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Literature summary for 6.2.1.3 extracted from

  • Weimar, J.D.; DiRusso, C.C.; Delio, R.; Black, P.N.
    Functional role of fatty acyl-coenzyme A synthetase in the transmembrane movement and activation of exogenous long-chain fatty acids: Amino acid residues within the ATP/AMP signature motif of Escherichia coli FadD are required for enzyme activity and fatty acid transport (2002), J. Biol. Chem., 277, 29369-29376.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Protein Variants

Protein Variants Comment Organism
E361A inactive mutant enzyme Escherichia coli
G216A the ratio of turnover number to Km-value for the reaction with oleate is 32.7% of the wild-type ratio Escherichia coli
G219A the ratio of turnover number to Km-value for the reaction with oleate is 1.3fold higher than the wild-type ratio Escherichia coli
K222A the ratio of turnover number to Km-value for the reaction with oleate is 8% of the wild-type ratio Escherichia coli
T214A the ratio of turnover number to Km-value for the reaction with oleate is 10.3% of the wild-type ratio Escherichia coli
T217A the ratio of turnover number to Km-value for the reaction with oleate is 6.7% of the wild-type ratio Escherichia coli
Y213A inactive mutant enzyme Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.06
-
ATP pH 7.5, 37°C, mutant enzyme G219A Escherichia coli
0.11
-
ATP pH 7.5, 37°C, mutant enzyme G216A Escherichia coli
0.13
-
ATP pH 7.5, 37°C, wild-type enzyme Escherichia coli
0.13
-
ATP pH 7.5, 37°C, mutant enzyme T214A Escherichia coli
0.44
-
ATP pH 7.5, 37°C, mutant enzyme K222A Escherichia coli
0.53
-
ATP pH 7.5, 37°C, mutant enzyme T217A Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli the enzyme plays a central role in intermediary metabolism by catalyzing the formation of acyl-CoA. The enzyme functions in the vectorial movement of exogenous fatty acids across the plasma membrane by acting as a metabolic trap, which results in the formation of acyl-CoA esters ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + decanoate + CoA
-
Escherichia coli AMP + diphosphate + decanoyl-CoA
-
?
ATP + oleate + CoA
-
Escherichia coli AMP + diphosphate + oleoyl-CoA
-
?
additional information the enzyme plays a central role in intermediary metabolism by catalyzing the formation of acyl-CoA. The enzyme functions in the vectorial movement of exogenous fatty acids across the plasma membrane by acting as a metabolic trap, which results in the formation of acyl-CoA esters Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
FACS
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.003
-
ATP pH 7.5, 37°C, mutant enzyme T214A Escherichia coli
0.008
-
ATP pH 7.5, 37°C, mutant enzyme G216A Escherichia coli
0.008
-
ATP pH 7.5, 37°C, mutant enzyme K222A Escherichia coli
0.008
-
ATP pH 7.5, 37°C, mutant enzyme T217A Escherichia coli
0.017
-
ATP pH 7.5, 37°C, mutant enzyme G219A Escherichia coli
0.029
-
ATP pH 7.5, 37°C, wild-type enzyme Escherichia coli