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Information on EC 2.7.2.4 - aspartate kinase and Organism(s) Arabidopsis thaliana and UniProt Accession Q9LYU8
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2.7.2.4 aspartate kinaseIUBMB Comments
The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction.
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Word Map
- 2.7.2.4
- corynebacterium
- glutamicum
-
threonine-sensitive
- l-lysine
- l-threonine
- dihydrodipicolinate
-
i-homoserine
- diaminopimelate
- semialdehyde
-
feedback-resistant
-
aspartate-derived
-
feedback-insensitive
- aec
- l-isoleucine
- s-2-aminoethyl-l-cysteine
-
lysine-producing
- flavum
- thialysine
- meso-diaminopimelate
- ectoine
- synthesis
- agriculture
- medicine
- nutrition
- food industry
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
aspartokinase, aspartate kinase, thra1, aspartokinase ii, aspartokinase iii, aspartokinase i, akiii, thra2, ak iii, ak ii, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
AK
aspartate kinase
aspartate kinase (phosphorylating)
-
-
-
-
aspartate kinase II
-
also acts as homoserine dehydrogenase (EC 1.1.1.3)
aspartic kinase
-
-
-
-
aspartokinase
-
-
-
-
beta-aspartokinase
-
-
-
-
AK
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
phospho group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
ATP:L-aspartate 4-phosphotransferase
The enzyme from Escherichia coli is a multifunctional protein, which also catalyses the reaction of EC 1.1.1.3 homoserine dehydrogenase. This is also the case for two of the four isoenzymes in Arabidopsis thaliana. The equilibrium constant strongly favours the reaction from right to left, i.e. the non-physiological direction of reaction.
CAS REGISTRY NUMBER
COMMENTARY
9012-50-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
first and third step of the synthesis of methionine, catalyzed by a bifunctional enzyme
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
first and third step of the synthesis of methionine, catalyzed by a bifunctional enzyme
-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
L-lysine
AK1 is inhibited in a synergistic manner by lysine and SAM
L-lysine
AK2 is inhibited by lysine, SAM by itself has no effect on the enzyme activity
L-lysine
AK3 is inhibited only by lysine, SAM by itself has no effect on the enzyme activity
L-threonine
-
inhibition at 0.5-1.0 mM in complemented S2207A cells is variable, it does not exceed 67%
additional information
-
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM 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
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 100 microM Lys and 20 microM 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
-
additional information
-
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
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
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
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 5 microM Lys for AK2
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK2
-
additional information
-
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3
-
additional information
no additional inhibition is observed upon addition of Thr or Leu in the presence of 5 microM Lys for AK3
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
1.095
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
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
0.98
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
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
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. Mutant plant phenotypes, overview
physiological function
biosynthesis of aspartate-derived amino acids lysine, methionine, threonine, and isoleucine involves monofunctional Asp kinases and dual-functional Asp kinase-homoserine dehydrogenases (AK-HSDHs). Isozymes AK2 and AK-HSDH1 are the major contributors to overall AK and HSDH activities, respectively
malfunction
physiological function
biosynthesis of aspartate-derived amino acids lysine, methionine, threonine, and isoleucine involves monofunctional Asp kinases and dual-functional Asp kinase-homoserine dehydrogenases (AK-HSDHs). Isozymes AK2 and AK-HSDH1 are the major contributors to overall AK and HSDH activities, respectively
malfunction
four-week-old loss-of-function Arabidopsis thaliana mutants in the AK-HSDH2 gene have increased amounts of Asp and Asp-derived amino acids, especially Thr, in leaves, phenotype, 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. However, the Thr increase in ak-hsdh2 is observed in ak-hsdh1-1 but not in ak1-1, ak2-1, or ak3-1. Mutant plant phenotypes, overview
malfunction
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. Mutant plant phenotypes, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). AK1_ARATH
569
0
62298
Swiss-Prot
Chloroplast (Reliability: 5)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
55900
470000
53200
55100
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
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
monofunctional AK3, proteins are separated on a 10% polyacrylamide (w/v) slab gel under denaturing conditions and stained with Coomassie brilliant blue R-250
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S2207A/pM1-1
-
mutant S2207A complemented with plasmid pM1-1, phenotype Thr+ Met+ Ura+
additional information
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 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 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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h. During this period of time, AK1 and AK2 retained all their activity
additional information
additional information
-
AK1 retaines all activity when stored at room temperature
additional information
AK1 retaines all activity when stored at room temperature
additional information
AK1 retaines all activity when stored at room temperature
additional information
AK1 retaines all activity when stored at room temperature
additional information
-
AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
AK3 is highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
-
AK2 retaines all activity when stored at room temperature
additional information
AK2 retaines all activity when stored at room temperature
additional information
AK2 retaines all activity when stored at room temperature
additional information
AK2 retaines all activity when stored at room temperature
additional information
-
AK3 proves to be highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
AK3 proves to be highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
AK3 proves to be highly unstable when stored at room temperature, losing 95% of its activity in 24 h
additional information
AK3 proves to be highly unstable when stored at room temperature, losing 95% of its activity in 24 h
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
pure protein , quickly frozen in N2 can be stored at -80°C for several months without any loss of activity
-
pure protein, quickly frozen in N2 can be stored at -80°C for several months without any loss of activity
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, HEPES buffer, pH 7.5, 1 mM Lys, 10% (v/v) glycerol, several month, without any loss of activity
-80°C, HEPES buffer, pH 7.5, 1 mm Lys, 10% (v/v) glycerol, several months
-80°C, HEPES buffer, pH 7.5, 1 mM Lys, 10% (v/v) glycerol, several month, without any loss of activity
-80°C, HEPES buffer, pH 7.5, 1 mm Lys, 10% (v/v) glycerol, several months
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
weak anion exchange chromatography, affinity chromatogrphy for AK1
weak anion exchange chromatography, gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+
ligated into pET 23d(+) vector, expressed in Escherichia coli BL21 codon (+)
by functional complementation of a Saccharomyces cerevisiae strain mutated in its homoserine dehydrogenase gene (hom6), expression in Escherichia coli, two of the three isolated clones are also able to complement a mutant yeast aspartate kinase gene (hom3), expression of the AK-HSDH gene in Arabidopsis thaliana (meristematic cells, leaves and stamens)
-
cDNA located on chromosome 4, cloned in Escherichia coli DH5alpha, overproduced in Escherichia coli BL21pLysS
ligated into pET 23d(+) vector and Escherichia coli strain DH10B for cloning, expression in Escherichia coli BL21 (DE3) pLysS codon+
ligated into pET 23d(+) vector, expressed in Escherichia coli BL21 codon (+)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
transcription of aspartate kinase genes is down-regulated under energy-depleted conditions formed by darkness and low sugar levels.The sugar-sensitive enhancer sequence of the AK/HSD1 promoter interacts with DPBF4 (Atb-ZIP12/EEL1) and ABI5 (AtbZIP39/DPBF1) in yeast one-hybrid system and in planta
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
enzyme does not exist in animals, good target for conception of new pesticides controlling weeds, fungi and bacteria
additional information
additional information
-
upon binding to the inactive AK1-Lys complex, S-adenosyl-L-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1-Lys-S-adenosyl-L-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-L-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1-Lys towards the inactive form, S-adenosyl-L-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-L-methionine binding
additional information
upon binding to the inactive AK1-Lys complex, S-adenosyl-L-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1-Lys-S-adenosyl-L-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-L-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1-Lys towards the inactive form, S-adenosyl-L-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-L-methionine binding
additional information
upon binding to the inactive AK1-Lys complex, S-adenosyl-L-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1-Lys-S-adenosyl-L-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-L-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1-Lys towards the inactive form, S-adenosyl-L-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-L-methionine binding
additional information
upon binding to the inactive AK1-Lys complex, S-adenosyl-L-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1-Lys-S-adenosyl-L-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-L-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1-Lys towards the inactive form, S-adenosyl-L-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-L-methionine binding
additional information
-
upon binding to the inactive AK1Lys complex, S-adenosyl-l-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1LysS-adenosyl-l-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-l-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1Lys towards the inactive form, S-adenosyl-l-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-l-methionine binding
additional information
upon binding to the inactive AK1Lys complex, S-adenosyl-l-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1LysS-adenosyl-l-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-l-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1Lys towards the inactive form, S-adenosyl-l-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-l-methionine binding
additional information
upon binding to the inactive AK1Lys complex, S-adenosyl-l-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1LysS-adenosyl-l-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-l-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1Lys towards the inactive form, S-adenosyl-l-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-l-methionine binding
additional information
upon binding to the inactive AK1Lys complex, S-adenosyl-l-methionine promotes a slow conformational transition leading to formation of a stable aspartate kinase 1LysS-adenosyl-l-methionine complex. Increase in AK1 apparent affinity for lysine in the presence of S-adenosyl-l-methionine results from the displacement of the unfavorable equilibrium between AK1 and aspartate kinase 1Lys towards the inactive form, S-adenosyl-l-methionine and Lys binding to AK1 is sequential, with Lys binding preceding S-adenosyl-l-methionine binding
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Heremans, B.; Jacobs, M.
A mutant of Arabidopsis thaliana (L.) Heynh. with modified control of aspartate kinase by threonine
Biochem. Genet.
35
139-153
1997
Arabidopsis thaliana
Paris, S.; Wessel, P.M.; Dumas, R.
Overproduction, purification, and characterization of recombinant bifunctional threonine-sensitive aspartate kinase-homoserine dehydrogenase from Arabidopsis thaliana
Protein Expr. Purif.
24
105-110
2002
Arabidopsis thaliana, Arabidopsis thaliana (O81852)
Paris, S.; Viemon, C.; Curien, G.; Dumas, R.
Mechanism of control of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase by threonine
J. Biol. Chem.
278
5361-5366
2003
Arabidopsis thaliana
Rognes, S.E.; Dewaele, E.; Aas, S.F.; Jacobs, M.; Frankard, V.
Transcriptional and biochemical regulation of a novel Arabidopsis thaliana bifunctional aspartate kinase-homoserine dehydrogenase gene isolated by functional complementation of a yeast hom6 mutant
Plant Mol. Biol.
51
281-294
2003
Arabidopsis thaliana
Curien, G.; Ravanel, S.; Robert, M.; Dumas, R.
Identification of six novel allosteric effectors of Arabidopsis thaliana aspartate kinase-homoserine dehydrogenase isoforms. Physiological context sets the specificity
J. Biol. Chem.
280
41178-41183
2005
Arabidopsis thaliana
Curien, G.; Laurencin, M.; Robert-Genthon, M.; Dumas, R.
Allosteric monofunctional aspartate kinases from Arabidopsis
FEBS J.
274
164-176
2007
Arabidopsis thaliana, Arabidopsis thaliana (O23653), Arabidopsis thaliana (Q9LYU8), Arabidopsis thaliana (Q9S702)
Ufaz, S.; Shukla, V.; Soloveichik, Y.; Golan, Y.; Breuer, F.; Koncz, Z.; Galili, G.; Koncz, C.; Zilberstein, A.
Transcriptional control of aspartate kinase expression during darkness and sugar depletion in Arabidopsis: involvement of bZIP transcription factors
Planta
233
1025-1040
2011
Arabidopsis thaliana
Clark, T.J.; Lu, Y.
Analysis of loss-of-function mutants in aspartate kinase and homoserine dehydrogenase genes points to complexity in the regulation of aspartate-derived amino acid contents
Plant Physiol.
168
1512-1526
2015
Arabidopsis thaliana (O23653), Arabidopsis thaliana (O81852), Arabidopsis thaliana (Q9LYU8), Arabidopsis thaliana (Q9S702), Arabidopsis thaliana (Q9SA18)
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