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Literature summary for 6.3.1.20 extracted from

  • Fujiwara, K.; Maita, N.; Hosaka, H.; Okamura-Ikeda, K.; Nakagawa, A.; Taniguchi, H.
    Global conformational change associated with the two-step reaction catalyzed by Escherichia coli lipoate-protein ligase A (2010), J. Biol. Chem., 285, 9971-9980.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.3.1.20

Protein Variants

Protein Variants Comment Organism
D122A D122A mutation results in a marked reduction in the overall, lipoate adenylation, and lipoate transfer reaction activities (0.14, 4, and 4% of those of wild type, respectively) Escherichia coli
H149A mutations does not cause a significant reduction in three reaction activities (overall, lipoate adenylation, and lipoate transfer reaction activities), Km value for ATP and lipoic acid increases to 15 and 5.8fold, respectively, relative to those of wild-type Escherichia coli
K133A K133A mutation almost completely abolishes the overall reaction activity (0.01% of that of wild type) and causes marked reduction in lipoate adenylation and lipoate transfer activities (0.2 and 2.5% of that of wild type, respectively) Escherichia coli
N121A N121A affects only the lipoate adenylation activity and consequently the overall reaction activity (1.4 and 0.19% of those of wild-type, respectively) but retains a significant lipoate transfer activity (24.2%) Escherichia coli
S72A mutations does not cause a significant reduction in three reaction activities (overall, lipoate adenylation, and lipoate transfer reaction activities), Km value for ATP and lipoic acid increases to 28 and 2.3fold, respectively, relative to those of wild-type Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P32099
-
-

Reaction

Reaction Comment Organism Reaction ID
ATP + (R)-lipoate + a [lipoyl-carrier protein]-L-lysine = a [lipoyl-carrier protein]-N6-(lipoyl)lysine + AMP + diphosphate LplA structures are determined: LplA/lipoyl-AMP binary complex and LplA/octyl-5'-AMP/apoH-protein ternary complex. These structures represent a post-lipoate adenylation stage and a pre-lipoate transfer stage, respectively. Three large scale conformational changes in the Escherichia coli LplA structure upon completion of the lipoate adenylation reaction are found, which enable LplA to accommodate apoprotein for the second reaction Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + D-lipoic acid
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 Escherichia coli diphosphate + D-lipoyl-AMP
-
 ?

Synonyms

Synonyms Comment Organism
LPLA
-
 Escherichia coli

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
-
-
 assay at Escherichia coli

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Escherichia coli