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Literature summary extracted from

  • Wu, R.; Cao, J.; Lu, X.; Reger, A.S.; Gulick, A.M.; Dunaway-Mariano, D.
    Mechanism of 4-chlorobenzoate:coenzyme A ligase catalysis (2008), Biochemistry, 47, 8026-8039.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
6.2.1.33 DNA sequence determination, expression of the His-tagged enzyme in Escherichia coli strain JM109 Alcaligenes sp.

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
6.2.1.33 purified recombinant enzyme, X-ray diffraction structure determination and analysis, modelling Alcaligenes sp.

Protein Variants

EC Number Protein Variants Comment Organism
6.2.1.33 D385A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 E410A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 F473A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat Alcaligenes sp.
6.2.1.33 G408A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 H207A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 H207F site-directed mutagenesis,the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 H207Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 H254A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 K477A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 K492A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 K492L site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 K492R site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 M203A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 N302A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 R400A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 R439A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 R475A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 R87A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 S407A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 T161A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 T251A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 T306A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 T307A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.
6.2.1.33 W440A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme, but increased kcat Alcaligenes sp.
6.2.1.33 Y304F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Alcaligenes sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.2.1.33 4-chlorophenacyl-CoA a product analogue, noncompetitive versus 4-methylbenzoate and ATP, dead-end inhibitor Alcaligenes sp.
6.2.1.33 AMP is a noncompetitive inhibitor versus ATP and an uncompetitive versus CoA Alcaligenes sp.
6.2.1.33 diphosphate competitive versus ATP Alcaligenes sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.33 additional information
-
 additional information transient-state and steady-state kinetics of wild-type and mutant enzymes, overview Alcaligenes sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
6.2.1.33 Mg2+
-
 Alcaligenes sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
6.2.1.33 4-Chlorobenzoate + CoA + ATP Alcaligenes sp.
-
 4-Chlorobenzoyl-CoA + AMP + diphosphate
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.33 Alcaligenes sp. Q8GN86
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
6.2.1.33 recombinant His-tagged enzyme from Escherichia coli strain JM109 by nickel affinity chromatography Alcaligenes sp.

Reaction

EC Number Reaction Comment Organism Reaction ID
6.2.1.33 4-Chlorobenzoate + CoA + ATP = 4-chlorobenzoyl-CoA + AMP + diphosphate kinetic reaction mechanism, overview Alcaligenes sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.33 4-Chlorobenzoate + CoA + ATP
-
 Alcaligenes sp. 4-Chlorobenzoyl-CoA + AMP + diphosphate
-
 ?
6.2.1.33 4-Chlorobenzoate + CoA + ATP the rate-limiting step in CBL catalysis follows the formation of 4-chlorobenzoate-CoA Alcaligenes sp. 4-Chlorobenzoyl-CoA + AMP + diphosphate
-
 ?
6.2.1.33 4-Methylbenzoate + CoA + ATP
-
 Alcaligenes sp. 4-Methylbenzoyl-CoA + AMP + diphosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
6.2.1.33 More domain and active site structure, overview Alcaligenes sp.

Synonyms

EC Number Synonyms Comment Organism
6.2.1.33 4-Chlorobenzoate:coenzyme A ligase
-
 Alcaligenes sp.
6.2.1.33 CBL
-
 Alcaligenes sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
6.2.1.33 25
-
 assay at Alcaligenes sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2.1.33 7.5
-
 assay at Alcaligenes sp.

Cofactor

EC Number Cofactor Comment Organism Structure
6.2.1.33 ATP
-
 Alcaligenes sp.

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
6.2.1.33 additional information
-
 additional information inhibition kinetics, overview Alcaligenes sp.