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Literature summary extracted from

  • Bareich, D.C.; Wright, G.D.
    Functionally important amino acids in Saccharomyces cerevisiae aspartate kinase (2003), Biochem. Biophys. Res. Commun., 311, 597-603.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.4 the gene is cloned into the NheI and BamHI restriction enzyme sites of the expression vector pET28 to create pET28+AKSc, expression in Escherichia coli Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.4 E254A 9.1fold decrease in kcat for aspartate and 11fold decrease in kcat for ATP Saccharomyces cerevisiae
2.7.2.4 E279A kcat is decreased 47 times for aspartate and 44 times for ATP Saccharomyces cerevisiae
2.7.2.4 H292A 4.5 times increase in Km for ATP and 120 times decrease in kcat for ATP Saccharomyces cerevisiae
2.7.2.4 H292Q no significant differences to wild type Saccharomyces cerevisiae
2.7.2.4 H497A kcat is decreased 6.7fold for both substrates Saccharomyces cerevisiae
2.7.2.4 K18A Km values for both substrates similar to wild type Saccharomyces cerevisiae
2.7.2.4 K18Q Km values for both substrates similar to wild type Saccharomyces cerevisiae
2.7.2.4 K18R Km values for aspartate similar to wildtype, Km value for ATP 2.9fold decreased Saccharomyces cerevisiae
2.7.2.4 R419A 10fold decrease in kcat for aspartate and 8.9fold decrease in kcat for ATP Saccharomyces cerevisiae
2.7.2.4 S23A differs significantly only in the kcat/Km ratio, which is decreased 4fold for aspartate and 3.7fold for ATP Saccharomyces cerevisiae
2.7.2.4 T22A Km for ATP increases 4.2fold Saccharomyces cerevisiae
2.7.2.4 T295V 6.7 times decrease in the kcat/Km ratio for ATP Saccharomyces cerevisiae

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-threonine
-
 Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.4 0.26
-
 ATP mutant K18R Saccharomyces cerevisiae
2.7.2.4 0.61
-
 ATP mutant K18Q Saccharomyces cerevisiae
2.7.2.4 0.7
-
 ATP mutant E254A Saccharomyces cerevisiae
2.7.2.4 0.74
-
 ATP wild type Saccharomyces cerevisiae
2.7.2.4 0.89
-
 ATP mutant K18A Saccharomyces cerevisiae
2.7.2.4 1.05
-
 ATP mutant S23A Saccharomyces cerevisiae
2.7.2.4 1.15
-
 ATP mutant E279A Saccharomyces cerevisiae
2.7.2.4 1.26
-
 ATP mutant H497A Saccharomyces cerevisiae
2.7.2.4 1.45
-
 ATP mutant H292Q Saccharomyces cerevisiae
2.7.2.4 1.63
-
 L-aspartate mutant K18R Saccharomyces cerevisiae
2.7.2.4 2.33
-
 L-aspartate mutant E279A Saccharomyces cerevisiae
2.7.2.4 2.35
-
 ATP mutant T295V Saccharomyces cerevisiae
2.7.2.4 2.4
-
 ATP mutant R419A Saccharomyces cerevisiae
2.7.2.4 3.1
-
 ATP mutant T22A Saccharomyces cerevisiae
2.7.2.4 3.19
-
 L-aspartate mutant T295V Saccharomyces cerevisiae
2.7.2.4 3.21
-
 L-aspartate mutant K18A Saccharomyces cerevisiae
2.7.2.4 3.25
-
 L-aspartate mutant R419A Saccharomyces cerevisiae
2.7.2.4 3.36
-
 ATP mutant H292A Saccharomyces cerevisiae
2.7.2.4 4.25
-
 L-aspartate mutant K18Q Saccharomyces cerevisiae
2.7.2.4 4.59
-
 L-aspartate wild type Saccharomyces cerevisiae
2.7.2.4 6.81
-
 L-aspartate mutant H292A Saccharomyces cerevisiae
2.7.2.4 6.99
-
 L-aspartate mutant S23A Saccharomyces cerevisiae
2.7.2.4 7.08
-
 L-aspartate mutant T22A Saccharomyces cerevisiae
2.7.2.4 8.66
-
 L-aspartate mutant H497A Saccharomyces cerevisiae
2.7.2.4 9.77
-
 L-aspartate mutant E254A Saccharomyces cerevisiae
2.7.2.4 11.9
-
 L-aspartate mutant H292Q Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.2.4 ATP + L-aspartate Saccharomyces cerevisiae
-
 ADP + phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Saccharomyces cerevisiae
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4 recombinant enzyme from E. coli Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
 Saccharomyces cerevisiae ADP + phospho-L-aspartate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 AK
-
 Saccharomyces cerevisiae
2.7.2.4 aspartate kinase
-
 Saccharomyces cerevisiae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.2.4 0.3
-
 L-aspartate mutant K18R Saccharomyces cerevisiae
2.7.2.4 0.31
-
 ATP mutant K18R Saccharomyces cerevisiae
2.7.2.4 0.41
-
 ATP mutant H292A Saccharomyces cerevisiae
2.7.2.4 0.41
-
 L-aspartate mutant K18A Saccharomyces cerevisiae
2.7.2.4 0.53
-
 ATP mutant K18A Saccharomyces cerevisiae
2.7.2.4 0.54
-
 L-aspartate mutant K18Q Saccharomyces cerevisiae
2.7.2.4 0.6
-
 ATP mutant K18Q Saccharomyces cerevisiae
2.7.2.4 0.98
-
 L-aspartate mutant E279A Saccharomyces cerevisiae
2.7.2.4 1.13
-
 ATP mutant E279A Saccharomyces cerevisiae
2.7.2.4 2.49
-
 L-aspartate mutant H292A Saccharomyces cerevisiae
2.7.2.4 4.43
-
 ATP mutant E254A Saccharomyces cerevisiae
2.7.2.4 4.65
-
 L-aspartate mutant R419A Saccharomyces cerevisiae
2.7.2.4 5.14
-
 L-aspartate mutant E254A Saccharomyces cerevisiae
2.7.2.4 5.55
-
 ATP mutant R419A Saccharomyces cerevisiae
2.7.2.4 6.92
-
 L-aspartate mutant H497A Saccharomyces cerevisiae
2.7.2.4 7.33
-
 ATP mutant H497A Saccharomyces cerevisiae
2.7.2.4 8.3
-
 ATP mutant H292Q Saccharomyces cerevisiae
2.7.2.4 10.3
-
 L-aspartate mutant H292Q Saccharomyces cerevisiae
2.7.2.4 17.9
-
 L-aspartate mutant S23A Saccharomyces cerevisiae
2.7.2.4 18
-
 L-aspartate mutant T295V Saccharomyces cerevisiae
2.7.2.4 19.1
-
 ATP mutant S23A Saccharomyces cerevisiae
2.7.2.4 23.3
-
 ATP mutant T295V Saccharomyces cerevisiae
2.7.2.4 45
-
 L-aspartate mutant T22A Saccharomyces cerevisiae
2.7.2.4 46.6
-
 L-aspartate wild type Saccharomyces cerevisiae
2.7.2.4 49.3
-
 ATP wild type Saccharomyces cerevisiae
2.7.2.4 56.9
-
 ATP mutant T22A Saccharomyces cerevisiae

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.7.2.4 1.9
-
 L-threonine wild type, with aspartate as substrate Saccharomyces cerevisiae
2.7.2.4 3.4
-
 L-threonine wild type, with ATP as substrate Saccharomyces cerevisiae
2.7.2.4 14
-
 L-threonine mutant E279A, with aspartate as substrate Saccharomyces cerevisiae
2.7.2.4 28
-
 L-threonine mutant E279A, with ATP as substrate Saccharomyces cerevisiae