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Literature summary extracted from

  • Segall, M.L.; Cashman, M.A.; Colman, R.F.
    Important roles of hydroxylic amino acid residues in the function of Bacillus subtilis adenylosuccinate lyase (2007), Protein Sci., 16, 441-448.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

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

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.2 S306A conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function Bacillus subtilis
4.3.2.2 S94A conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function Bacillus subtilis
4.3.2.2 T140A conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function Bacillus subtilis
4.3.2.2 T93A conserved amino acid in all adenylosuccinate lyases, mutant for testing the involvement of the residue in the enzyme function Bacillus subtilis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.3.2.2 0.00177
-
 adenylosuccinate wild-type enzyme Bacillus subtilis
4.3.2.2 0.00224
-
 adenylosuccinate mutant S94A Bacillus subtilis
4.3.2.2 0.0128
-
 adenylosuccinate mutant S306A Bacillus subtilis
4.3.2.2 0.0177
-
 adenylosuccinate mutant T93A Bacillus subtilis
4.3.2.2 0.0192
-
 adenylosuccinate mutant T140A Bacillus subtilis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.3.2.2 193000
-
 determined by native polyacrylamide gel electrophoresis, mutant S93A Bacillus subtilis
4.3.2.2 194000
-
 determined by native polyacrylamide gel electrophoresis, mutant T93A Bacillus subtilis
4.3.2.2 194800
-
 determined by analytical ultracentrifugation, mutant T140A Bacillus subtilis
4.3.2.2 196000
-
 determined by native polyacrylamide gel electrophoresis, wild-type enzyme Bacillus subtilis
4.3.2.2 199700
-
 determined by analytical ultracentrifugation, wild-type enzyme Bacillus subtilis
4.3.2.2 216400
-
 determined by analytical ultracentrifugation, mutant S306A 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 affinity chromatography 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 additional information
-
 complementation of inactive mutant ASLs, maximum specific activity, T140A + H141Q, T93A + H68Q, S306A + H68Q 0% wild-type activity Bacillus subtilis
4.3.2.2 0.068
-
 complementation of inactive mutant ASLs, maximum specific activity, T93A + H141Q, 3.0% wild-type activity Bacillus subtilis
4.3.2.2 0.096
-
 complementation of inactive mutant ASLs, maximum specific activity, S306A + H141Q, 4.6% wild-type activity Bacillus subtilis
4.3.2.2 0.21
-
 complementation of inactive mutant ASLs, maximum specific activity, T93A + K268Q, 10.1% wild-type activity Bacillus subtilis
4.3.2.2 0.24
-
 complementation of inactive mutant ASLs, maximum specific activity, T140A + H68Q, 11.5% wild-type activity Bacillus subtilis
4.3.2.2 0.32
-
 complementation of inactive mutant ASLs, maximum specific activity, S306A + K268Q, 15.4% wild-type activity Bacillus subtilis
4.3.2.2 0.32
-
 complementation of inactive mutant ASLs, maximum specific activity, T140A + K268Q, 15.4% wild-type activity 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

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.3.2.2 0.00048
-
 adenylosuccinate mutant T140A Bacillus subtilis
4.3.2.2 0.00689
-
 adenylosuccinate mutant S306A Bacillus subtilis
4.3.2.2 0.01
-
 adenylosuccinate mutant T93A Bacillus subtilis
4.3.2.2 1.14
-
 adenylosuccinate mutant S94A Bacillus subtilis
4.3.2.2 1.74
-
 adenylosuccinate wild-type enzyme Bacillus subtilis

pH Optimum

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