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Literature summary for 2.7.2.4 extracted from

  • Gao, Y.; Han, C.; Liu, C.; Wang, J.; Zhao, L.; Fang, L.; Min, W.
    Enzymatic characterization and molecular mechanism of a novel aspartokinase mutant M372I/T379W from Corynebacterium pekinense (2019), RSC Adv., 9, 21344-21354 .
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
M372I/T379W the mutant shows 16.51fold higher activity, weakened inhibitory effect of L-lysine and significantly improved thermostability as compared to the wild type enzyme Corynebacterium pekinense

Inhibitors

Inhibitors Comment Organism Structure
L-lysine 40.72% residual activity at 10 mM Corynebacterium pekinense
L-threonine 61.33% residual activity at 10 mM Corynebacterium pekinense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.16
-
 ATP mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense
5.77
-
 L-aspartate mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense
6.18
-
 L-aspartate wild type enzyme, at pH 7.4 and 28°C Corynebacterium pekinense
7.93
-
 ATP wild type enzyme, at pH 7.4 and 28°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
-
 ?
ATP + L-aspartate Corynebacterium pekinense ATCC 13032
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

Organism UniProt Comment Textmining
Corynebacterium pekinense
-
-
-
Corynebacterium pekinense ATCC 13032
-
-
-

Purification (Commentary)

Purification (Comment) Organism
nickel ion affinity 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
-
 ?
ATP + L-aspartate
-
 Corynebacterium pekinense ATCC 13032 ADP + 4-phospho-L-aspartate
-
 ?

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
28
-
-
 Corynebacterium pekinense

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
26 30 more than 50% activity between 26 and 30°C Corynebacterium pekinense

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
28 40 the half-life of the wild type enzyme at 28°C and 30°C is 3.8 h and 2.5 h, respectively. The wild type enzyme is almost inactive after 4 h at 35°C and 40°C Corynebacterium pekinense

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
-
 Corynebacterium pekinense

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.01
-
 L-aspartate wild type enzyme, at pH 7.4 and 28°C Corynebacterium pekinense
14.96
-
 ATP wild type enzyme, at pH 7.4 and 28°C Corynebacterium pekinense
17.28
-
 ATP mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense
33.19
-
 L-aspartate mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense