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Literature summary extracted from

  • Black, S.
    Conversion of aspartic acid to homoserine (1962), Methods Enzymol., 5, 820-827.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Fe2+ can partially replace Mg2+, but to a smaller extent than Mn2+ Saccharomyces cerevisiae
2.7.2.4 Mg2+ essential for enzyme activity, can be partially replaced by Mn2+ and to a smaller extent by Fe2+ Saccharomyces cerevisiae
2.7.2.4 Mn2+ can partially replace Mg2+ 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 + 4-phospho-L-aspartate
-
 r

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4
-
 Saccharomyces cerevisiae

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.2.4 8.2
-
-
 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 + 4-phospho-L-aspartate
-
 r
2.7.2.4 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 Saccharomyces cerevisiae ?
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.2.4 50
-
 very heat-labile, being largely destroyed when kept for 10 min Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 5 9 no optimum point of activity in this range Saccharomyces cerevisiae