Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

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 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.2.4 5.16
-
 ATP mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense
2.7.2.4 5.77
-
 L-aspartate mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense
2.7.2.4 6.18
-
 L-aspartate wild type enzyme, at pH 7.4 and 28°C Corynebacterium pekinense
2.7.2.4 7.93
-
 ATP wild type enzyme, at pH 7.4 and 28°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
-
 ?
2.7.2.4 ATP + L-aspartate Corynebacterium pekinense ATCC 13032
-
 ADP + 4-phospho-L-aspartate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.2.4 Corynebacterium pekinense
-
-
-
2.7.2.4 Corynebacterium pekinense ATCC 13032
-
-
-

Purification (Commentary)

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

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 28
-
-
 Corynebacterium pekinense

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.7.2.4 26 30 more than 50% activity between 26 and 30°C Corynebacterium pekinense

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.2.4 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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.2.4 7.5
-
-
 Corynebacterium pekinense

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.2.4 2.01
-
 L-aspartate wild type enzyme, at pH 7.4 and 28°C Corynebacterium pekinense
2.7.2.4 14.96
-
 ATP wild type enzyme, at pH 7.4 and 28°C Corynebacterium pekinense
2.7.2.4 17.28
-
 ATP mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense
2.7.2.4 33.19
-
 L-aspartate mutant enzyme M372I/T379W, at pH 7.4 and 28°C Corynebacterium pekinense