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Literature summary for 2.7.2.4 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
Search for more literature for 2.7.2.4

Cloned(Commentary)

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

Protein Variants

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

Inhibitors

Inhibitors Comment Organism Structure
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
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
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]

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

Metals/Ions

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-aspartate Corynebacterium pekinense
-
 ADP + 4-phospho-L-aspartate
-
 ir

Organism

Organism UniProt Comment Textmining
Corynebacterium pekinense
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni Sepharose column chromatography Corynebacterium pekinense

Substrates and Products (Substrate)

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

Subunits

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

Synonyms

Synonyms Comment Organism
aspartokinase
-
 Corynebacterium pekinense

Temperature Optimum [°C]

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

Temperature Range [°C]

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

Temperature Stability [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
-
 Corynebacterium pekinense

pH Range

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