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Literature summary extracted from

  • Wang, X.; Lopez-Valenzuela, J.A.; Gibbon, B.C.; Gakiere, B.; Galili, G.; Larkins, B.A.
    Characterization of monofunctional aspartate kinase genes in maize and their relationship with free amino acid content in the endosperm (2007), J. Exp. Bot., 58, 2653-2660.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.2.4 additional information ASK1 and ASK2 share a high degree of identity with each other, there is one amino acid difference in the Ask2 enzymes of Oh545o2 and Oh51Ao2 Zea mays

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.4 the monofunctional AK, Ask1 and Ask2 coding sequences are cloned using RNA from the B73 inbred, the two maize genes share a high degree of identity with each other and similar genes of other species, Ask2-Oh545o2 and Ask2-Oh51Ao2 sequences are expressed in Saccharomyces cerevisiae hom3/ura3 mutant sigma a3hu, there is one amino acid difference between the Ask2 alleles, Ask2-Oh545o2 and Ask2-Oh51Ao2 have similar lysine-sensitivity properties but differ in basal activity, the Ask2 gene is tightly linked to the QTL on chromosome 2 that is associated with a high endosperm lysine content. There is one amino acid difference in the Ask2 enzymes of Oh545o2 and Oh51Ao2. Zea mays
2.7.2.4 yeast hom3/ura3 mutant sigmaa3hu was transformed with plasmids expressing the maize Ask2-Oh545o2 and Ask2-Oh51Ao2 sequences Zea mays

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 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 Zea mays

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 Zea mays
-
ADP + 4-phospho-L-aspartate
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Zea mays
-
-
-
2.7.2.4 Zea mays B0L9J2 expression in Saccharomyces cerevisiae sigma a3hu
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.2.4 endosperm
-
Zea mays
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
Zea mays ADP + 4-phospho-L-aspartate
-
?

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 ASK1
-
Zea mays
2.7.2.4 ASK2
-
Zea mays
2.7.2.4 aspartate kinase
-
Zea mays

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.7.2.4 0.08
-
Ask2-Oh545o2 and Ask2-Oh51Ao2 Zea mays L-lysine
2.7.2.4 0.08
-
extract of transformed yeast hom3 cells by Ask2-Oh545o2 and Ask2-Oh51Ao2 Zea mays L-lysine