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Literature summary extracted from

  • Tsai, M.; Koo, J.; Yip, P.; Colman, R.F.; Segall, M.L.; Howell, P.L.
    Substrate and product complexes of Escherichia coli adenylosuccinate lyase provide new insights into the enzymatic mechanism (2007), J. Mol. Biol., 370, 541-554.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.3.2.2 subcloned from the pUC118 into the pET28a vector for expression in Escherichia coli B834DE3 cells Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
4.3.2.2 the crystal structures of wild-type ADL, and mutant-substrate, H171A-ADS, and -product, H171N-AMP-FUM, complexes are determined to 2.0, 1.85, and 2.0 A resolution, respectively Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.3.2.2 H171A mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups Escherichia coli
4.3.2.2 H171N mutant to map out the residues involved in adenylosuccinate binding, and to identify the putative catalytic groups Escherichia coli
4.3.2.2 S295A mutant to probe the role of S295 in the catalytic mechanism Escherichia coli

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 Escherichia coli
-
 fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 ?
4.3.2.2 N6-(1,2-dicarboxyethyl)AMP Escherichia coli
-
 fumarate + AMP
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.3.2.2 Escherichia coli P0AB89
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.3.2.2 using a Ni-NTA column Escherichia coli

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 0.004
-
 mutant S295A, pH 7.0 Escherichia coli
4.3.2.2 0.008
-
 mutant H171N, pH 7.0 Escherichia coli
4.3.2.2 0.009
-
 mutant H171A, pH 7.0 Escherichia coli
4.3.2.2 0.031
-
 mutant H171A, pH 8.5 Escherichia coli
4.3.2.2 0.04
-
 mutant H171N, pH 8.5 Escherichia coli
4.3.2.2 4.65
-
 wild-type protein, pH 7.0 Escherichia coli
4.3.2.2 16.47
-
 wild-type protein, pH 8.5 Escherichia coli

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
-
 Escherichia coli fumarate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide
-
 ?
4.3.2.2 5-aminoimidazole-(N-succinylocarboxamide) ribotide
-
 Escherichia coli 5-aminoimidazole-4-carboxamide ribotide + fumarate
-
 ?
4.3.2.2 adenylosuccinate
-
 Escherichia coli AMP + fumarate
-
 ?
4.3.2.2 N6-(1,2-dicarboxyethyl)AMP
-
 Escherichia coli fumarate + AMP
-
 ?

Subunits

EC Number Subunits Comment Organism
4.3.2.2 homotetramer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.3.2.2 adenylosuccinate lyase
-
 Escherichia coli
4.3.2.2 ADL
-
 Escherichia coli

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.3.2.2 7
-
 activity assay Escherichia coli
4.3.2.2 8.5
-
 activity assay Escherichia coli