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Literature summary for 2.7.2.4 extracted from

  • Kochhar, S.; Kochhar, V.K.; Sane, P.V.
    Isolation, characterization and regulation of isoenzymes of aspartate kinase differentially sensitive to calmodulin from spinach leaves (1986), Biochim. Biophys. Acta, 880, 220-225.
No PubMed abstract available
Search for more literature for 2.7.2.4

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin isoenzyme II Spinacia oleracea

Inhibitors

Inhibitors Comment Organism Structure
EGTA isoenzyme II Spinacia oleracea
L-lysine isoenzyme I Spinacia oleracea
L-threonine isoenzyme II Spinacia oleracea

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1
-
 ATP pH 7.5, isoenzyme I Spinacia oleracea
1.67
-
 ATP pH 7.5, isoenzyme II Spinacia oleracea
2
-
 L-aspartate pH 7.5, isoenzyme I and II Spinacia oleracea

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ isoenzyme I is insensitive to Ca2+ and calmodulin, isoenzyme II is activated by calmodulin, the effect is further increased by Ca2+ Spinacia oleracea

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
200000
-
 isoenzyme II, gel filtration Spinacia oleracea
330000
-
 isoenzyme I, gel filtration Spinacia oleracea

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate Spinacia oleracea
-
 ADP + 4-phospho-L-aspartate
-
 r

Organism

Organism UniProt Comment Textmining
Spinacia oleracea
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
leaf
-
 Spinacia oleracea
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
 Spinacia oleracea ADP + 4-phospho-L-aspartate
-
 r