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Literature summary extracted from

  • Sivendran, S.; Segall, M.L.; Rancy, P.C.; Colman, R.F.
    Effect of Asp69 and Arg310 on the pK of His68, a key catalytic residue of adenylosuccinate lyase (2007), Protein Sci., 16, 1700-1707.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.2.2 for expression in Escherichia coli BL21DE3 cells Bacillus subtilis

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.2 D69E mutant exibits an increase in its pK2 Bacillus subtilis
4.3.2.2 D69N mutant exibits a decrease in its pK2 Bacillus subtilis
4.3.2.2 R310K mutant shows little change in pK2 Bacillus subtilis
4.3.2.2 R310Q mutant exibits a decrease in its pK2 Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.2.2 0.0015
-
 adenylosuccinate mutant D69E Bacillus subtilis
4.3.2.2 0.0021
-
 adenylosuccinate wild-type enzyme Bacillus subtilis
4.3.2.2 0.0071
-
 adenylosuccinate mutant R310K Bacillus subtilis
4.3.2.2 0.0093
-
 adenylosuccinate mutant D69N Bacillus subtilis
4.3.2.2 0.023
-
 adenylosuccinate mutant R310Q Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.2.2 147000
-
 determined by native polyacrylamide gel electrophoresis, wild-type enzyme Bacillus subtilis
4.3.2.2 148000
-
 determined by native polyacrylamide gel electrophoresis, mutant R310K Bacillus subtilis
4.3.2.2 176000
-
 determined by light scattering, mutant D69N Bacillus subtilis
4.3.2.2 182000
-
 determined by light scattering, mutant R310K Bacillus subtilis
4.3.2.2 191000
-
 determined by light scattering, wild-type enzyme Bacillus subtilis
4.3.2.2 194000
-
 determined by light scattering, mutant D69E Bacillus subtilis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.3.2.2 (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate Bacillus subtilis
-
 fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 ?
4.3.2.2 N6-(1,2-dicarboxyethyl)AMP Bacillus subtilis
-
 fumarate + AMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.2 Bacillus subtilis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.2.2 using nickel nitrilotriacetic acid-agarose Bacillus subtilis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.3.2.2 0.000083
-
 mutant R310Q, pH 7.0 Bacillus subtilis
4.3.2.2 0.04
-
 mutant D69N, pH 7.0 Bacillus subtilis
4.3.2.2 0.1
-
 mutant R310K, pH 7.0 Bacillus subtilis
4.3.2.2 0.4
-
 mutant D69E, pH 7.0 Bacillus subtilis
4.3.2.2 1.75
-
 wild-type enzyme, pH 7.0 Bacillus subtilis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.3.2.2 (S)-2-[5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido]succinate
-
 Bacillus subtilis fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 ?
4.3.2.2 5-aminoimidazole-(N-succinylocarboxamide) ribotide
-
 Bacillus subtilis 5-aminoimidazole-4-carboxamide ribotide + fumarate
-
 ?
4.3.2.2 adenylosuccinate
-
 Bacillus subtilis AMP + fumarate
-
 ?
4.3.2.2 N6-(1,2-dicarboxyethyl)AMP
-
 Bacillus subtilis fumarate + AMP
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.3.2.2 adenylosuccinate lyase
-
 Bacillus subtilis
4.3.2.2 ASL
-
 Bacillus subtilis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.3.2.2 25
-
 activity assay Bacillus subtilis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.2.2 7
-
 activity assay Bacillus subtilis