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Literature summary extracted from

  • Han, C.; Liu, S.; Liu, C.; Xie, X.; Fang, L.; Min, W.
    The mutant T379L of novel aspartokinase from Corynebacterium pekinense A combined experimental and molecular dynamics simulation study (2019), Process Biochem., 83, 77-85 .
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.2.4 expressed in Escherichia coli BL21 cells Corynebacterium pekinense

Protein Variants

EC Number Protein Variants Comment Organism
2.7.2.4 T379 F the mutant shows 2.65fold higher enzymatic activity compared to the wild type enzyme Corynebacterium pekinense
2.7.2.4 T379E the mutant shows 4.66fold higher enzymatic activity compared to the wild type enzyme Corynebacterium pekinense
2.7.2.4 T379K the mutant shows 5.25fold higher enzymatic activity compared to the wild type enzyme Corynebacterium pekinense
2.7.2.4 T379L the mutant shows 9.16fold higher enzymatic activity compared to the wild type enzyme Corynebacterium pekinense

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.2.4 L-lysine 85.43% residual activity at 10 mM. The inhibition rate for the single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met) Corynebacterium pekinense
2.7.2.4 L-methionine 73.72% residual activity at 10 mM. The inhibition rate for a single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met) Corynebacterium pekinense
2.7.2.4 L-threonine 89.37% residual activity at 5 mM. The inhibition rate for a single inhibitor is about 10%, this rate is further increased to 65% under the combined action of two inhibitors (Lys+Thr, Lys+Met, and Thr+Met) Corynebacterium pekinense

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.4 3.67
-
 L-aspartate mutant enzyme T379L, at pH 8.0 and 26°C Corynebacterium pekinense
2.7.2.4 4.17
-
 L-aspartate wild type enzyme, at pH 8.0 and 26°C Corynebacterium pekinense

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.2.4 Mg2+ 1.6 mM used in assay conditions Corynebacterium pekinense

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 Corynebacterium pekinense
-
 ADP + 4-phospho-L-aspartate
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Corynebacterium pekinense
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.2.4 Ni Sepharose column chromatography Corynebacterium pekinense

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.2.4 ATP + L-aspartate
-
 Corynebacterium pekinense ADP + 4-phospho-L-aspartate
-
 ir

Subunits

EC Number Subunits Comment Organism
2.7.2.4 monomer 1 * 48000, SDS-PAGE Corynebacterium pekinense

Synonyms

EC Number Synonyms Comment Organism
2.7.2.4 aspartokinase
-
 Corynebacterium pekinense

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.2.4 26
-
-
 Corynebacterium pekinense

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.2.4 25 28 the enzyme shows more than 50% activity between 25°C and 28°C Corynebacterium pekinense

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.2.4 26
-
 the enzyme has a half-life of 4.5 h at 26°C Corynebacterium pekinense

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 8
-
-
 Corynebacterium pekinense

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.2.4 7 9 the enzyme shows more than 60% activity between pH 7.0 and 9.0 Corynebacterium pekinense