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Literature summary for 6.1.1.6 extracted from

  • Chen, X.; Boonyalai, N.; Lau, C.; Thipayang, S.; Xu, Y.; Wright, M.; Miller, A.D.
    Multiple catalytic activities of Escherichia coli lysyl-tRNA synthetase (LysU) are dissected by site-directed mutagenesis (2013), FEBS J., 280, 102-114.
    View publication on PubMed
Search for more literature for 6.1.1.6

Protein Variants

Protein Variants Comment Organism
E246D the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
E246R the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
E264A the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
E264K the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+) Escherichia coli
E264N the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+) Escherichia coli
E264Q the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+) Escherichia coli
E273A the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
E414A the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
E421A the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
F261A the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
F274A the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
G265A the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
H270A the mutant catalyses the production of glycerol-3-phosphate, powered by ATP turnover to ADP but shows little formation of diadenosine tri- and tetraphosphates under normal conditions (additional Zn2+/L-lysine/Mg2+) Escherichia coli
I266A the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
N260A inactive Escherichia coli
N263A inactive Escherichia coli
N271A inactive Escherichia coli
P272A the mutant shows more than 90% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
R262A inactive Escherichia coli
R269A inactive Escherichia coli
R269E inactive Escherichia coli
R269K inactive Escherichia coli
R269Q inactive Escherichia coli
R480A the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
S267A the mutant shows more than 50% loss in catalytic efficiency compared to the wild type enzyme Escherichia coli
V268A inactive Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ required, the wild-type enzyme has a weaker glycerol kinase-like capability in the absence of Zn2+ and is dominated by diadenosine tri- and tetraphosphate synthesis in its presence Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + L-lysine + tRNALys Escherichia coli
-
 AMP + diphosphate + L-lysyl-tRNALys
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
ammonium sulfate precipitation, Q Sepharose column chromatography, and Sephacryl S300 gel filtration Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-lysine + tRNALys
-
 Escherichia coli AMP + diphosphate + L-lysyl-tRNALys
-
 ?
additional information the enzyme also converts ATP to diadenosine tri- and tetraphosphates in the presence of L-lysine/Mg2+/Zn2+ Escherichia coli ?
-
 ?

Synonyms

Synonyms Comment Organism
LysU
-
 Escherichia coli
Lysyl-tRNA synthetase
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli