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Literature summary for 6.3.1.20 extracted from

  • Puthenveetil, S.; Liu, D.S.; White, K.A.; Thompson, S.; Ting, A.Y.
    Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase (2009), J. Am. Chem. Soc., 131, 16430-16438.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.2
-
LplA acceptor peptide 1
-
Escherichia coli
13.32
-
LplA acceptor peptide 2
-
Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + lipoate + H-protein Escherichia coli
-
AMP + diphosphate + ?
-
?
additional information Escherichia coli LplA's natural protein substrates have a conserved beta-hairpin structure ?
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + lipoate + biotin
-
Escherichia coli AMP + diphosphate + ?
-
?
ATP + lipoate + H-protein
-
Escherichia coli AMP + diphosphate + ?
-
?
ATP + lipoate + LplA acceptor peptide 1
-
Escherichia coli ?
-
?
ATP + lipoate + LplA acceptor peptide 2
-
Escherichia coli ?
-
?
additional information LplA's natural protein substrates have a conserved beta-hairpin structure Escherichia coli ?
-
?

Synonyms

Synonyms Comment Organism
lipoic acid ligase
-
Escherichia coli
LPLA
-
Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.22
-
LplA acceptor peptide 2
-
Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
0.0000165
-
LplA acceptor peptide 2
-
Escherichia coli