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Literature summary for 2.7.2.4 extracted from

  • McCarron, R.M.; Chang, Y.F.
    Aspartokinase of Streptococcus mutans: purification, properties, and regulation (1978), J. Bacteriol., 134, 483-491.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
L-methionine displays slight activation Streptococcus mutans

General Stability

General Stability Organism
feedback inhibitor pair protects the enzyme against heat denaturation Streptococcus mutans

Inhibitors

Inhibitors Comment Organism Structure
L-lysine concerted feedback inhibition with L-threonine; L-threonine methyl ester and L-threonine amide are able to substitute for L-threonine in feedback inhibition, but the requirement for L-lysine is strict Streptococcus mutans

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2
-
ATP pH 8.1, 29°C Streptococcus mutans
5.5
-
L-aspartate pH 8.1, 29°C Streptococcus mutans

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
6 * 40000, SDS-PAGE Streptococcus mutans
242000
-
gel filtration Streptococcus mutans

Organism

Organism UniProt Comment Textmining
Streptococcus mutans
-
-
-
Streptococcus mutans BHT
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Streptococcus mutans

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
13.92
-
-
Streptococcus mutans

Storage Stability

Storage Stability Organism
-20°C, appears to be stable over a period of several months' storage Streptococcus mutans
4°C, during 24 h of storage the loss of enzyme activity is substantial Streptococcus mutans

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-aspartate
-
Streptococcus mutans ADP + 4-phospho-L-aspartate
-
?
ATP + L-aspartate
-
Streptococcus mutans BHT ADP + 4-phospho-L-aspartate
-
?
additional information strict requirement for ATP as a phosphorylating agent, CTP and GTP are not active Streptococcus mutans ?
-
?
additional information strict requirement for ATP as a phosphorylating agent, CTP and GTP are not active Streptococcus mutans BHT ?
-
?

Subunits

Subunits Comment Organism
hexamer 6 * 40000, SDS-PAGE Streptococcus mutans

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
-
Streptococcus mutans

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
10 35 stable in this range Streptococcus mutans
50
-
about 50% of the enzyme is inactivated after 20 min Streptococcus mutans

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.5 8.5
-
Streptococcus mutans

pH Stability

pH Stability pH Stability Maximum Comment Organism
6 9 in pH regions below 6.0 and above 9.0 the enzyme activity rapidly decreases Streptococcus mutans

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
10
-
L-lysine pH 8.1, 29°C, noncompetitive inhibition with respect to aspartate, mixed with respect to ATP Streptococcus mutans