4.3.2.2: adenylosuccinate lyase
This is an abbreviated version!
For detailed information about adenylosuccinate lyase, go to the full flat file.
Word Map on EC 4.3.2.2
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4.3.2.2
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purine
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saicar
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succinyladenosine
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autistic
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carboxamide
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psychomotor
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imp
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succinylaminoimidazole
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amylosucrase
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ribotide
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geothermalis
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aminoimidazole
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drug development
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medicine
- 4.3.2.2
- purine
-
saicar
-
succinyladenosine
-
autistic
- carboxamide
-
psychomotor
- imp
-
succinylaminoimidazole
- amylosucrase
- ribotide
- geothermalis
-
aminoimidazole
- drug development
- medicine
Reaction
Synonyms
adenylosuccinase, adenylosuccinate lyase, ADL, ADSL, AMPS lyase, ASASE, ASL, Glutamyl-tRNA synthetase regulatory factor, lyase, adenylosuccinate, PurB, succino AMP-lyase, succino-AMP lyase
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KM Value
KM Value on EC 4.3.2.2 - adenylosuccinate lyase
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0.0111
(S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
pH 7.5, 25°C
0.0003
pH 7.0, 25°C, mutant S290A
0.0016
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
pH 7.0, 25°C, wild-type enzyme
0.0029
5-aminoimidazole-4-(N-succinylcarboxamide) ribonucleotide
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pH 7.0, 25°C, wild-type enzyme
0.0007
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recombinant His-tagged mutant R426H, pH 7.4, 25°C
0.00174
phosphoribosylsuccinyl-aminoimidazole carboxamide
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recombinant His-tagged wild-type enzyme, pH 7.4, 25°C
0.009
phosphoribosylsuccinyl-aminoimidazole carboxamide
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recombinant His-tagged mutant R303C, pH 7.4, 25°C
0.0014
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recombinant His-tagged mutant R426H, pH 7.4, 25°C
0.0021
succinyladenosine monophosphate
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recombinant His-tagged wild-type enzyme, pH 7.4, 25°C
0.0027
succinyladenosine monophosphate
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recombinant His-tagged mutant R303C, pH 7.4, 25°C
additional information
additional information
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Michaelis-Menten kinetics
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additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview
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additional information
additional information
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thermodynamics and kinetics, initial velocity and transient kinetics of succinyladenosine monophosphate cleavage, overview
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additional information
additional information
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non-linear dependence of the activities on the substrate ratios due to competitive binding. The enzyme does not follow simple Michaelis-Menten kinetics, kinetic analysis of wild-type and mutant enzymes, overview. Wild-type enzyme and mutant R426H appear to have equivalent cooperative binding on both substrates, while mutant R303C demonstrates no cooperativity
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additional information
additional information
the enzyme shows cooperativity and does not follow simple Michaelis-Menten kinetics, kinetic analysis, overview
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additional information
additional information
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the enzyme shows cooperativity and does not follow simple Michaelis-Menten kinetics, kinetic analysis, overview
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