium sedimentation
40000
-
6 * 40000, SDS-PAGE
42000
-
SDS-PAGE, recombinant protein
43200
-
alpha subunit, calculated from nucleotide sequence
43700
-
alpha subunit, calculated from nucleotide sequence
44000
-
SDS-PAGE, recombinant protein
44108
-
1 * 44108 + 1 * 18145, ask alpha and ask beta, SDS-PAGE
44300
-
calculated from cDNA
45000
-
1 * 18000 + 1 * 45000, Western blot immunoanalysis
48000
-
4 * 48000, SDS-PAGE
49000
-
2 * 49000 + 2 * 60000, SDS-PAGE
52400
-
calculated from cDNA
53000
-
1 * 17000 + 1 * 53000, urea treatment, SDS-PAGE
58100
-
wild type, calculated from protein sequence
58700
-
wild type, SDS-PAGE
61200
-
alphabeta, calculated from nucleotide sequence
62200
-
alphabeta, calculated from nucleotide sequence
66000
-
4 * 66000, ultracentrifugation
79000
-
second AK isoenzyme, gel filtration
80000
-
4 * 80000, aspartokinase-homoserine dehydrogenase complex, sedimentation equlibrium performed on guanidinium chloride dissolved complex
83000
dynamic light-scattering, addition of increasing levels of guanidine-HCl up to 2000 mM causes a decrease in the AK particle size, dissociation into dimers
84000
-
4 * 84000, SDS-PAGE
87500
-
4 * 87500, SDS-PAGE
88000
-
4 * 88000, gel filtration in 6.0 mM guanidinium chloride
90300
-
alpha2, beta2, gel filtration
93000
? * 93000, SDS-PAGE
100000
-
gel filtration
100000
-
sucrose density gradient centrifugation, peak 1
110000
-
-
121400
-
alpha2, beta2, calculated from nucleotide sequence
121400
-
alpha2, beta2, calculated from nucleotide sequence
17000
-
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE
17000
-
1 * 17000 + 1 * 43000, SDS-PAGE
17000
-
1 * 17000 + 1 * 53000, urea treatment, SDS-PAGE
17000
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE
17000
-
2 * 17000 + 2 * 47000, SDS-PAGE
17720
full-length beta subunit (Met1Ala161) with a His6-tag extension at the C-terminal end, calculated
17720
beta subunit (Met1-Ala161), calculated from nucleotide sequence
18000
-
18000
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beta subunit, calculated from nucleotide sequence
18000
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SDS-PAGE, recombinant protein, beta-subunit (amino acids 248-255)
18000
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1 * 18000 + 1 * 45000, Western blot immunoanalysis
18000
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alpha2, beta2, 2 * 42700 + 2 * 18000, gel filtration, ultracentrifugation, calculated from nucleotide sequence
23000
AKbeta, gel filtration
23000
AKbeta gel-filtration chromatography, absence of additives, somewhat larger than the mass of a monomer, addition of lysine causes no change
280000
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gel filtration
280000
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glutathione-S-transferase fusion protein, in the presence of threonine, gel filtration
344000
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glutathione-S-transferase fusion protein, gel filtration
344000
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threonine insensitive mutant, with and without threonine in the buffer, blue native gel electrophoresis
345000
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threonine insensitive mutant, with and without threonine in the buffer, gel filtration
345000
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wild type, blue native gel electrophoresis, gel filtration
346000
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wild type, gel filtration
346000
-
aspartokinase-homoserine dehydrogenase complex, sedimentation equilibrium
346000
-
glutathione-S-transferase fusion protein, blue native gel electrophoresis
42700
-
alpha subunit, calculated from nucleotide sequence
42700
-
alpha subunit, calculated from nucleotide sequence
43000
-
3 * 43000, SDS-PAGE
43000
-
1 * 17000 + 1 * 43000, alpha and beta subunits, SDS-PAGE
43000
-
1 * 17000 + 1 * 43000, SDS-PAGE
43000
-
2 * 17000 +2 * 43000, catalytic centre as well as the 3 types of allosteric sites reside on the alpha subunit, beta subunit may function during the folding or maturation of the enzyme, SDS-PAGE
43000
-
4 * 43000, aspartokinase II, equilibrium sedimentation
43900
-
alpha subunit, calculated from nucleotide sequence
43900
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alpha subunit, calculated from nucleotide sequence
450000
gel filtration
450000
about, recombinant enzyme, gel filtration
47000
-
47000
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2 * 17000 + 2 * 47000, SDS-PAGE
470000
gel filtration
50000
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SDS-PAGE, recombinant protein
50000
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recombinant protein, expressed in E. coli, gel filtration
53200
gel filtration
53200
monofunctional AK2, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
55100
gel filtration
55100
monofunctional AK3, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
55900
gel filtration
55900
monofunctional AK1, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
58000
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wild type, gel filtration
58000
dynamic light-scattering, addition up to 4000 mM guanidine-HCl leads to dissociation of the AK dimers into monomers
60000
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2 * 49000 + 2 * 60000, SDS-PAGE
60000
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? * 60000, high-speed sedimentation equilibrium in 6.0 mM guanidinium chloride
60700
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alphabeta, calculated from nucleotide sequence
60700
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alphabeta, calculated from nucleotide sequence
64200
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alpha2, gel filtration
64200
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alpha2, gel filtration
87800
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alpha2, calculated from nucleotide sequence
87800
-
alpha2, calculated from nucleotide sequence
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I441A
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site-directed mutagenesis
I552A
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site-directed mutagenesis
Q443A
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site-directed mutagenesis
Q524A
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site-directed mutagenesis
S2207A
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phenotype Thr- Met- Ura-
S2207A/pM1-1
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mutant S2207A complemented with plasmid pM1-1, phenotype Thr+ Met+ Ura+
A279T
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isolated from Corynebacterium glutamicum strain IWJ001, aspartate kinase mutant AKA279T is encoded by gene lysC1. The mutant enzymes is completely resistant to feed-back inhibition by L-threonine and L-lysine
D45A
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the inhibition of CgAK by lysine is substantially reduced in D45A mutant
G110A
mutant enzyme shows normal and negligible response to Thr and Lys, dimerized by Thr
K106A
mutant showing change in Lys response
M105A
mutant showing change in Lys response
N50A
mutant showing change in Lys response
S301F
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the S301F mutant exhibits resistance to feedback inhibition by lysine and threonine, showing activity in the presence of both lysine and threonine
V51A
mutant showing change in Lys response
A279T
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isolated from Corynebacterium glutamicum strain IWJ001, aspartate kinase mutant AKA279T is encoded by gene lysC1. The mutant enzymes is completely resistant to feed-back inhibition by L-threonine and L-lysine
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A380I
-
the mutant has 11.32fold higher enzyme activity than the wild type enzyme, enhanced thermal stability and shows weakened inhibition with L-lysine
M372I/T379W
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the mutant shows 16.51fold higher activity, weakened inhibitory effect of L-lysine and significantly improved thermostability as compared to the wild type enzyme
R169A
site-directed mutagenesis, the Km for aspartate is decreased compared to the wild-type enzyme
R169D
site-directed mutagenesis, the mutant shows 2.57fold higher catalytic activity with aspartate than the wild-type enzyme
R169H
site-directed mutagenesis, the mutant shows 2.13fold higher catalytic activity with aspartate than the wild-type enzyme
R169P
site-directed mutagenesis, the mutant shows 2.25fold higher catalytic activity with aspartate than the wild-type enzyme
R169Y
site-directed mutagenesis, the mutant shows 4.7fold higher catalytic activity with aspartate than the wild-type enzyme. The three-dimensional structure of R169Y is more stable than that of the wild-type
T379 F
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the mutant shows 2.65fold higher enzymatic activity compared to the wild type enzyme
T379E
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the mutant shows 4.66fold higher enzymatic activity compared to the wild type enzyme
T379K
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the mutant shows 5.25fold higher enzymatic activity compared to the wild type enzyme
T379L
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the mutant shows 9.16fold higher enzymatic activity compared to the wild type enzyme
Y198N/D201M
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the mutant shows 18.26fold increased activity compared to the wild type enzyme, is less inhibited by L-lysine and L-threonine and activated by Lys + Met, Thr + Met, Lys + Thr + Met at 5 and 10 mM concentration
M372I/T379W
-
the mutant shows 16.51fold higher activity, weakened inhibitory effect of L-lysine and significantly improved thermostability as compared to the wild type enzyme
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C428R
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
E346A
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mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
E346R
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
F329R
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
G323D
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
G433R
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased homoserine dehydrogenase activity (62.4% of the maximum theoretical yield)
H320A
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mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
I337P
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mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
I344P
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mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
I427P
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mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
L325F
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mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
M251P
-
mutation destroys van der Waals interaction significantly which releases L-lysine inhibition
M417I
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
N424A
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mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
N426A
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mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
P458S
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased homoserine dehydrogenase activity (62.4% of the maximum theoretical yield)
Q351A
-
mutation reduces feedback-inhibition of AK1 by L-threonine without significant change in enzymatic activity
R305A
-
mutation destroys van der Waals interaction significantly which releases L-lysine inhibition
R416A
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
S315A
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
S338L
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
S345L
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
T253R
-
mutation leads to repulse interaction with Arg305 which destroys the allosteric regulation by L-lysine
T352I
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
V339A
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
V347M
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
V349M
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
M318I
-
mutant enzyme T344M is more conducive to L-lysine production than mutant M318I
-
T344M
-
mutant enzyme T344M is more conducive to L-lysine production than mutant M318I
-
G433R
-
site-directed mutagenesis, strain HS33/pACYC-pycP458S-thrAG433R-lysC shows increased homoserine dehydrogenase activity (62.4% of the maximum theoretical yield)
-
S449L
transgenic plants expressing the mutant enzyme show a 6.6fold increased free lysine content
T448M
transgenic plants expressing the mutant enzyme show about 2fold increased free lysine content
D182/R184A
the mutations decrease the enzyme activities to about 65%
G152L
the mutant shows about 35% activity compared to the wild type enzyme
H399A
the mutant shows wild type activity
N371A/I372A
the mutations do not affect the ATP binding with threonine
R150A
the mutant shows about 30% activity compared to the wild type enzyme
S12C/S231C
the mutant shows wild type activity
V357/M351A
the mutant shows reduced activity compared to the wild type enzyme
A406T
-
site-directed mutagenesis, 30fold more strongly inhibited by threonine
D34E
wild type background
E254A
-
9.1fold decrease in kcat for aspartate and 11fold decrease in kcat for ATP
E279A
-
kcat is decreased 47 times for aspartate and 44 times for ATP
G25D
-
site-directed mutagenesis, reduced affinity for its substrates aspartate and ATP
H292A
-
4.5 times increase in Km for ATP and 120 times decrease in kcat for ATP
H292Q
-
no significant differences to wild type
H497A
-
kcat is decreased 6.7fold for both substrates
K18A
-
Km values for both substrates similar to wild type
K18Q
-
Km values for both substrates similar to wild type
K18R
-
Km values for aspartate similar to wildtype, Km value for ATP 2.9fold decreased
K26I
-
site-directed mutagenesis, reduced affinity for its substrates aspartate and ATP
R419A
-
10fold decrease in kcat for aspartate and 8.9fold decrease in kcat for ATP
S23A
-
differs significantly only in the kcat/Km ratio, which is decreased 4fold for aspartate and 3.7fold for ATP
T22A
-
Km for ATP increases 4.2fold
T295V
-
6.7 times decrease in the kcat/Km ratio for ATP
I119V/M68V/T309
random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, the mutations remove the regulation from the Ask wild type enzyme and conferre a feedback-inhibition resistance
I19V/M68V/T309A
removes regulation from the Ask wild type enzyme and conferrs a feedback-inhibition resistance, assay mixture with 100 mM L-lysine plus 100 mM L-threonine reveals more than 80% activity
I119V/M68V/T309
-
random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, the mutations remove the regulation from the Ask wild type enzyme and conferre a feedback-inhibition resistance
-
I19V/M68V/T309A
-
removes regulation from the Ask wild type enzyme and conferrs a feedback-inhibition resistance, assay mixture with 100 mM L-lysine plus 100 mM L-threonine reveals more than 80% activity
-
A157L
-
site-directed mutagenesis
A189L
-
site-directed mutagenesis
A23L
-
site-directed mutagenesis
A42S
-
site-directed mutagenesis
D154A
-
site-directed mutagenesis
D154N
-
site-directed mutagenesis
D174A
-
site-directed mutagenesis
D182A
-
site-directed mutagenesis
E202A
-
site-directed mutagenesis
F136A
-
site-directed mutagenesis
G10A
-
site-directed mutagenesis
G10D/G324W
construction of an engineered chimeric mutant enzyme containing the N-terminal catalytic region from Bacillus subtilis AKII and the C-terminal region from Thermus thermophilus AKII, through random mutagenesis and then screened using a high throughput synthetic RNA device which comprises of an L-lysine-sensing riboswitch and a selection module. Of three evolved aspartate kinases, the best mutant BT3 shows 160% increased in vitro activity compared to the wild-type enzyme from Bacillus subtilis. The mutant enzymes is feedback-resistant to L-lysine
G135A
-
site-directed mutagenesis
G149A
-
site-directed mutagenesis
G152A
-
site-directed mutagenesis
G177A
-
site-directed mutagenesis
G73A
-
site-directed mutagenesis
I171A
-
site-directed mutagenesis
L148A
-
site-directed mutagenesis
P183A
-
site-directed mutagenesis
R150A
-
site-directed mutagenesis
S12A
-
site-directed mutagenesis
S153A
-
site-directed mutagenesis
S41A
-
site-directed mutagenesis
T238A
-
site-directed mutagenesis
T47A
-
site-directed mutagenesis
V39A
-
site-directed mutagenesis
Y8A
-
site-directed mutagenesis
E257K
-
mutation of the conserved Glu-257 to Lys or the double mutations T359I/E257K render the enzyme insensitive to L-lysine with 86- and 112fold increases in IC50 values, respectively, when compared to the wild-type enzyme. E257K and E257K/T359I alleles exhibit a 1.2- to 1.7fold decrease in Vmax value and 2- to 6fold decrease in kcat/Km value for either substrate compared to wild-type
T359I
-
mutation increases the L-lysine IC50 value by 104fold, but no substantial differences are observed in kinetic parameters except lower Km ATP value compared to the wild-type enzyme. Seed-specific expression of the feedback-resistant mutant T359I or mutant E257K results in increases of free L-threonine levels of up to 100fold in R1 soybean seed when compared to wild-type
T359I/E257K
-
mutation of the conserved Glu-257 to Lys or the double mutations T359I/E257K render the enzyme insensitive to L-lysine with 86- and 112fold increases in IC50 values, respectively, when compared to the wild-type enzyme. E257K and E257K/T359I alleles exhibit a 1.2- to 1.7fold decrease in Vmax value and 2- to 6fold decrease in kcat/Km value for either substrate compared to wild-type
G10D/G324W
construction of an engineered chimeric mutant enzyme containing the N-terminal catalytic region from Bacillus subtilis AKII and the C-terminal region from Thermus thermophilus AKII, through random mutagenesis and then screened using a high throughput synthetic RNA device which comprises of an L-lysine-sensing riboswitch and a selection module. Of three evolved aspartate kinases, the best mutant BT3 shows 160% increased in vitro activity compared to the wild-type enzyme from Bacillus subtilis. The mutant enzymes is feedback-resistant to L-lysine
G10D/G324W
-
construction of an engineered chimeric mutant enzyme containing the N-terminal catalytic region from Bacillus subtilis AKII and the C-terminal region from Thermus thermophilus AKII, through random mutagenesis and then screened using a high throughput synthetic RNA device which comprises of an L-lysine-sensing riboswitch and a selection module. Of three evolved aspartate kinases, the best mutant BT3 shows 160% increased in vitro activity compared to the wild-type enzyme from Bacillus subtilis. The mutant enzymes is feedback-resistant to L-lysine
-
G345D
-
mutation in the beta-subunit of the ask gene
G345D
-
mutation in the beta-subunit of the ask gene
-
E114A
changes in the inhibitory profile upon addition of Thr, monomer even with the addition of Thr
E114A
changes in the inhibitory profile upon addition of threonine, monomer even with the addition of Thr
F115A
changes in the inhibitory profile upon addition of Thr, pentamer or hexamer in the presence and in the absence of Thr
F115A
changes in the inhibitory profile upon addition of threonine, pentamer or hexamer in the presence and in the absence of Thr
G28A
changes in the inhibitory profile upon addition of Thr
G28A
changes in the inhibitory profile upon addition of threonine
Q49A
changes in the inhibitory profile upon addition of Thr, monomer even with the addition of Thr
Q49A
changes in the inhibitory profile upon addition of threonine, monomer even with the addition of Thr
T112A
changes in the inhibitory profile upon addition of Thr, monomer even with the addition of Thr
T112A
changes in the inhibitory profile upon addition of threonine, monomer even with the addition of Thr
V111A
changes in the inhibitory profile upon addition of Thr, pentamer or hexamer in the presence and in the absence of Thr
V111A
changes in the inhibitory profile upon addition of threonine, pentamer or hexamer in the presence and in the absence of Thr
DR1365
disruption mutant does not grow in the minimal medium, Deinococcus radiodurans uses DR1365 for biosyntheses of methionine and threonine, but does not use it for lysine biosynthesis, the growth rate is lower than that of the wild type
DR1365
-
disruption mutant does not grow in the minimal medium, Deinococcus radiodurans uses DR1365 for biosyntheses of methionine and threonine, but does not use it for lysine biosynthesis, the growth rate is lower than that of the wild type
-
M318I
-
mutation within L-lysine binding site desensitizes AK3 from L-lysine inhibition. Mutant shows reduced L-lysine inhibition
M318I
mutant enzyme T344M is more conducive to L-lysine production than mutant M318I
T344M
-
mutation is not directly involved in L-lysine binding. Mutation located within regulatory domain, participates in the allosteric regulation within regulatory domain. Mutation greatly reduces L-lysine inhibition
T344M
mutant enzyme T344M is more conducive to L-lysine production than mutant M318I
S378A/E202A
the mutant shows slightly increased activity (about 108%) compared to the wild type enzyme
S378A/E202A
the mutations do not affect the ATP binding with threonine
M68V
is almost fully resistant to feedback inhibition, increase in the catalytic activity, homologous expression reveals increase in varepsilon-poly-lysine productivity
M68V
random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, fully resistant to feedback inhibition, increase in epsilon-poly-L-lysine productivity
M68V
-
is almost fully resistant to feedback inhibition, increase in the catalytic activity, homologous expression reveals increase in varepsilon-poly-lysine productivity
-
M68V
-
random mutagenesis by error-prone PCR and subsequent site-directed mutagenesis, fully resistant to feedback inhibition, increase in epsilon-poly-L-lysine productivity
-
additional information
generation of ak-hsdh1 mutants, and double mutants from ak-hsdh1 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age. A Thr increase is observed in mutant ak-hsdh1-1, it also has an increased Met content, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh1 mutants, and double mutants from ak-hsdh1 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age. A Thr increase is observed in mutant ak-hsdh1-1, it also has an increased Met content, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh1 mutants, and double mutants from ak-hsdh1 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age. A Thr increase is observed in mutant ak-hsdh1-1, it also has an increased Met content, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh1 mutants, and double mutants from ak-hsdh1 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age. A Thr increase is observed in mutant ak-hsdh1-1, it also has an increased Met content, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh1 mutants, and double mutants from ak-hsdh1 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age. A Thr increase is observed in mutant ak-hsdh1-1, it also has an increased Met content, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh2 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 and ak-hsdh2-1/ak2-1 double mutants. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh2 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 and ak-hsdh2-1/ak2-1 double mutants. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh2 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 and ak-hsdh2-1/ak2-1 double mutants. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh2 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 and ak-hsdh2-1/ak2-1 double mutants. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak-hsdh2 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants that are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 and ak-hsdh2-1/ak2-1 double mutants. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak1 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 double mutant. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak1 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 double mutant. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak1 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 double mutant. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak1 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 double mutant. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak1 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak1-1 double mutant. In the ak-hsdh2-1/ak1-1 double mutant, both AK1 and AK-HSDH2 transcripts are completely abolished, and there is a 64% decrease in total AK-HSDH transcripts. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak2 mutants, and double mutants from ak-hsdh2 and ak2 genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak2-1 double mutant. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak2 mutants, and double mutants from ak-hsdh2 and ak2 genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak2-1 double mutant. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak2 mutants, and double mutants from ak-hsdh2 and ak2 genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak2-1 double mutant. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak2 mutants, and double mutants from ak-hsdh2 and ak2 genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak2-1 double mutant. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak2 mutants, and double mutants from ak-hsdh2 and ak2 genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutant are not observed in the double mutants at the same age, only ak-hsdh2-1/ak2-1 has an increased Asp content. The Thr increase observed in mutants ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 single mutants is absent in ak-hsdh2-1/ak2-1 double mutant. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. Simultaneous loss of AK-HSDH2 and monofunctional AK1 or AK2 has an additive effect on the reduction of overall AK activity. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak3 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants are not observed in the double mutants at the same age. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak3 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants are not observed in the double mutants at the same age. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak3 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants are not observed in the double mutants at the same age. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak3 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants are not observed in the double mutants at the same age. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
generation of ak3 mutants, and double mutants from ak-hsdh2 and ak genes. Near-unanimous increases of Asp, Lys, and Ile in the single mutants are not observed in the double mutants at the same age. The ak-hsdh2-1/ak3-1 double mutant still has a high amount of Thr (280% higher than the wild type), and all three double mutants have increased Met contents, overview. The contents of Asp, Lys, and Met in ak1-1, ak2-1, ak3-1, ak-hsdh1-1, ak-hsdh2-1, and ak-hsdh2-2 are significantly higher than those in the wild-type. Increases of Asp, Lys, and Met in ak-hsdh2 are also observed in mutants ak1-1, ak2-1, ak3-1, and ak-hsdh1-1. The Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Transcript levels of AK and AK-HSDH genes in leaves of 4-week-old engineered plants, mutant plant phenotypes, overview
additional information
site-directed mutagenesis is used to construct a mutant of the region coding for regulatory beta-subunit in the aspartate kinase by replacing the codon TCC-GTC to deregulate it from feedback inhibition, which results in improved L-lysine production. The mutant enzymes are resistant against S-(2-aminoethyl)-L-cysteine and feedback inhibition, phenotype, overview
additional information
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site-directed mutagenesis is used to construct a mutant of the region coding for regulatory beta-subunit in the aspartate kinase by replacing the codon TCC-GTC to deregulate it from feedback inhibition, which results in improved L-lysine production. The mutant enzymes are resistant against S-(2-aminoethyl)-L-cysteine and feedback inhibition, phenotype, overview
-
additional information
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AK DR1365 disruption mutant, does not grow in minimal medium, growth rate in minimal medium supplemented with methionine and threonine is identical to that supplemented with methionine, threonine and lysine, this phenotype is similar to a Thermus thermophilus AK TTC0166 disprution mutant
additional information
AK DR1365 disruption mutant, does not grow in minimal medium, growth rate in minimal medium supplemented with methionine and threonine is identical to that supplemented with methionine, threonine and lysine, this phenotype is similar to a Thermus thermophilus AK TTC0166 disprution mutant
additional information
-
AK DR1365 disruption mutant, does not grow in minimal medium, growth rate in minimal medium supplemented with methionine and threonine is identical to that supplemented with methionine, threonine and lysine, this phenotype is similar to a Thermus thermophilus AK TTC0166 disprution mutant
-
additional information
key metabolic pathway for construction of an inducer-free L-homoserine-producing strain to maximize the productivity of L-homoserine based on genetic-engineering tools, comparison of L-homoserine production, cell growth, and glucose consumption in different engineered strains, overview. L-Homoserine is a nonessential amino acid for the biosynthesis of L-threonine and L-methionine. It is also an important precursor for the production of isobutanol, 1,4-butanediol, L-phosphinothricin, 2,4-ihydroxybutyrate, and 1,3-propanediol. The initial L-homoserine-producing strain HS1 is obtained by blocking the degradative and competitive pathways and overexpressing thrA (encoding homoserine dehydrogenase) based on an O-succinyl homoserine-producing strain, using the pull-push-block strategy, an efficient method to engineer microorganisms involved in biosynthesizing target products by modifying metabolic networks. L-homoserine-converting pathway-related genes (thrB, encoding homoserine kinase, and metA, encoding homoserine O-succinyltransferase) are successively deleted to block L-homoserine degradation. Gene thrAis overexpressed to push the carbon flux to L-homoserine production. Then, the lysine-auxotrophic strain HS2 is generated by deleting lysA to eliminate a precursor competing metabolic pathway on L-homoserine production. For strengthening the capability of the L-homoserine transport system and the transformation of other toxic intermediate metabolites, gene rhtA, encoding the inner membrane transporter that is involved in the export of L-homoserine, is overexpressed chromosomally by replacing the native promoter with the trc promoter to obtain strain HS3 (Trc-rhtA). The strain shows increased activity. Increase in the L-homoserine export capacity and relieve the growth burden of homoserine-producing strains to enable survival via replacement of the native promoter of the eamA gene by the trc promoter in strain HS4 (Trc-eamA). Two rhtA gene copies (the native rhtA gene and replacement of the lacI gene) and eamA are overexpressed under the trc promoter in the chromosome to construct strain HS5 (DELTAlacI::Trc-rhtA Trc-rhtA Trc-eamA). Under batch culture, strain HS5, with modification of the transport system and construction of a constitutive expression system, can produce 3.14 g/l L-homoserine, which is 54.2% higher than strain HS2 production. In addition, the specific production of strain HS5 is also increased. Repression of candidate genes by the CRISPRi system to further enhance L-homoserine production
additional information
-
key metabolic pathway for construction of an inducer-free L-homoserine-producing strain to maximize the productivity of L-homoserine based on genetic-engineering tools, comparison of L-homoserine production, cell growth, and glucose consumption in different engineered strains, overview. L-Homoserine is a nonessential amino acid for the biosynthesis of L-threonine and L-methionine. It is also an important precursor for the production of isobutanol, 1,4-butanediol, L-phosphinothricin, 2,4-ihydroxybutyrate, and 1,3-propanediol. The initial L-homoserine-producing strain HS1 is obtained by blocking the degradative and competitive pathways and overexpressing thrA (encoding homoserine dehydrogenase) based on an O-succinyl homoserine-producing strain, using the pull-push-block strategy, an efficient method to engineer microorganisms involved in biosynthesizing target products by modifying metabolic networks. L-homoserine-converting pathway-related genes (thrB, encoding homoserine kinase, and metA, encoding homoserine O-succinyltransferase) are successively deleted to block L-homoserine degradation. Gene thrAis overexpressed to push the carbon flux to L-homoserine production. Then, the lysine-auxotrophic strain HS2 is generated by deleting lysA to eliminate a precursor competing metabolic pathway on L-homoserine production. For strengthening the capability of the L-homoserine transport system and the transformation of other toxic intermediate metabolites, gene rhtA, encoding the inner membrane transporter that is involved in the export of L-homoserine, is overexpressed chromosomally by replacing the native promoter with the trc promoter to obtain strain HS3 (Trc-rhtA). The strain shows increased activity. Increase in the L-homoserine export capacity and relieve the growth burden of homoserine-producing strains to enable survival via replacement of the native promoter of the eamA gene by the trc promoter in strain HS4 (Trc-eamA). Two rhtA gene copies (the native rhtA gene and replacement of the lacI gene) and eamA are overexpressed under the trc promoter in the chromosome to construct strain HS5 (DELTAlacI::Trc-rhtA Trc-rhtA Trc-eamA). Under batch culture, strain HS5, with modification of the transport system and construction of a constitutive expression system, can produce 3.14 g/l L-homoserine, which is 54.2% higher than strain HS2 production. In addition, the specific production of strain HS5 is also increased. Repression of candidate genes by the CRISPRi system to further enhance L-homoserine production
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Oryza sativa Japonica Group (Q5JK18)
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Corynebacterium pekinense, Corynebacterium pekinense ATCC 13032
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Corynebacterium pekinense
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